{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGI0","uniProtkbId":"PSBA_SELUN","entryAudit":{"firstPublicDate":"2008-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":84,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II protein D1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII D1 protein"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"1.10.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II Q(B) protein"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"psbA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 a plastoquinone + 4 hnu + 2 H2O = 2 a plastoquinol + O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36359"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:62192"}],"ecNumber":"1.10.3.9","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Belongs to the reaction center PufL/M/PsbA/D family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Photosystem II protein D1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_0000340066"},{"type":"Propeptide","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_0000340067"},{"type":"Transmembrane","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"ChlzD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:136840"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"pheophytin a","id":"ChEBI:CHEBI:136840","label":"D1"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"PD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Tyrosine radical intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Stabilizes free radical intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Cleavage; by CTPA","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylthreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0106","category":"Ligand","name":"Calcium"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0359","category":"Biological process","name":"Herbicide resistance"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00196.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"YP_009584171.1","properties":[{"key":"NucleotideSequenceId","value":"NC_041575.1"}]},{"database":"AlphaFoldDB","id":"Q2WGI0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGI0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39713311","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016168","properties":[{"key":"GoTerm","value":"F:chlorophyll binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010242","properties":[{"key":"GoTerm","value":"F:oxygen evolving activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009772","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd09289","properties":[{"key":"EntryName","value":"Photosystem-II_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.85.10:FF:000002","properties":[{"key":"EntryName","value":"Photosystem II protein D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.85.10","properties":[{"key":"EntryName","value":"Photosystem II protein D1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01379","properties":[{"key":"EntryName","value":"PSII_PsbA_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR055266","properties":[{"key":"EntryName","value":"D1/D2"}]},{"database":"InterPro","id":"IPR036854","properties":[{"key":"EntryName","value":"Photo_II_D1/D2_sf"}]},{"database":"InterPro","id":"IPR000484","properties":[{"key":"EntryName","value":"Photo_RC_L/M"}]},{"database":"InterPro","id":"IPR055265","properties":[{"key":"EntryName","value":"Photo_RC_L/M_CS"}]},{"database":"InterPro","id":"IPR005867","properties":[{"key":"EntryName","value":"PSII_D1"}]},{"database":"NCBIfam","id":"TIGR01151","properties":[{"key":"EntryName","value":"psbA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149:SF12","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II D2 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II PROTEIN D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00124","properties":[{"key":"EntryName","value":"Photo_RC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00256","properties":[{"key":"EntryName","value":"REACTNCENTRE"}]},{"database":"SUPFAM","id":"SSF81483","properties":[{"key":"EntryName","value":"Bacterial photosystem II reaction centre, L and M subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00244","properties":[{"key":"EntryName","value":"REACTION_CENTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTATLERRENASLWGNFCDWITSTENRLYIGWFGVLMIPTLLTATSVFITAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASIDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANAGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAASIEAPSLNG","length":354,"molWeight":38909,"crc64":"41FC2BD7B47CF5DC","md5":"CCEB23EA5693611AF4BB44A1B1F5C930"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":2,"MISCELLANEOUS":2,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Propeptide":1,"Transmembrane":5,"Binding site":13,"Site":3,"Modified residue":2},"uniParcId":"UPI000065C9E7"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGC5","uniProtkbId":"PSAB_SELUN","entryAudit":{"firstPublicDate":"2007-02-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":70,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Photosystem I P700 chlorophyll a apoprotein A2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PSI-B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"psaB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Belongs to the PsaA/PsaB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":734,"modifier":"EXACT"}},"description":"Photosystem I P700 chlorophyll a apoprotein A2","featureId":"PRO_0000275973"},{"type":"Transmembrane","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Helical; Name=I","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Helical; Name=II","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Helical; Name=III","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Helical; Name=IV","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Helical; Name=V","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Helical; Name=VI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"Helical; Name=VII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":535,"modifier":"EXACT"}},"description":"Helical; Name=VIII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"Helical; Name=IX","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":643,"modifier":"EXACT"},"end":{"value":665,"modifier":"EXACT"}},"description":"Helical; Name=X","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":707,"modifier":"EXACT"},"end":{"value":727,"modifier":"EXACT"}},"description":"Helical; Name=XI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Binding site","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":654,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":662,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"}},{"type":"Binding site","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":671,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18067"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"phylloquinone","id":"ChEBI:CHEBI:18067","label":"B"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00251.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"YP_009584231.1","properties":[{"key":"NucleotideSequenceId","value":"NC_041575.1"}]},{"database":"AlphaFoldDB","id":"Q2WGC5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGC5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39713387","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009522","properties":[{"key":"GoTerm","value":"C:photosystem I"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.1130.10:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I P700 chlorophyll a apoprotein A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1130.10","properties":[{"key":"EntryName","value":"Photosystem I PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00482","properties":[{"key":"EntryName","value":"PSI_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001280","properties":[{"key":"EntryName","value":"PSI_PsaA/B"}]},{"database":"InterPro","id":"IPR020586","properties":[{"key":"EntryName","value":"PSI_PsaA/B_CS"}]},{"database":"InterPro","id":"IPR036408","properties":[{"key":"EntryName","value":"PSI_PsaA/B_sf"}]},{"database":"InterPro","id":"IPR006244","properties":[{"key":"EntryName","value":"PSI_PsaB"}]},{"database":"NCBIfam","id":"TIGR01336","properties":[{"key":"EntryName","value":"psaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN, OMPA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128:SF19","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00223","properties":[{"key":"EntryName","value":"PsaA_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002905","properties":[{"key":"EntryName","value":"PSI_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00257","properties":[{"key":"EntryName","value":"PHOTSYSPSAAB"}]},{"database":"SUPFAM","id":"SSF81558","properties":[{"key":"EntryName","value":"Photosystem I subunits PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00419","properties":[{"key":"EntryName","value":"PHOTOSYSTEM_I_PSAAB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALRSPKSSRGLSQDPTTRRIWFGIATAHDFESHDGMTEERLYQNIFASHLGQLAIIFLWTSGNLFHVAWQGNSEARIKDPLHVRPIAHAIWDPHFGQPAVEAFARGGGLGPVNIAYPGVYQRWYTIGMRTDQDLYTGAFSLLIVSTLFLVAGWLHLEPKWAPSISWFKNAESRLNHHLSGLFGVSSLARAGHLVHVAIPESRGGHVRWGNLLSASPHPQGLGPLSAGQWGVYARDVDSSSHLFNTSQGAGTAIPTFTGGFHPQTQSPWLTDIAHHHLAIAVVFIIAGHTYRTNFGIGHSIGGALEAHIPPGGRLGRGHQGLYDTINNSLHFQLGLALASLGVVTSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFLTRDYSPERGRGNVLARVLEHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPVFAQWIQSAHGKASYGFDVLLSSPNDPAFNAGRSIWLPGRLDAIDNNSNSLFLTIGPGDFPVHHAIASGLHTTTLILSKGALDARGSKLMPDKKEFGYGFPCDGPGRGGTCDISAWDAFYPAVFWMLNTIGWVTLHWHWKHITLWQGNVAQLDESSTYLMGWSRDYSWLNSSQLINGYNPFGTNSLSVWAWMFSFGHLVWATGFMFLIPRRGYWQELIETLARAHERTPLANLVRWGDKPVALSIVQARLVGLAHFSVGYIFTYAAFPIPSTAGKFG","length":734,"molWeight":80815,"crc64":"DF499362DDCBF44A","md5":"3514D70428324D9726B866B456EE6063"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":11,"Binding site":6},"uniParcId":"UPI000065CA21"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGJ0","uniProtkbId":"ATPA_SELUN","entryAudit":{"firstPublicDate":"2006-05-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":92,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"ATP synthase subunit alpha, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"7.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"ATP synthase F1 sector subunit alpha"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"F-ATPase subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"atpA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Belongs to the ATPase alpha/beta chains family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":507,"modifier":"EXACT"}},"description":"ATP synthase subunit alpha, chloroplastic","featureId":"PRO_0000238439"},{"type":"Region","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0139","category":"Cellular component","name":"CF(1)"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00186.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q2WGJ0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGJ0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043531","properties":[{"key":"GoTerm","value":"F:ADP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18113","properties":[{"key":"EntryName","value":"ATP-synt_F1_alpha_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18116","properties":[{"key":"EntryName","value":"ATP-synt_F1_alpha_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01132","properties":[{"key":"EntryName","value":"F1-ATPase_alpha_CD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000002","properties":[{"key":"EntryName","value":"ATP synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.150.20","properties":[{"key":"EntryName","value":"ATP synthase alpha/beta chain, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01346","properties":[{"key":"EntryName","value":"ATP_synth_alpha_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023366","properties":[{"key":"EntryName","value":"ATP_synth_asu-like_sf"}]},{"database":"InterPro","id":"IPR000793","properties":[{"key":"EntryName","value":"ATP_synth_asu_C"}]},{"database":"InterPro","id":"IPR038376","properties":[{"key":"EntryName","value":"ATP_synth_asu_C_sf"}]},{"database":"InterPro","id":"IPR033732","properties":[{"key":"EntryName","value":"ATP_synth_F1_a_nt-bd_dom"}]},{"database":"InterPro","id":"IPR005294","properties":[{"key":"EntryName","value":"ATP_synth_F1_asu"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR036121","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N_sf"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00962","properties":[{"key":"EntryName","value":"atpA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48082","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48082:SF2","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00306","properties":[{"key":"EntryName","value":"ATP-synt_ab_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47917","properties":[{"key":"EntryName","value":"C-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50615","properties":[{"key":"EntryName","value":"N-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVNIRPDETSSIILGQTAQYDQEVGVFSTGTVLQVGDGIARIHGPDGVTAGELVESEDGTVGIALNSEPDNAGAVSMGDGSTIQEGSSVKATGKIAQIPVSDAYLGRVANAPAQPTDGKGRIAASEPRLTESPAPGIISRRSVYEPMQTGLIATDPMIPTGRGQRELIIGDRQTGKTAVAIDTTPNQRGQNVICVYVAIGQKASPAAQVVSTFEERGAMEYTVAVAETANPPATSQYLAPYTGAALAEYFMYRKRHTLIIYDDPSKQAQAYRQMSLLPRRPPGREAHPGDVPHLHPRPPERAAKLSSQPGEGSTTASPTVETQAGDVSAYIPTNVTSTTDGQIFLSADLSNAGVRPATNVGISASRVGPAAQIKATKQVAGKSKSELAQFAEPEASAQFASDPDKATRNQSARGQRSRELLKQSQPAPLPVEEQVATTHAGASGFSDVSEIGQVQGSPAQSREYLVTNKPEPAEIVRPTKTFTERAETILKEAIKEHTESFSLKKQI","length":507,"molWeight":53516,"crc64":"03D2FFED32ACDC8D","md5":"CD93EDC93AFF92582FC0B6D1D3F7A615"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":3,"Compositional bias":2,"Binding site":1,"Site":1},"uniParcId":"UPI000065C9DD"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGC1","uniProtkbId":"RK23_SELUN","entryAudit":{"firstPublicDate":"2007-01-23","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":69,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Large ribosomal subunit protein uL23cz/uL23cy"}},"alternativeNames":[{"fullName":{"value":"50S ribosomal protein L23, chloroplastic"}}]},"genes":[{"geneName":{"value":"rpl23-A"}},{"geneName":{"value":"rpl23-B"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds to 23S rRNA"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Part of the 50S ribosomal subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the universal ribosomal protein uL23 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Large ribosomal subunit protein uL23cz/uL23cy","featureId":"PRO_0000272931"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"id":"KW-0689","category":"Molecular function","name":"Ribosomal protein"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00232.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00255.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q2WGC1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGC1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005840","properties":[{"key":"GoTerm","value":"C:ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003735","properties":[{"key":"GoTerm","value":"F:structural constituent of ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.70.330","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01369_B","properties":[{"key":"EntryName","value":"Ribosomal_uL23_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012677","properties":[{"key":"EntryName","value":"Nucleotide-bd_a/b_plait_sf"}]},{"database":"InterPro","id":"IPR013025","properties":[{"key":"EntryName","value":"Ribosomal_uL23-like"}]},{"database":"InterPro","id":"IPR012678","properties":[{"key":"EntryName","value":"Ribosomal_uL23/eL15/eS24_sf"}]},{"database":"Pfam","id":"PF00276","properties":[{"key":"EntryName","value":"Ribosomal_L23"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54189","properties":[{"key":"EntryName","value":"Ribosomal proteins S24e, L23 and L15e"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGGVENPVSTDKAIRLPERKQYSSNAEPNPSKTEVKRRIERFPRVRIVAINSHRLPAGAARGSAGSVTGRRVRRKRMITTLRLNHPIPLFPGKQNGFVS","length":99,"molWeight":11041,"crc64":"BF47ED3C2BBD7EA8","md5":"759B8E443D05D1351AF82B215F6B6BD6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":2},"uniParcId":"UPI000065CA0E"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGC7","uniProtkbId":"PSBZ_SELUN","entryAudit":{"firstPublicDate":"2007-02-06","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2006-01-10","entryVersion":62,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"Photosystem II reaction center protein Z"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"PSII-Z"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"psbZ"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"May control the interaction of photosystem II (PSII) cores with the light-harvesting antenna, regulates electron flow through the 2 photosystem reaction centers. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}],"value":"Belongs to the PsbZ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Photosystem II reaction center protein Z","featureId":"PRO_0000277234"},{"type":"Transmembrane","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}]},{"type":"Transmembrane","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00644"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0674","category":"Cellular component","name":"Reaction center"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00249.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"YP_009584229.1","properties":[{"key":"NucleotideSequenceId","value":"NC_041575.1"}]},{"database":"AlphaFoldDB","id":"Q2WGC7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGC7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39713384","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009539","properties":[{"key":"GoTerm","value":"C:photosystem II reaction center"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042549","properties":[{"key":"GoTerm","value":"P:photosystem II stabilization"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.287.740","properties":[{"key":"EntryName","value":"Photosystem II PsbZ, reaction centre"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00644","properties":[{"key":"EntryName","value":"PSII_PsbZ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002644","properties":[{"key":"EntryName","value":"PSII_PsbZ"}]},{"database":"InterPro","id":"IPR036512","properties":[{"key":"EntryName","value":"PSII_PsbZ_sf"}]},{"database":"NCBIfam","id":"TIGR03043","properties":[{"key":"EntryName","value":"PS_II_psbZ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34971","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II REACTION CENTER PROTEIN Z"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34971:SF2","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II REACTION CENTER PROTEIN Z"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01737","properties":[{"key":"EntryName","value":"Ycf9"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161055","properties":[{"key":"EntryName","value":"PsbZ-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVALQSAVFASIAIPFIPVIGVPAVFASPDGWSSGKNVVFSGATPRIGPVPLVGILNSSVS","length":62,"molWeight":6195,"crc64":"9A8B0BFED5E4E158","md5":"C455513E1E2A5025866DCD92AD098D7C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":2},"uniParcId":"UPI000065CA1F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGI1","uniProtkbId":"MATK_SELUN","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":49,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Probable maturase K"}},"alternativeNames":[{"fullName":{"value":"Intron maturase"}}]},"genes":[{"geneName":{"value":"matK"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the intron maturase 2 family. MatK subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"Probable maturase K","featureId":"PRO_0000363783"},{"type":"Region","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00195.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q2WGI1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0006397","properties":[{"key":"GoTerm","value":"P:mRNA processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"InterPro","id":"IPR002866","properties":[{"key":"EntryName","value":"Maturase_MatK"}]},{"database":"InterPro","id":"IPR024942","properties":[{"key":"EntryName","value":"Maturase_MatK_N"}]},{"database":"PANTHER","id":"PTHR34811","properties":[{"key":"EntryName","value":"MATURASE K"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34811:SF1","properties":[{"key":"EntryName","value":"MATURASE K"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01824","properties":[{"key":"EntryName","value":"MatK_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAWASTGRGLRINNVWCQQRLLHPLPSRDDTHAIAFSSSPGKSDPEQEGVTGPNKKHSDLATIKQPTSGIRRQDASSSSCFAGRGSSGLEGCRDRRRPLRSYTNISLELAVGGPLTMVPQICHPVKARQPLVVHEWNIFRSIPSTFILTEEGPPRCHRFLGTELSYSSHPEIPIRIPRCRIRDAPLPHSPRITLHGHRNSGVPQRSAARSPAGTNGFIIPPWNHYMYEPECRLTRLCGQAPHSRVPPCGACAPNTTRSTRGVAGHIAKGLSRIVEPPLWIVILPPKRILPLPKGEPSIHYARCVNHFMIASKAATSAEKWKHHHPRFRRYHPSARARSGFMDQSFEDCSASLCYVSGTRPEIRKVRARMVGDPLLTGTPSEELLAATPTTHSIGLSAEDKYRSTAGRPTSRSARTILPRDDDVSNRSYRISASIHYCGECSKERNGLYRMQHIPRSSCAKTPARKHGGTIRVARDEYGPGVFRAPPPTPAEGRALLLIGVRRQGRTNWYSDMTRVDCVANHLRRERAPHTRCR","length":534,"molWeight":59433,"crc64":"A4BA5DD721561899","md5":"55959B5FB84975FF041C34CBB2A1404F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1},"uniParcId":"UPI000065C9E6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGD3","uniProtkbId":"TI214_SELUN","entryAudit":{"firstPublicDate":"2006-11-28","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":38,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"Protein TIC 214"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"Translocon at the inner envelope membrane of chloroplasts 214"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"AtTIC214"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"TIC214"},"synonyms":[{"value":"ycf1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"Part of the Tic complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56785"}],"value":"Plastid, chloroplast inner membrane","id":"SL-0051"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the TIC214 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1601,"modifier":"EXACT"}},"description":"Protein TIC 214","featureId":"PRO_0000262628"},{"type":"Transmembrane","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":535,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":806,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":879,"modifier":"EXACT"},"end":{"value":916,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1216,"modifier":"EXACT"},"end":{"value":1244,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1521,"modifier":"EXACT"},"end":{"value":1574,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":794,"modifier":"EXACT"},"end":{"value":806,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1230,"modifier":"EXACT"},"end":{"value":1244,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-1001","category":"Cellular component","name":"Plastid inner membrane"},{"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00243.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q2WGD3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009706","properties":[{"key":"GoTerm","value":"C:chloroplast inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"InterPro","id":"IPR008896","properties":[{"key":"EntryName","value":"TIC214"}]},{"database":"PANTHER","id":"PTHR33163:SF40","properties":[{"key":"EntryName","value":"PROTEIN TIC 214"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33163","properties":[{"key":"EntryName","value":"PROTEIN TIC 214-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05758","properties":[{"key":"EntryName","value":"Ycf1"},{"key":"MatchStatus","value":"3"}]}],"sequence":{"value":"MQKWASHLCAPQVPLSLWIRSSGPPILLGLYCGFAATLPTGPFHVPSVRASVSGREGVSGRSVASSSVTGQPVIIPSAYSPHFHVVSVKPHAVTSSAPPCISLYWYRHRVGIEAPRTAEPRAVTAIGWAYAAVASRDTEVWVRRSTLLDIIILPLPHHVPVLSPALARLVRLFVLRHSNQFLLVISSLRGWSGGSIPLEYLATPLVVPKIDPTDDGPSEPPVEPPAEASTTHRVPGTIVTALRLLCLGRAPLPVLFRETRHEPQRSSGGGDQEDFSWLNAWPASAFDYQKGVRPFRYVTDGYNPGSSVKKELSQYHFCTVVGPRKQTLSLSSPPGLSIPDDNSDKSVNLSLLPTTHKEPPPCREWIRTGGRKESDSNNDSMNRTEAPREGYSLVKVVDSNNGLYDHGESVPAEIHDPSISNGSRGRIVGFRSTRLSTRRKSGRRTASNSFRNSPGAPVEEGRNTGNHHREHPLLFVDATRRNSYSSLVTRVLRTHDMIRLLCIIIEHKQTFRWILNVVNDLLSVGSSDNSDDAYAADGANDAATGGGDDTDDDADDDANAAGYIRSMKVRNVEYAVNERTGNLRVLKRPVLQPDYRRNLIAGLMRARRRKTLVWESLQSRTHSPLFLRMIGNSAPPQFSPGINAKAILTPHRSAAEEEDNKAKPVFRRSAKMATAKRIAAAKRWDFTTAHLTRGCSPIAQLYLRRNVILPTLTIFRNICYLIMFQKGEWGEDWNELNKEVYVGRSYDGNAAEVAKGLPRRWYRNGLQIKIVNPFYLKHRRHFVYGQSEPDDGTGINSTGTRNGMSKSISSYETNSYGNSSSAGGGMGFGHSTVLGCLAESPLGDRIKRPSFWKPLLMELGRVWWGNVPWIRKTHIENLPSRPAGKDPSPVGKADGLDAGTGKSIGDRVAGTRPGECGAHSAKVGGGISDLSIEFMPERDCPLAVSDQSEYRARMSTGELGCLVARGNDGASRVTGEFAGAGKAIAPFGPTGQDRGYTGGSGTAAPILIHRIVVRARGRCLRLLRVSTCFVQIPFSGFHGAAAPICRFLPVWFNIRLITRSTRRYVSKVRRARDLLAGRGGGDSIGVYSSRRDVRVISQAYVLSRAWRLSAVNKFRPADPEYGRGNPGARKSTAHLGVGGQGILGKRPLRALGGRYEWARDPRRYNVPSGIWCRIAPRGRKMKDEYPRMKDRELNKKQSMTLDEAICLRGIDPEPAAGVERSRKIDRQYGSNPPSKSSPDVVPDSSEIRGFAKPWRMGRGIIPNDRTRKHRERIVSGGGWDRPENRMNERKNLPFGSNIHSWLYIDIPERFHILEMPEFVATRYLGLACELNVSTASGYVCAGRGSARARVETEFREDRIEGRWDLGSKQVTVRARKMRDATNVPHAVFIGSNIEYPREGSVESTCESMSRDMAPPPYHAAPPDSTNGMLDGNRGHRATGVDKRFLKHKMLSVLPNFQNRFRGILDFIAYYEKSVPPRTGILEDGGDKTICPHSSHIGDVPLPKRRAGSRILESFYLAEGRSRGARSEGGTVEGHERRDEEPPVQNRNAEENETQTINSILRPGHRPEDPSRMNRPRFCTNNGSQFAAARVRIYPSAGIFMT","length":1601,"molWeight":176986,"crc64":"492A852AE0FBC74C","md5":"BE48275781A32F2BB8E49EC7479E4574"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":4,"Region":8,"Compositional bias":4},"uniParcId":"UPI000065CA19"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q2WGF1","uniProtkbId":"RR8_SELUN","entryAudit":{"firstPublicDate":"2007-06-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-01-10","entryVersion":60,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Small ribosomal subunit protein uS8c"}},"alternativeNames":[{"fullName":{"value":"30S ribosomal protein S8, chloroplastic"}}]},"genes":[{"geneName":{"value":"rps8"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Part of the 30S ribosomal subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the universal ribosomal protein uS8 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Small ribosomal subunit protein uS8c","featureId":"PRO_0000290992"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"id":"KW-0689","category":"Molecular function","name":"Ribosomal protein"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"17297557","citationType":"journal article","authors":["Tsuji S.","Ueda K.","Nishiyama T.","Hasebe M.","Yoshikawa S.","Konagaya A.","Nishiuchi T.","Yamaguchi K."],"citationCrossReferences":[{"database":"PubMed","id":"17297557"},{"database":"DOI","id":"10.1007/s10265-006-0055-y"}],"title":"The chloroplast genome from a lycophyte (microphyllophyte), Selaginella uncinata, has a unique inversion, transpositions and many gene losses.","publicationDate":"2007","journal":"J. Plant Res.","firstPage":"281","lastPage":"290","volume":"120"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB197035","properties":[{"key":"ProteinId","value":"BAE00225.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"YP_009584204.1","properties":[{"key":"NucleotideSequenceId","value":"NC_041575.1"}]},{"database":"AlphaFoldDB","id":"Q2WGF1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q2WGF1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39713349","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005840","properties":[{"key":"GoTerm","value":"C:ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003735","properties":[{"key":"GoTerm","value":"F:structural constituent of ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.30.1490.10:FF:000001","properties":[{"key":"EntryName","value":"30S ribosomal protein S8"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1370.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1490.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01302_B","properties":[{"key":"EntryName","value":"Ribosomal_uS8_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000630","properties":[{"key":"EntryName","value":"Ribosomal_uS8"}]},{"database":"InterPro","id":"IPR035987","properties":[{"key":"EntryName","value":"Ribosomal_uS8_sf"}]},{"database":"PANTHER","id":"PTHR11758","properties":[{"key":"EntryName","value":"40S RIBOSOMAL PROTEIN S15A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00410","properties":[{"key":"EntryName","value":"Ribosomal_S8"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56047","properties":[{"key":"EntryName","value":"Ribosomal protein S8"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGNDAIDDVTTAPRNASSRGAETVRVSSTDITISIGRVLVEEGFSGNPREHRQGTNRFPVSTSKYQGRTRKARITTRRRVSKPGLRIYPGYKDIPEVSGGIGTATPPTPGGTTTDREARQKRIGGEAPRHVWR","length":133,"molWeight":14515,"crc64":"3D10A5B0F275FCCE","md5":"1C7195553D3F05C4ED83A0C518E97714"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":2,"Compositional bias":4},"uniParcId":"UPI000065CA07"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UGV5","uniProtkbId":"A0A0G2UGV5_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":43,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004332"}],"value":"Photosystem II protein D1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII D1 protein"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"1.10.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II Q(B) protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}],"value":"psbA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055838"}],"value":"This is one of the two reaction center proteins of photosystem II"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 a plastoquinone + 4 hnu + 2 H2O = 2 a plastoquinol + O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36359"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:62192"}],"ecNumber":"1.10.3.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004331"}],"value":"Belongs to the reaction center PufL/M/PsbA/D family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Photosystem II protein D1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_5047551915"},{"type":"Propeptide","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_5047551916"},{"type":"Transmembrane","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"ChlzD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:136840"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"pheophytin a","id":"ChEBI:CHEBI:136840","label":"D1"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"PD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Tyrosine radical intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Stabilizes free radical intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Cleavage; by CtpA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylthreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022494"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022991"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022646"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0359","category":"Biological process","name":"Herbicide resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023276"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01379"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29331.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028141","properties":[{"key":"ProteinId","value":"AKI29331.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"RefSeq","id":"YP_009584171.1","properties":[{"key":"NucleotideSequenceId","value":"NC_041575.1"}]},{"database":"AlphaFoldDB","id":"A0A0G2UGV5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A0G2UGV5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"39713311","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016168","properties":[{"key":"GoTerm","value":"F:chlorophyll binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010242","properties":[{"key":"GoTerm","value":"F:oxygen evolving activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009772","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd09289","properties":[{"key":"EntryName","value":"Photosystem-II_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.85.10:FF:000002","properties":[{"key":"EntryName","value":"Photosystem II protein D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.85.10","properties":[{"key":"EntryName","value":"Photosystem II protein D1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01379","properties":[{"key":"EntryName","value":"PSII_PsbA_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR055266","properties":[{"key":"EntryName","value":"D1/D2"}]},{"database":"InterPro","id":"IPR036854","properties":[{"key":"EntryName","value":"Photo_II_D1/D2_sf"}]},{"database":"InterPro","id":"IPR000484","properties":[{"key":"EntryName","value":"Photo_RC_L/M"}]},{"database":"InterPro","id":"IPR055265","properties":[{"key":"EntryName","value":"Photo_RC_L/M_CS"}]},{"database":"InterPro","id":"IPR005867","properties":[{"key":"EntryName","value":"PSII_D1"}]},{"database":"NCBIfam","id":"TIGR01151","properties":[{"key":"EntryName","value":"psbA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149:SF12","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II D2 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II PROTEIN D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00124","properties":[{"key":"EntryName","value":"Photo_RC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00256","properties":[{"key":"EntryName","value":"REACTNCENTRE"}]},{"database":"SUPFAM","id":"SSF81483","properties":[{"key":"EntryName","value":"Bacterial photosystem II reaction centre, L and M subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00244","properties":[{"key":"EntryName","value":"REACTION_CENTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTATLERRENASLWGNFCDWITSTENRLYIGWFGVLMIPTLLTATSVFITAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASIDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANAGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAASIEAPSLNG","length":354,"molWeight":38909,"crc64":"41FC2BD7B47CF5DC","md5":"CCEB23EA5693611AF4BB44A1B1F5C930"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":2,"MISCELLANEOUS":2,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Propeptide":1,"Transmembrane":5,"Binding site":13,"Site":3,"Modified residue":2},"uniParcId":"UPI000065C9E7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF57","uniProtkbId":"A0A0G2UF57_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATP synthase subunit c, chloroplastic"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATP synthase F(0) sector subunit c"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATPase subunit III"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F-type ATPase subunit c"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F-ATPase subunit c"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Lipid-binding protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}],"value":"atpH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025198"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"value":"In plastids the F-type ATPase is also known as CF(1)CF(0)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006704"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"Belongs to the ATPase C chain family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}]},{"type":"Domain","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"V-ATPase proteolipid subunit C-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00137"}]},{"type":"Site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023310"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022547"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0138","category":"Cellular component","name":"CF(0)"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023121"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004221"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01396"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29302.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028112","properties":[{"key":"ProteinId","value":"AKI29302.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF57","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033177","properties":[{"key":"GoTerm","value":"C:proton-transporting two-sector ATPase complex, proton-transporting domain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18183","properties":[{"key":"EntryName","value":"ATP-synt_Fo_c_ATPH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.20.10:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit c, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.20.10","properties":[{"key":"EntryName","value":"F1F0 ATP synthase subunit C"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01396","properties":[{"key":"EntryName","value":"ATP_synth_c_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005953","properties":[{"key":"EntryName","value":"ATP_synth_csu_bac/chlpt"}]},{"database":"InterPro","id":"IPR000454","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu"}]},{"database":"InterPro","id":"IPR020537","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu_DDCD_BS"}]},{"database":"InterPro","id":"IPR038662","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu_sf"}]},{"database":"InterPro","id":"IPR002379","properties":[{"key":"EntryName","value":"ATPase_proteolipid_c-like_dom"}]},{"database":"InterPro","id":"IPR035921","properties":[{"key":"EntryName","value":"F/V-ATP_Csub_sf"}]},{"database":"NCBIfam","id":"TIGR01260","properties":[{"key":"EntryName","value":"ATP_synt_c"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF005608","properties":[{"key":"EntryName","value":"PRK07354.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10031","properties":[{"key":"EntryName","value":"ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10031:SF0","properties":[{"key":"EntryName","value":"ATPASE PROTEIN 9"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00137","properties":[{"key":"EntryName","value":"ATP-synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00124","properties":[{"key":"EntryName","value":"ATPASEC"}]},{"database":"SUPFAM","id":"SSF81333","properties":[{"key":"EntryName","value":"F1F0 ATP synthase subunit C"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00605","properties":[{"key":"EntryName","value":"ATPASE_C"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNPLISAASVVAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV","length":81,"molWeight":7976,"crc64":"170060613EE08D23","md5":"2235C48C54A76EFC2A590779460A57D1"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Site":1},"uniParcId":"UPI00063D6113"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF63","uniProtkbId":"A0A0G2UF63_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Light-independent protochlorophyllide reductase subunit N"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"DPOR subunit N"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"LI-POR subunit N"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}],"value":"chlN"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Belongs to the BchN/ChlN family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"Nitrogenase/oxidoreductase component 1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00148"}]},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00352"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29307.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028117","properties":[{"key":"ProteinId","value":"AKI29307.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF63","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01979","properties":[{"key":"EntryName","value":"Pchlide_reductase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1980","properties":[{"key":"EntryName","value":"Nitrogenase molybdenum iron protein domain"},{"key":"MatchStatus","value":"3"}]},{"database":"HAMAP","id":"MF_00352","properties":[{"key":"EntryName","value":"ChlN_BchN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050293","properties":[{"key":"EntryName","value":"LIPOR_BchN/ChlN"}]},{"database":"InterPro","id":"IPR000510","properties":[{"key":"EntryName","value":"Nase/OxRdtase_comp1"}]},{"database":"InterPro","id":"IPR005970","properties":[{"key":"EntryName","value":"Protochl_reductN"}]},{"database":"NCBIfam","id":"TIGR01279","properties":[{"key":"EntryName","value":"DPOR_bchN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002768","properties":[{"key":"EntryName","value":"PRK02842.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39429","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39429:SF3","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00148","properties":[{"key":"EntryName","value":"Oxidored_nitro"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000162","properties":[{"key":"EntryName","value":"P_chlorophyll_rd"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53807","properties":[{"key":"EntryName","value":"Helical backbone' metal receptor"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKGFETPTFECETGNYHTFCPISCVAWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAQLNDYGELKRLCLQIMTNRDPGVIVWIGTCTTEVIKMDLEGMAPELESEIGVPIVVARANGLDYAFTQGEDTVLAAMAHRCVERDLGSADERQPVRSPLSKTEYSKPATVLPAGEGTNPPLVLFGSLPSMVASQLNLELKRQSVRVWGWLPARSYTALPSLGAGVYVCGVNPFLSRTATALMRRRKCRLIGAPFPIGPDGTRAWIEKICSVFGIRTKGLRERERHVWEGLKDYLDLVRGKSVFFMGDNLLEVSLARFLIRCGMIVYEIGIPYMDKRYQAAELALLRDTCRDMCVLVPRIVEKPDNYDQIQRMRELRPDLAITGMANANPLEARGIDTKWSVELTFAQIHGFTNARGVLRLVTRSLRRNDLVGDLGWAANPAEAEGDNDPLTQR","length":468,"molWeight":52261,"crc64":"F0224942EF9CD490","md5":"6F6B32D244982B9C6323460676D14889"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":3},"uniParcId":"UPI00063D5C64"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF70","uniProtkbId":"A0A0G2UF70_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"NAD(P)H dehydrogenase subunit 3"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"NADH-plastoquinone oxidoreductase subunit 3"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}],"value":"ndhC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003257"}],"value":"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29091"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"7.1.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049551"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004225"}],"value":"Mitochondrion membrane","id":"SL-0171"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004225"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008472"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}],"value":"Belongs to the complex I subunit 3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}]},{"type":"Transmembrane","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003641"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01394"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29312.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028122","properties":[{"key":"ProteinId","value":"AKI29312.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF70","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0031966","properties":[{"key":"GoTerm","value":"C:mitochondrial membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0030964","properties":[{"key":"GoTerm","value":"C:NADH dehydrogenase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0019684","properties":[{"key":"GoTerm","value":"P:photosynthesis, light reaction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.20.58.1610","properties":[{"key":"EntryName","value":"NADH:ubiquinone/plastoquinone oxidoreductase, chain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01394","properties":[{"key":"EntryName","value":"NDH1_NuoA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023043","properties":[{"key":"EntryName","value":"NAD(P)H_OxRDtase_bac/plastid"}]},{"database":"InterPro","id":"IPR000440","properties":[{"key":"EntryName","value":"NADH_UbQ/plastoQ_OxRdtase_su3"}]},{"database":"InterPro","id":"IPR038430","properties":[{"key":"EntryName","value":"NDAH_ubi_oxred_su3_sf"}]},{"database":"PANTHER","id":"PTHR11058","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11058:SF9","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00507","properties":[{"key":"EntryName","value":"Oxidored_q4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLSILEYNSLLLFLLIASLVPLAAYLISGIVAPVSGGPEKFLGYESGMESMGDTRTQFQIRYYMFALVFVVFDVETVFLYPWATSFRELGVSAFIEAFTFVVILIVGLVYAWRKGALEWS","length":120,"molWeight":13484,"crc64":"59729B50FDED1348","md5":"D39765EADD56C5E8D573E2B75D43EC3A"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":2},"uniParcId":"UPI00063D56F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF77","uniProtkbId":"A0A0G2UF77_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NAD(P)H-quinone oxidoreductase subunit H, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NAD(P)H dehydrogenase, subunit H"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NADH-plastoquinone oxidoreductase 49 kDa subunit"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NADH-plastoquinone oxidoreductase subunit H"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}],"value":"ndhH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"value":"Stromal side","id":"SL-9917"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005769"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003685"}],"value":"Belongs to the complex I 49 kDa subunit family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"NADH-quinone oxidoreductase subunit D","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00346"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01358"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29317.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028127","properties":[{"key":"ProteinId","value":"AKI29317.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF77","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016655","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019684","properties":[{"key":"GoTerm","value":"P:photosynthesis, light reaction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.645.10","properties":[{"key":"EntryName","value":"Cytochrome-c3 Hydrogenase, chain B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01358","properties":[{"key":"EntryName","value":"NDH1_NuoD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001135","properties":[{"key":"EntryName","value":"NADH_Q_OxRdtase_suD"}]},{"database":"InterPro","id":"IPR014029","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_49kDa_CS"}]},{"database":"InterPro","id":"IPR022885","properties":[{"key":"EntryName","value":"NDH1_su_D/H"}]},{"database":"InterPro","id":"IPR029014","properties":[{"key":"EntryName","value":"NiFe-Hase_large"}]},{"database":"NCBIfam","id":"NF004739","properties":[{"key":"EntryName","value":"PRK06075.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF005649","properties":[{"key":"EntryName","value":"PRK07415.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11993:SF10","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11993","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00346","properties":[{"key":"EntryName","value":"Complex1_49kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56762","properties":[{"key":"EntryName","value":"HydB/Nqo4-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00535","properties":[{"key":"EntryName","value":"COMPLEX1_49K"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTMSTERGNTMVVSMGPHHPSMHGVLRLIANLDGENVIDCEPVLGYLHRGMEKIAENRTIVQYLPYVTRWDYLATMFTEAVTVNAPERLIDIQVPKRASYIRIIMLELSRIASHLLWLGPFMADIGAQTPFFCIFREREMVYDLFEAATGMRMMHNYFRVGGVAVDLPYGWVDKCLDFCDYFLPRVDEYERLITRNPIFLKRVEGVGIVSGEEAINWGLSGPMLRASGVRWDLRRVDHYECYDELDWRGVWQKEGDSLARYLVRIGEMRESAGIIQQALRLIPGGPYENLEARRLKMNSMEDWNNFEYRFISKKPSPTLRLPEREHYVRVEAPKGELGIFLMGDDSTFPWRCKIRPPGFINLQILPQLVEGMKLADIMTILGSIDIIMGEVDR","length":393,"molWeight":45410,"crc64":"9B81F58A6DC7D36D","md5":"8C95FF8A1FECC163236AB9D1BC3B01A0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI00063D5E5A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF82","uniProtkbId":"A0A0G2UF82_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":39,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00035697"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"value":"Cytochrome b6"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}],"value":"petB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003068"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"Binds 2 heme b groups non-covalently with two histidine residues as axial ligands."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme c","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:61717"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"value":"Binds one heme group covalently by a single cysteine link with no axial amino acid ligand. This heme was named heme ci."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060385"}],"value":"Thylakoid","id":"SL-0450"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"value":"Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"value":"Belongs to the cytochrome b family. PetB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"Cytochrome b/b6 N-terminal region profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51002"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003291"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00633"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29322.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028132","properties":[{"key":"ProteinId","value":"AKI29322.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF82","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016491","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0022904","properties":[{"key":"GoTerm","value":"P:respiratory electron transport chain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00284","properties":[{"key":"EntryName","value":"Cytochrome_b_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.810.10:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome b6"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.810.10","properties":[{"key":"EntryName","value":"Cytochrome Bc1 Complex, Chain C"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00633","properties":[{"key":"EntryName","value":"Cytb6_f_cytb6"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005797","properties":[{"key":"EntryName","value":"Cyt_b/b6_N"}]},{"database":"InterPro","id":"IPR023530","properties":[{"key":"EntryName","value":"Cyt_B6_PetB"}]},{"database":"InterPro","id":"IPR027387","properties":[{"key":"EntryName","value":"Cytb/b6-like_sf"}]},{"database":"InterPro","id":"IPR048259","properties":[{"key":"EntryName","value":"Cytochrome_b_N_euk/bac"}]},{"database":"InterPro","id":"IPR016174","properties":[{"key":"EntryName","value":"Di-haem_cyt_TM"}]},{"database":"NCBIfam","id":"NF002990","properties":[{"key":"EntryName","value":"PRK03735.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19271","properties":[{"key":"EntryName","value":"CYTOCHROME B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19271:SF16","properties":[{"key":"EntryName","value":"CYTOCHROME B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00033","properties":[{"key":"EntryName","value":"Cytochrome_B"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000032","properties":[{"key":"EntryName","value":"Cytochrome_b6"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81342","properties":[{"key":"EntryName","value":"Transmembrane di-heme cytochromes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51002","properties":[{"key":"EntryName","value":"CYTB_NTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFGSVRYMMTEVNFGWLVRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSVSVGQSTLTRFYSLHTFVLPLLTAAFMLMHFLIIRKQGISGPL","length":215,"molWeight":24235,"crc64":"CB25763A1F394D42","md5":"0696793236562BCC2DE0DD844E7A60CE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":4,"Domain":1,"Binding site":9},"uniParcId":"UPI00063D60E6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UF87","uniProtkbId":"A0A0G2UF87_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Photosystem I P700 chlorophyll a apoprotein A2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PSI-B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}],"value":"psaB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003162"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048912"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Belongs to the PsaA/PsaB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":645,"modifier":"EXACT"},"end":{"value":665,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":707,"modifier":"EXACT"},"end":{"value":726,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Binding site","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":654,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":662,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"}},{"type":"Binding site","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":671,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18067"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"phylloquinone","id":"ChEBI:CHEBI:18067","label":"B"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022494"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022991"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022836"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00482"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29327.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028137","properties":[{"key":"ProteinId","value":"AKI29327.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UF87","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009522","properties":[{"key":"GoTerm","value":"C:photosystem I"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.1130.10:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I P700 chlorophyll a apoprotein A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1130.10","properties":[{"key":"EntryName","value":"Photosystem I PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00482","properties":[{"key":"EntryName","value":"PSI_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001280","properties":[{"key":"EntryName","value":"PSI_PsaA/B"}]},{"database":"InterPro","id":"IPR020586","properties":[{"key":"EntryName","value":"PSI_PsaA/B_CS"}]},{"database":"InterPro","id":"IPR036408","properties":[{"key":"EntryName","value":"PSI_PsaA/B_sf"}]},{"database":"InterPro","id":"IPR006244","properties":[{"key":"EntryName","value":"PSI_PsaB"}]},{"database":"NCBIfam","id":"TIGR01336","properties":[{"key":"EntryName","value":"psaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN, OMPA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128:SF19","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00223","properties":[{"key":"EntryName","value":"PsaA_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002905","properties":[{"key":"EntryName","value":"PSI_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00257","properties":[{"key":"EntryName","value":"PHOTSYSPSAAB"}]},{"database":"SUPFAM","id":"SSF81558","properties":[{"key":"EntryName","value":"Photosystem I subunits PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00419","properties":[{"key":"EntryName","value":"PHOTOSYSTEM_I_PSAAB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALRFPKFSRGLSQDPTTRRIWFGIATAHDFESHDGMTEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFEAWIKDPLHVRPIAHAIWDPHFGQPAVEAFARGGGLGPVNIAYSGVYQWWYTIGMRTDQDLYTGAFFLLIVSTLFLVAGWLHLEPKWAPSISWFKNAESRLNHHLSGLFGVSSLAWAGHLVHVAIPESRGGHVRWGNLLSASPHPQGLGPLFAGQWGVYARDVDSSSHLFNTSQGAGTAILTFTGGFHPQTQSLWLTDIAHHHLAIAVVFIIAGHMYRTNFGIGHSIGGALEAHIPPGGRLGRGHQGLYDTINNSLHFQLGLALASLGVVTSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFLTRDYSPERGRGNVLARVLEHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPVFAQWIQSAHGKASYGFDVLLSSPNDPAFNAGRSIWLPGWLDAIDNNSNSLFLTIGPGDFLVHHAIALGLHTTTLILSKGALDARGSKLMPDKKEFGYGFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVAQFDESSTYLMGWLRDYLWLNSSQLINGYNPFGTNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLVRWGDKPVALSIVQARLVGLAHFSVGYIFTYAAFLISSTAGKFG","length":734,"molWeight":81608,"crc64":"0FE37A377725E767","md5":"DE8BC638142B7BD7E50C9317B424DD23"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":7,"Binding site":6},"uniParcId":"UPI00063D58BE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFA3","uniProtkbId":"A0A0G2UFA3_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017673"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Light-independent protochlorophyllide reductase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"DPOR subunit B"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"LI-POR subunit B"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012713"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}],"value":"chlB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025201"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049483"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004949"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025959"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008935"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Belongs to the ChlB/BchB/BchZ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Nitrogenase/oxidoreductase component 1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00148"}]},{"type":"Domain","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"Light-independent protochlorophyllide reductase subunit B-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08369"}]},{"type":"Active site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}]},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"ligand":{"name":"substrate"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00353"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29305.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028115","properties":[{"key":"ProteinId","value":"AKI29305.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UFA3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01981","properties":[{"key":"EntryName","value":"Pchlide_reductase_B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.89.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1980","properties":[{"key":"EntryName","value":"Nitrogenase molybdenum iron protein domain"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"1.10.8.550","properties":[{"key":"EntryName","value":"Proto-chlorophyllide reductase 57 kD subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00353","properties":[{"key":"EntryName","value":"ChlB_BchB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050152","properties":[{"key":"EntryName","value":"ChlB/BchB/BchZ"}]},{"database":"InterPro","id":"IPR013580","properties":[{"key":"EntryName","value":"LI-POR_suB-like_C"}]},{"database":"InterPro","id":"IPR000510","properties":[{"key":"EntryName","value":"Nase/OxRdtase_comp1"}]},{"database":"InterPro","id":"IPR042298","properties":[{"key":"EntryName","value":"P-CP_red_C"}]},{"database":"InterPro","id":"IPR005969","properties":[{"key":"EntryName","value":"Protochl_reductB"}]},{"database":"InterPro","id":"IPR016209","properties":[{"key":"EntryName","value":"Protochlorophyllide_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01278","properties":[{"key":"EntryName","value":"DPOR_BchB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002789","properties":[{"key":"EntryName","value":"PRK02910.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33712","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33712:SF7","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00148","properties":[{"key":"EntryName","value":"Oxidored_nitro"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08369","properties":[{"key":"EntryName","value":"PCP_red"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000163","properties":[{"key":"EntryName","value":"PCP_ChlB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53807","properties":[{"key":"EntryName","value":"Helical backbone' metal receptor"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERDRDFTPVTASTVDRHVLARGSQEKVVENITRKGKEERPDLIVLTPTCTSSILQEDLQNFVRGASITSDSDVILADVNHYRVDELQAADGTLEQVVRYYLNKARGQGTLGRSLANIPSANIIGTSTLGFHNQHDCRELERLLRDIGIRIHQIIPEGGFVGNLHNLPKAWFNLVPYREVGLMTAVYLDEEFGMPCVSTTPAGIVDTAECIRQMQECVGKWAPVLLEEEVDYEPYIDRQTRFVSQAAWFSRSIDCQNLTGKRAVIFGDATHATAMTKILSREMGIRVCCAGTYCKHDAEWFNEQVRGFCDKVLVTDDHTEVGDMIGREEPSAIFGTQMERHVGKRLDIPCGVISSPVHIQNFPLGYRPFLGYEGTNQIADLVYNSYTLGMEDHLLDIFGGHDTERAATEPSPVEQDPLIWSPESQLGLSQIPRFVRGKIQGKTEKFARQNGITNITLEVMYAAREILGT","length":514,"molWeight":57557,"crc64":"1632401A09A0FA62","md5":"AAFE73792DC93B8F479A30A968D6BBD3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":2},"uniParcId":"UPI00063D5464"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFA8","uniProtkbId":"A0A0G2UFA8_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NAD(P)H dehydrogenase subunit 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH subunit 1"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NADH-plastoquinone oxidoreductase subunit 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}],"value":"ndhA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010535"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Belongs to the complex I subunit 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]},{"type":"Transmembrane","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000474"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29310.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028120","properties":[{"key":"ProteinId","value":"AKI29310.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UFA8","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003954","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016655","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019684","properties":[{"key":"GoTerm","value":"P:photosynthesis, light reaction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_01350","properties":[{"key":"EntryName","value":"NDH1_NuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001694","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1/FPO"}]},{"database":"InterPro","id":"IPR018086","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1_CS"}]},{"database":"NCBIfam","id":"NF004741","properties":[{"key":"EntryName","value":"nuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432:SF3","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00146","properties":[{"key":"EntryName","value":"NADHdh"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00667","properties":[{"key":"EntryName","value":"COMPLEX1_ND1_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00668","properties":[{"key":"EntryName","value":"COMPLEX1_ND1_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVIDMESDKRVTDSLQVLGFSKDDLSGFAWTGFSILTLVLVVVMGVLVIVWLERKISAGIQQRIGPGYAGPLGIIQALADGVKLLFKEDIIPSKGDPWLFSIGPAMVIAPVLVGHLVIPFGHSIVLADLGTGVLFWIAASSIAPLGLLMTGYGSNNKYSFLGGLRAAAQSISYEIPLALCVLSISLLSSSLSTVDIVEAQSKYGFWGWNLWRQPIGFVAFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLASSLFATVFYLGGWNDPLIPLYSALGFGNLSSGMTDGAAEVISAAVGIIVVLAKAYLFLFVTITARWTLPRVRMDQLLDLGWKFLLPIALGNLLLTASFQLLNLSSV","length":374,"molWeight":40315,"crc64":"DEF049D0F4D349B0","md5":"1D12103F062ABB518EEFB948861A23CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":7},"uniParcId":"UPI00063D54D2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFC0","uniProtkbId":"A0A0G2UFC0_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":38,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NAD(P)H-quinone oxidoreductase subunit K, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NAD(P)H dehydrogenase subunit K"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NADH-plastoquinone oxidoreductase subunit K"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}],"value":"ndhK"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048026"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047726"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011199"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Stromal side","id":"SL-9917"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009173"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"value":"Belongs to the complex I 20 kDa subunit family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"NADH:ubiquinone oxidoreductase-like 20kDa subunit","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01058"}]},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022957"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023078"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29320.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028130","properties":[{"key":"ProteinId","value":"AKI29320.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UFC0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045271","properties":[{"key":"GoTerm","value":"C:respiratory chain complex I"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019684","properties":[{"key":"GoTerm","value":"P:photosynthesis, light reaction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.12280:FF:000003","properties":[{"key":"EntryName","value":"NAD(P)H-quinone oxidoreductase subunit K, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12280","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01356","properties":[{"key":"EntryName","value":"NDH1_NuoB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006137","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase-like_20kDa"}]},{"database":"InterPro","id":"IPR006138","properties":[{"key":"EntryName","value":"NADH_UQ_OxRdtase_20Kd_su"}]},{"database":"NCBIfam","id":"NF005012","properties":[{"key":"EntryName","value":"nuoB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01957","properties":[{"key":"EntryName","value":"nuoB_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995:SF14","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01058","properties":[{"key":"EntryName","value":"Oxidored_q6"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56770","properties":[{"key":"EntryName","value":"HydA/Nqo6-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01150","properties":[{"key":"EntryName","value":"COMPLEX1_20K"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVLTYECFGCDNSIGNDSVNPVVNSMGRPIPGVDRAATPDSIILTTLNDFTNWARLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLIITAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTVTGGMFSTDSYSTVRGVDKLIPVDIYLPGCPPKPEAIVDAIIKLREKVSRETYDNYRDKLREGNRFFTLNHQFRIVSNMRP","length":215,"molWeight":24041,"crc64":"E1B1D0BBA8D30B1B","md5":"9062B927F92D6C2DCE08A93A722FB2B7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI00063D615E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFD0","uniProtkbId":"A0A0G2UFD0_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2015-09-16","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000619"}],"value":"Cytochrome b559 subunit alpha"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}],"value":"PSII reaction center subunit V"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}],"value":"psbE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}],"value":"This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"value":"With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004167"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004167"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}],"value":"Belongs to the PsbE/PsbF family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"}]},{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Photosystem II cytochrome b559 N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00283"}]},{"type":"Domain","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Photosystem II cytochrome b559 alpha subunit lumenal region","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00284"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","note":"ligand shared with beta subunit"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004529"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023276"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00642"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29335.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028145","properties":[{"key":"ProteinId","value":"AKI29335.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UFD0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009539","properties":[{"key":"GoTerm","value":"C:photosystem II reaction center"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009767","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport chain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.5.860","properties":[{"key":"EntryName","value":"Photosystem II cytochrome b559, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00642","properties":[{"key":"EntryName","value":"PSII_PsbE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006217","properties":[{"key":"EntryName","value":"PSII_cyt_b559_asu"}]},{"database":"InterPro","id":"IPR037025","properties":[{"key":"EntryName","value":"PSII_cyt_b559_asu_sf"}]},{"database":"InterPro","id":"IPR006216","properties":[{"key":"EntryName","value":"PSII_cyt_b559_CS"}]},{"database":"InterPro","id":"IPR013081","properties":[{"key":"EntryName","value":"PSII_cyt_b559_N"}]},{"database":"InterPro","id":"IPR013082","properties":[{"key":"EntryName","value":"PSII_cytb559_asu_lum"}]},{"database":"NCBIfam","id":"TIGR01332","properties":[{"key":"EntryName","value":"cyt_b559_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391:SF9","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00283","properties":[{"key":"EntryName","value":"Cytochrom_B559"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00284","properties":[{"key":"EntryName","value":"Cytochrom_B559a"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000036","properties":[{"key":"EntryName","value":"PsbE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161045","properties":[{"key":"EntryName","value":"Cytochrome b559 subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00537","properties":[{"key":"EntryName","value":"CYTOCHROME_B559"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGSTGERPFADIVTSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRRDIPLITGRFDSSEQIDGFTGSL","length":83,"molWeight":9251,"crc64":"65B8359015AA8C7B","md5":"5C44904821FCCA672BCBD3F7B196320B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":1,"Domain":2,"Binding site":1},"uniParcId":"UPI00063D5DEB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFH5","uniProtkbId":"A0A0G2UFH5_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":37,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017725"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Ribulose bisphosphate carboxylase large chain"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"RuBisCO large subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012287"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"4.1.1.39"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}],"value":"rbcL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025664"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO2 + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58272"}],"ecNumber":"4.1.1.39","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049469"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-3-phosphoglycerate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36631"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58033"},{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048059"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025888"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Belongs to the RuBisCO large chain family. Type I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02788"}]},{"type":"Domain","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Active site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Active site","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"in homodimeric partner","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"N6,N6,N6-trimethyllysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}]},{"type":"Disulfide bond","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Interchain; in linked form","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0113","category":"Biological process","name":"Calvin cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023300"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0120","category":"Biological process","name":"Carbon dioxide fixation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0488","category":"PTM","name":"Methylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023033"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"}],"id":"KW-0601","category":"Biological process","name":"Photorespiration"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29345.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028155","properties":[{"key":"ProteinId","value":"AKI29345.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UFH5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016984","properties":[{"key":"GoTerm","value":"F:ribulose-bisphosphate carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019253","properties":[{"key":"GoTerm","value":"P:reductive pentose-phosphate cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd08212","properties":[{"key":"EntryName","value":"RuBisCO_large_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.110:FF:000001","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.150:FF:000001","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.110","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase, large subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.150","properties":[{"key":"EntryName","value":"RuBisCO large subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01338","properties":[{"key":"EntryName","value":"RuBisCO_L_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR033966","properties":[{"key":"EntryName","value":"RuBisCO"}]},{"database":"InterPro","id":"IPR020878","properties":[{"key":"EntryName","value":"RuBisCo_large_chain_AS"}]},{"database":"InterPro","id":"IPR000685","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C"}]},{"database":"InterPro","id":"IPR036376","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C_sf"}]},{"database":"InterPro","id":"IPR017443","properties":[{"key":"EntryName","value":"RuBisCO_lsu_fd_N"}]},{"database":"InterPro","id":"IPR036422","properties":[{"key":"EntryName","value":"RuBisCO_lsu_N_sf"}]},{"database":"InterPro","id":"IPR020888","properties":[{"key":"EntryName","value":"RuBisCO_lsuI"}]},{"database":"NCBIfam","id":"NF003252","properties":[{"key":"EntryName","value":"PRK04208.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704:SF17","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00016","properties":[{"key":"EntryName","value":"RuBisCO_large"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02788","properties":[{"key":"EntryName","value":"RuBisCO_large_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01052","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00014","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00301","properties":[{"key":"EntryName","value":"RuBisCO-like_proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51649","properties":[{"key":"EntryName","value":"RuBisCo, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54966","properties":[{"key":"EntryName","value":"RuBisCO, large subunit, small (N-terminal) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00157","properties":[{"key":"EntryName","value":"RUBISCO_LARGE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSPQTETKASVGFKAGVRDYRLTYYTPDYETQATDILAAFRMTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYDIEPVPGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFKGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFVAEALNKAQAETGEIKGHYLNATAGACDEMMKRAEFARELGVPIVMHDYLTGGFTANTSLAYYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGERQVTLGFVDLLRDDYIDKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLALEGNEVIREASKWSPELAAACEVWKEIKFEFDTVDIL","length":475,"molWeight":52654,"crc64":"9CFCC23AA08CE5D2","md5":"FAEB6597D901882067E590746736BD8E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":9,"Site":1,"Modified residue":2,"Disulfide bond":1},"uniParcId":"UPI00063D54B9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UFI5","uniProtkbId":"A0A0G2UFI5_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":39,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"DNA-directed RNA polymerase subunit beta''"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"PEP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Plastid-encoded RNA polymerase subunit beta''"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"RNA polymerase subunit beta''"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}],"value":"rpoC2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Binds 1 Zn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"RNA polymerase Rpb1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05000"}]},{"type":"Domain","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"RNA polymerase Rpb1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04998"}]},{"type":"Region","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":867,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":850,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":860,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01324"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29355.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028165","properties":[{"key":"ProteinId","value":"AKI29355.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02655","properties":[{"key":"EntryName","value":"RNAP_beta'_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.132.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.390","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1790.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.274.100","properties":[{"key":"EntryName","value":"RNA polymerase Rpb1, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01324","properties":[{"key":"EntryName","value":"RNApol_bact_RpoC2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012756","properties":[{"key":"EntryName","value":"DNA-dir_RpoC2_beta_pp"}]},{"database":"InterPro","id":"IPR042102","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3_sf"}]},{"database":"InterPro","id":"IPR007083","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"}]},{"database":"InterPro","id":"IPR007081","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"}]},{"database":"InterPro","id":"IPR038120","properties":[{"key":"EntryName","value":"Rpb1_funnel_sf"}]},{"database":"NCBIfam","id":"TIGR02388","properties":[{"key":"EntryName","value":"rpoC2_cyan"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48443","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48443:SF1","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05000","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04998","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEPGQLLFCNRVMDKIAMKQFISGLTIHFGTVYTAHILDQLKTLGFQQATHAAASLGIDDLITTPSKEWLVQDAESQDWFEEQHHCYGNAHVVERLRRLIEVWYTMSEHIKMEMNPNFGMTDPLNPVHVMSFSGARGNISQIHQLLGMRGLMSNPKGQTIDLPIRSNFREGLSLAEYMISCYGARKGIVDTAVRTADAGYLTRRLVEVVQRVVVRTVDCGTIRGVTVSPVLDRQSRQMIIARSRLIGCVLADNVYVDTRCIAARDQDIGAELADQLVSFQKRPISIRSPLACKSMFWICRLCYGWSLAHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGIFTGDIAQHIRTPFTGTVMFNAANSVHYTRTPHGHPAWVCDDDLSVAIGNEYEACHLTIPSQSLIMVRNGQHVEANQVLAEIHAEKPITRDKVRKYIYSSMYGEMHLGTRVPCRNSEHCIYSSIHILPETSYVWVLSGAAPCAGGTRSIFHGGGDKIDAQSLLAGKDQSTPDSLYTGNPNTNPRYYRSDGAAAYELTTFDRRCDRGAPGNRDEDLIPLSLTRSYRVVTRGHERGGVHCLSEQRRWKCGGNGMIPRSEPFQQDVAADSSANRSGYATTEPEMIEFRATIVGSAGGRTGGMGAERPVARRHHVATEQQGGHFRSVSEDARRITHEPTCPVPRADVAQAGAQTIPSGRWSTEGAGAQSTREGSMIRISSGGNVICVTESDGASETEDTSVPPTEITYGASESVDWNHYWRRVALYTDKAFASLGRKRRRGGRRLTMEDHEIRSKSGVFEFPNWDLLEGGQRGTPKWVRAAVSCPRGEDGVGVVGDTWTRPRRSAQPRRPRILDRQKQDLAEEADTPSVEVTTSALLARYHASINRDSVGHSLMSDYGCNAGAGFQYISDARVCRPAVHSTGDNNLVLSQHGGILRVPHDRYRKRTTSLPILSSPGNACQIPLSHALARMAGGKKKPDGSDDAAIPSTANPLRNSRAFIRPHRREDKRSTRLDSEMTANAFLASSLYDSTRRMAPPETLALGLPGNNLHGMGRLAAPTHRLTRHRCLTCEVLSEDSTISKLFKTSSVLSKWFLRGEDRAYSQLLIMRERARTPARLYPSSLTQCLLPSPSCATLRSVSLGRLICEGVSVRGSGGLTSRSCQVKAINVEFAVIGLAELYLANERATVHGSSGGTIGEGDALVTLISERLRFEDIISQGLPKIEQFLESRPDTSVSTDLKDSFRDWSSGGMAWIFGRALGYLLGARTSLERSRVNLVDCIEREYRSQGVQIADKHVEMIVRQVTSKMVVLEDGMANAFLPGELIEVSRAWRMDCALEAKITCRPVLLGVTRASLNTKSFISGASFQETTRVLAGAAIRGQTDWLKGLKENVIVGRTVPAGTGCGGALRKVIPLDELEEISGTGGNPFHSAEDLSLNSAEFILRLPPSGRTIRRVSASVCYGAHTAEKRP","length":1467,"molWeight":160890,"crc64":"D578300F286D7882","md5":"3DACD6E68A7B3D10F5D805534BA24AE3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":2,"Binding site":4},"uniParcId":"UPI00063D62CA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UGT9","uniProtkbId":"A0A0G2UGT9_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2015-09-16","entryVersion":39,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"DPOR subunit L"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"LI-POR subunit L"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}],"value":"chlL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Binds 1 [4Fe-4S] cluster per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005504"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003688"}],"value":"Belongs to the NifH/BchL/ChlL family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00355"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29306.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028116","properties":[{"key":"ProteinId","value":"AKI29306.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UGT9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02032","properties":[{"key":"EntryName","value":"Bchl-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00355","properties":[{"key":"EntryName","value":"ChlL_BchL"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR030655","properties":[{"key":"EntryName","value":"NifH/chlL_CS"}]},{"database":"InterPro","id":"IPR000392","properties":[{"key":"EntryName","value":"NifH/frxC"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005971","properties":[{"key":"EntryName","value":"Protochlorophyllide_ATP-bd"}]},{"database":"NCBIfam","id":"TIGR01281","properties":[{"key":"EntryName","value":"DPOR_bchL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42864","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42864:SF2","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00142","properties":[{"key":"EntryName","value":"Fer4_NifH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000363","properties":[{"key":"EntryName","value":"Nitrogenase_iron"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00091","properties":[{"key":"EntryName","value":"NITROGNASEII"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00746","properties":[{"key":"EntryName","value":"NIFH_FRXC_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00692","properties":[{"key":"EntryName","value":"NIFH_FRXC_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51026","properties":[{"key":"EntryName","value":"NIFH_FRXC_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIAVYGKGGIGKSTTSCNISIALARRGRRVLQIGCDPKHDSTFTLTGFLIPTIIDTLRSKDYHYEDVWPEDVIYEGYGGVGCVEAGGPPAGAGCGGYVVGETVKLLKELNAFHEYDIILFDVLGDVVCGGFASPLNYADYCIVITDNGFDALFATNRITASVREKARTHPLRLAGLVGNRTSRRDLIDKYVEACPMPVLEVLPLIEHVRVSRVKGKTLFEMVESQPHLNYVCDFYLDIADQVLSQPEGIVPKEVSDRELFSLLSDFYSDPTRSQGGGNDQENLLDSVRMI","length":291,"molWeight":31976,"crc64":"2FD1CCB9CBE4665D","md5":"5522ADCBFDB534A1155D27B84E44E407"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Binding site":6},"uniParcId":"UPI00063D5D44"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UGU4","uniProtkbId":"A0A0G2UGU4_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NAD(P)H dehydrogenase, subunit 2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NADH-plastoquinone oxidoreductase subunit 2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}],"value":"ndhB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"value":"Belongs to the complex I subunit 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Transmembrane","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"NAD(P)H-quinone oxidoreductase subunit 2 N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF19530"}]},{"type":"Domain","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"NADH:quinone oxidoreductase/Mrp antiporter transmembrane","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00361"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022957"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023078"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00445"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29311.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028121","properties":[{"key":"ProteinId","value":"AKI29311.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UGU4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042773","properties":[{"key":"GoTerm","value":"P:ATP synthesis coupled electron transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006857","properties":[{"key":"GoTerm","value":"P:oligopeptide transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019684","properties":[{"key":"GoTerm","value":"P:photosynthesis, light reaction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00445","properties":[{"key":"EntryName","value":"NDH1_NuoN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010096","properties":[{"key":"EntryName","value":"NADH-Q_OxRdtase_suN/2"}]},{"database":"InterPro","id":"IPR001750","properties":[{"key":"EntryName","value":"ND/Mrp_TM"}]},{"database":"InterPro","id":"IPR045693","properties":[{"key":"EntryName","value":"Ndh2_N"}]},{"database":"InterPro","id":"IPR018456","properties":[{"key":"EntryName","value":"PTR2_symporter_CS"}]},{"database":"NCBIfam","id":"TIGR01770","properties":[{"key":"EntryName","value":"NDH_I_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22773","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19530","properties":[{"key":"EntryName","value":"Ndh2_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00361","properties":[{"key":"EntryName","value":"Proton_antipo_M"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01023","properties":[{"key":"EntryName","value":"PTR2_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MESGFDLRFLYGSTILPECILILGLIILLAIDLTSEGDTYWSYPISLTGSVTGIMVLFSQWRGEPIISLLCGPQTNTCDDIFQFLILLCLILCAPLFTEYFQCTEMAVTESLFFALAATLGGMFLCCASDLVTIFVALECSSLCFYLLSGCTSRDVRSGEATMKYLLMGGTSSSILVYGFSWLYGLSGGEVQLWGILNGLVESKMQNSEGTSIALVCIMVGIAFKLSLVPFHQWTPDVYEGLPTPVVAFLSVTSKVAALALATRIFNLFAPFSDEWHLLLEILAILSMILGNFIAIAQTSMKRMLAYSSISQIGYIMIGLIAGNPSGYASMLTYTLFYIFVNLGAFASIALFGLRTGTDSIRDCAGLYGQDPLLALCLTLCLLSLGGFPPLSGFFGKLYLFWCGWQAGLYLLVSIGLVASVISIYCYLKIIKLLMGGGHGGELDTPRTGDDRILSFSSPHTPESLIELSMMLCVIASTTLGLIMNPITTIARDNIFN","length":497,"molWeight":53917,"crc64":"72673E431EF1BB24","md5":"3A14B4FE65708DB74725962FAB980936"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":13,"Domain":2},"uniParcId":"UPI00063D5BAE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UGU9","uniProtkbId":"A0A0G2UGU9_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"Cytochrome f"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}],"value":"petA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003068"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"value":"Binds 1 heme group covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025834"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046266"}],"value":"Plastid thylakoid membrane","id":"SL-0216"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046266"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008923"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"value":"Belongs to the cytochrome f family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}]},{"type":"Chain","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Cytochrome f","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"featureId":"PRO_5008988106"},{"type":"Transmembrane","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}]},{"type":"Domain","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Cytochrome f large","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16639"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602325-50"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023078"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00610"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29321.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028131","properties":[{"key":"ProteinId","value":"AKI29321.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UGU9","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.5.700:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome f"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.830:FF:000001","properties":[{"key":"EntryName","value":"Cytochrome f"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.830","properties":[{"key":"EntryName","value":"Cytochrome f large domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.700","properties":[{"key":"EntryName","value":"Single helix bin"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00610","properties":[{"key":"EntryName","value":"Cytb6_f_cytF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024058","properties":[{"key":"EntryName","value":"Cyt-f_TM"}]},{"database":"InterPro","id":"IPR002325","properties":[{"key":"EntryName","value":"Cyt_f"}]},{"database":"InterPro","id":"IPR024094","properties":[{"key":"EntryName","value":"Cyt_f_lg_dom"}]},{"database":"InterPro","id":"IPR036826","properties":[{"key":"EntryName","value":"Cyt_f_lg_dom_sf"}]},{"database":"InterPro","id":"IPR011054","properties":[{"key":"EntryName","value":"Rudment_hybrid_motif"}]},{"database":"PANTHER","id":"PTHR33288","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33288:SF10","properties":[{"key":"EntryName","value":"CYTOCHROME F"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01333","properties":[{"key":"EntryName","value":"Apocytochr_F_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16639","properties":[{"key":"EntryName","value":"Apocytochr_F_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00610","properties":[{"key":"EntryName","value":"CYTOCHROMEF"}]},{"database":"SUPFAM","id":"SSF103431","properties":[{"key":"EntryName","value":"Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49441","properties":[{"key":"EntryName","value":"Cytochrome f, large domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51246","properties":[{"key":"EntryName","value":"Rudiment single hybrid motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51010","properties":[{"key":"EntryName","value":"CYTF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPNNTYAGVKLVTRSILILIVMSAIMARPSTSKSYPIFAQQGYENPREATGRIVCANCHLAKKPVDIEVPQSVLPDTVFEAVVRIPYDARVKQVLANGKKGALNVGAVLILPEGFKLAPPERITPEIRERVGNLFFQAYRPDKQNILVIGPVPGAKYSEIVFPILSPDPATEEGAHFLKYPIYVGGNRGRGQIYPDGSKSNNTICNASVAGRVSQILRKDKGGYEVTIDNTPDGRTVVETVPPGPELIVTEGELIKADQPLTNNPNVGGFGQGDAEIVLQDPSRVQGLLLFFASVILAQTFLVLKKKQFEKVQLAEMKNS","length":320,"molWeight":34804,"crc64":"655F04B289CA9717","md5":"CA30C8FB208A240036BB57CCE94EA702"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Domain":1,"Binding site":4},"uniParcId":"UPI00063D5651"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0G2UGV2","uniProtkbId":"A0A0G2UGV2_SELUN","entryAudit":{"firstPublicDate":"2015-09-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-09-16","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Selaginella uncinata","commonName":"Blue spike-moss","synonyms":["Lycopodium uncinatum"],"taxonId":307165,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginelloideae","Selaginella"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017774"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Photosystem I P700 chlorophyll a apoprotein A1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013197"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"PSI-A"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"PsaA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}],"value":"psaA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003162"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048912"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Belongs to the PsaA/PsaB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":535,"modifier":"EXACT"},"end":{"value":554,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":589,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":663,"modifier":"EXACT"},"end":{"value":685,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":726,"modifier":"EXACT"},"end":{"value":747,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Binding site","location":{"start":{"value":572,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":581,"modifier":"EXACT"},"end":{"value":581,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":674,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189419"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a'","id":"ChEBI:CHEBI:189419","label":"A1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":682,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"A3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":690,"modifier":"EXACT"},"end":{"value":690,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"A3"}},{"type":"Binding site","location":{"start":{"value":691,"modifier":"EXACT"},"end":{"value":691,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18067"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"phylloquinone","id":"ChEBI:CHEBI:18067","label":"A"}}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022494"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022991"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022836"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00458"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"25142065","citationType":"journal article","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"citationCrossReferences":[{"database":"PubMed","id":"25142065"},{"database":"DOI","id":"10.1261/rna.045575.114"}],"title":"Chloroplast RNA editing going extreme: more than 3400 events of C-to-U editing in the chloroplast transcriptome of the lycophyte Selaginella uncinata.","publicationDate":"2014","journal":"RNA","firstPage":"1499","lastPage":"1506","volume":"20"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}]},{"referenceNumber":2,"citation":{"id":"CI-4BH5RILM246BE","citationType":"submission","authors":["Oldenkott B.","Yamaguchi K.","Tsuji-Tsukinoki S.","Knie N.","Knoop V."],"publicationDate":"MAR-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKI29326.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KR028136","properties":[{"key":"ProteinId","value":"AKI29326.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0G2UGV2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.1130.10:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I P700 chlorophyll a apoprotein A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1130.10","properties":[{"key":"EntryName","value":"Photosystem I PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00458","properties":[{"key":"EntryName","value":"PSI_PsaA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006243","properties":[{"key":"EntryName","value":"PSI_PsaA"}]},{"database":"InterPro","id":"IPR001280","properties":[{"key":"EntryName","value":"PSI_PsaA/B"}]},{"database":"InterPro","id":"IPR020586","properties":[{"key":"EntryName","value":"PSI_PsaA/B_CS"}]},{"database":"InterPro","id":"IPR036408","properties":[{"key":"EntryName","value":"PSI_PsaA/B_sf"}]},{"database":"NCBIfam","id":"TIGR01335","properties":[{"key":"EntryName","value":"psaA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN, OMPA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128:SF19","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00223","properties":[{"key":"EntryName","value":"PsaA_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002905","properties":[{"key":"EntryName","value":"PSI_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00257","properties":[{"key":"EntryName","value":"PHOTSYSPSAAB"}]},{"database":"SUPFAM","id":"SSF81558","properties":[{"key":"EntryName","value":"Photosystem I subunits PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00419","properties":[{"key":"EntryName","value":"PHOTOSYSTEM_I_PSAAB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIRPVEPGIGIAVGTDPVNTSFEEWSKPGHFSRTLAKGPNTTTWIWDLHADVHDFDSHTNDLEDISRKVFSAHFGQLAIIFVWLSGMYFHGARFSNYEAWLSDPIHIKPSAQVVWPIVGQEVLNGDVGGGFQGIQITSGFFQVWRASGITSELQLYSTAIGGLIFAALMLFAGWFHYHRAAPQLAWFQSVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQLLGIGVDAKEIPLPHEFILDRHLLAQLYPGFAKGLTPFFTLNWSEYSDFLTFRGGLDPVTGGLWLTDTAHHHLAIAVVFLIAGHVYRTNWGIGHSPKEVLEAHKGPFTGEGHKGLYGILTTSWHAQLALNLAMLGSLTILVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTQCNNLLDRVLRHRDAIISHLNWACIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAMRLQPIFAQWVQNAHASAPVLTAPAANTATSLAWGGGVLAMGGKVVLSAIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLVPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGSVNDQGIVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLLFLGAHFVWAFSLMFLFSGRGYWQELIESVVWAHNKLRVAPAIQPRALSIVQGRAVGVAHYLLGGIATTWAFFLARIIAVG","length":749,"molWeight":82468,"crc64":"BCF260775A0843FF","md5":"BD8220985A583D610254657738E4FF29"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":9,"Binding site":6},"uniParcId":"UPI00063D55AC"}}]}