{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B2D2G5","uniProtkbId":"B2D2G5_CAPSN","entryAudit":{"firstPublicDate":"2008-05-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2008-05-20","entryVersion":54,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70177.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70177.1"}],"value":"70 kDa heat shock protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70177.1"}],"value":"hsp70"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061042"}],"value":"Belongs to the heat shock protein 70 (TC 1.A.33) family. DnaK subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007381"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"value":"Belongs to the heat shock protein 70 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":649,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003322"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70177.1"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7LUVBSA2TAOO8","citationType":"submission","authors":["Luan D.","Dong Y."],"title":"Cloning and sequence analysis of the gene encoding 70kd heat shock protein of Cappairs spinosa.","publicationDate":"MAR-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70177.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"EU574936","properties":[{"key":"ProteinId","value":"ACB70177.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"B2D2G5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006457","properties":[{"key":"GoTerm","value":"P:protein folding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009408","properties":[{"key":"GoTerm","value":"P:response to heat"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd10233","properties":[{"key":"EntryName","value":"ASKHA_NBD_HSP70_HSPA1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.34.10:FF:000002","properties":[{"key":"EntryName","value":"Heat shock 70 kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.640.10:FF:000002","properties":[{"key":"EntryName","value":"Heat shock 70 kDa"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1270.10:FF:000028","properties":[{"key":"EntryName","value":"Heat shock 70 kDa protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.30.30:FF:000019","properties":[{"key":"EntryName","value":"Heat shock 70 kDa protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000028","properties":[{"key":"EntryName","value":"heat shock 70 kDa protein-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.40:FF:000465","properties":[{"key":"EntryName","value":"Heat shock cognate 70 kDa protein 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.30.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.640.10","properties":[{"key":"EntryName","value":"Actin, Chain A, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.34.10","properties":[{"key":"EntryName","value":"Substrate Binding Domain Of DNAk, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR018181","properties":[{"key":"EntryName","value":"Heat_shock_70_CS"}]},{"database":"InterPro","id":"IPR029048","properties":[{"key":"EntryName","value":"HSP70_C_sf"}]},{"database":"InterPro","id":"IPR029047","properties":[{"key":"EntryName","value":"HSP70_peptide-bd_sf"}]},{"database":"InterPro","id":"IPR013126","properties":[{"key":"EntryName","value":"Hsp_70_fam"}]},{"database":"NCBIfam","id":"NF001413","properties":[{"key":"EntryName","value":"dnaK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19375","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 70KDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00012","properties":[{"key":"EntryName","value":"HSP70"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00301","properties":[{"key":"EntryName","value":"HEATSHOCK70"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF100934","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100920","properties":[{"key":"EntryName","value":"Heat shock protein 70kD (HSP70), peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00297","properties":[{"key":"EntryName","value":"HSP70_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00329","properties":[{"key":"EntryName","value":"HSP70_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01036","properties":[{"key":"EntryName","value":"HSP70_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPINTVFDAKRLIGRRYSDSSVQADMKLWPFKVVPGSGDKPMIVVNYKGEEKQFAAEEISSMVLIKMREIAEAFLGCTIKNGVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKAASVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKRDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLYEGIDFYTTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSNVHDIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIPRNTTIPTKKEQIFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELTGIPPAPRGVPQINVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKEEIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIKDEKIGSKLDPADKKKIEDAIDQAIQWLDGNQLAEADEFKDKMKELESICNPIIARMYQGAGGDMGGAGGADDASPAGGSGAGPKIEEVD","length":649,"molWeight":71045,"crc64":"A4716ACFC24B31BE","md5":"CBFBC6CA5FE42DAD7A9D2D8F2385A7D3"},"extraAttributes":{"countByCommentType":{"SIMILARITY":2},"countByFeatureType":{"Region":1,"Compositional bias":1},"uniParcId":"UPI000172CADD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q7YNU8","uniProtkbId":"Q7YNU8_CAPSN","entryAudit":{"firstPublicDate":"2003-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2003-10-01","entryVersion":89,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017725"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Ribulose bisphosphate carboxylase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012287"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"4.1.1.39"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}],"value":"rbcL"}}],"comments":[{"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":"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":"RuleBase","id":"RU000302"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Heterohexadecamer of 8 large chains and 8 small chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004229"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006204"}],"value":"Belongs to the RuBisCO large chain family. Type I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":135,"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":145,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Modified residue","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022567"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0113","category":"Biological process","name":"Calvin cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023300"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0120","category":"Biological process","name":"Carbon dioxide fixation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023033"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"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":"ARBA00023238"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0601","category":"Biological process","name":"Photorespiration"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"12695853","citationType":"journal article","authors":["Cummings M.P.","Nugent J.M.","Olmstead R.G.","Palmer J.D."],"citationCrossReferences":[{"database":"PubMed","id":"12695853"}],"title":"Phylogenetic analysis reveals five independent transfers of the chloroplast gene rbcL to the mitochondrial genome in angiosperms.","publicationDate":"2003","journal":"Curr. Genet.","firstPage":"131","lastPage":"138","volume":"43"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAO38788.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY167985","properties":[{"key":"ProteinId","value":"AAO38788.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"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:InterPro"}]},{"database":"GO","id":"GO:0016984","properties":[{"key":"GoTerm","value":"F:ribulose-bisphosphate carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0015977","properties":[{"key":"GoTerm","value":"P:carbon fixation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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:SF16","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":"SVGFKAGVKEYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVPGEENQYIAYVAYPLDLFXEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYTKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQDETGEIKGHYLNATAGTCEEMIKRAVCARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGDRESTLGFVDLLRDDFVEKDRSRGIFFTQDWVSIPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAVEGNEIIREASKWSAELAAA","length":449,"molWeight":49469,"crc64":"6002A70500675A67","md5":"714631292F33F5ECC33FE49D2CEBF206"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Binding site":1,"Modified residue":1,"Non-terminal residue":2},"uniParcId":"UPI000019ADE7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0H4JN20","uniProtkbId":"A0A0H4JN20_CAPSN","entryAudit":{"firstPublicDate":"2015-10-14","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2015-10-14","entryVersion":29,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}],"value":"Heat shock protein 90"}}],"flag":"Fragment"},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008239"}],"value":"Belongs to the heat shock protein 90 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-76FD7KCI146B4","citationType":"submission","authors":["Elmi Z.","Shariati M.","Hosseini Tafreshi S.A."],"title":"Study of the role of hsp genes of Capparis spinosa L. in resistance to salinity stress in Nicotiana bentamiana by using heterologous virus induced gene silencing (VIGS).","publicationDate":"JAN-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AKO69721.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KP718612","properties":[{"key":"ProteinId","value":"AKO69721.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0H4JN20","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A0H4JN20","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140662","properties":[{"key":"GoTerm","value":"F:ATP-dependent protein folding chaperone"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.30.230.80:FF:000001","properties":[{"key":"EntryName","value":"Heat shock protein 90 alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.80","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.11260","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR001404","properties":[{"key":"EntryName","value":"Hsp90_fam"}]},{"database":"InterPro","id":"IPR020575","properties":[{"key":"EntryName","value":"Hsp90_N"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"PANTHER","id":"PTHR11528","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 90 FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00183","properties":[{"key":"EntryName","value":"HSP90"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00775","properties":[{"key":"EntryName","value":"HEATSHOCK90"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"LVAGKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGENLGRGTKMTLFLKEDQLEYLEERRLKDLIKKHSEFISYPISLWVEKTIEKEISDDEDEEEKKDEEGKVEEVDEEKEKEEKKKKKIKEVSHEWSLVNKQKPIWMRKPEEITKEEYAAFYKSLTNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTRKKPNNIKLYVRRVFIMDNCEELMPEYLGFVKGIVDSEDLPLNISREMLQQNKILKVIRKNLVKKCIELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQ","length":330,"molWeight":39049,"crc64":"D98C1013EB847E25","md5":"F0CE5B0AD7D0EA293AB95434D7EAAB1A"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Non-terminal residue":2},"uniParcId":"UPI00065B33DB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A513U7Z7","uniProtkbId":"A0A513U7Z7_CAPSN","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2019-10-16","entryVersion":10,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}],"value":"4-coumarate--CoA ligase"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}],"value":"4CL"}}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"AMP-dependent synthetase/ligase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00501"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7K3P89UNO0B89","citationType":"submission","authors":["Kianersi F.","Abdollahi M.R.","Mirzaie-Asl A.","Dastan D."],"title":"Identification and expression analysis of some rutin biosynthesis-related genes in different tissues of capper (Capparis spinosa) under elicitation of salicylic acid and methyl jasmonate.","publicationDate":"DEC-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}],"value":"Leaf","type":"TISSUE"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10105.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MK301444","properties":[{"key":"ProteinId","value":"QDG10105.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A513U7Z7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016405","properties":[{"key":"GoTerm","value":"F:CoA-ligase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.980","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.38.10","properties":[{"key":"EntryName","value":"Luciferase, Domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000873","properties":[{"key":"EntryName","value":"AMP-dep_synth/lig_dom"}]},{"database":"PANTHER","id":"PTHR24096:SF251","properties":[{"key":"EntryName","value":"4-COUMARATE--COA LIGASE-LIKE 9"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24096","properties":[{"key":"EntryName","value":"LONG-CHAIN-FATTY-ACID--COA LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00501","properties":[{"key":"EntryName","value":"AMP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56801","properties":[{"key":"EntryName","value":"Acetyl-CoA synthetase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"FPQWSLLQGYGLTESTGPVAKTWGPVETERYGSTGRLCVNMEANIVDPASKKALPPGQKGELWLR","length":65,"molWeight":7118,"crc64":"9F9972D292552FF7","md5":"674FF693973F59DF04F1E4CC29F545B4"},"extraAttributes":{"countByFeatureType":{"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0011623B79"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A513U861","uniProtkbId":"A0A513U861_CAPSN","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":9,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}],"value":"Flavonol 3-O-glucoside rhamnosyltransferase"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}],"value":"RT"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009995"}],"value":"Belongs to the UDP-glycosyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7K3P89UNO0B89","citationType":"submission","authors":["Kianersi F.","Abdollahi M.R.","Mirzaie-Asl A.","Dastan D."],"title":"Identification and expression analysis of some rutin biosynthesis-related genes in different tissues of capper (Capparis spinosa) under elicitation of salicylic acid and methyl jasmonate.","publicationDate":"DEC-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}],"value":"Leaf","type":"TISSUE"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QDG10106.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MK301445","properties":[{"key":"ProteinId","value":"QDG10106.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A513U861","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.1.159","properties":[{"key":"OrganismId","value":"20539"}]},{"database":"GO","id":"GO:0035251","properties":[{"key":"GoTerm","value":"F:UDP-glucosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050481","properties":[{"key":"EntryName","value":"UDP-glycosyltransf_plant"}]},{"database":"PANTHER","id":"PTHR48049","properties":[{"key":"EntryName","value":"GLYCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48049:SF91","properties":[{"key":"EntryName","value":"UDP-GLYCOSYLTRANSFERASE 79B7-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"KKAQLQLQHLNIHPDYIVFRSVTVPSVEGLPSGVETASDIPISMTDLLVTAMDLTRDQFEAVVRSVKPDLIFYDFAHWVPEVAKEFGIKTVLYVVVSAASVAISLVPARGITRDKPVTVEEVAVPPPGYPSSKVTLRRNEAHALLFLSFPFGQGTTFFERSTLALHKCDVISIRTYKELEGKYCDYIESQYKKKVLLTGPILPQPDITKQLEDQWSKWLSGFESSSVVFCAFGSQITLEKDQFQELCLGFELSGSPFLVALKPPTG","length":266,"molWeight":29571,"crc64":"FCBB53EA7284069F","md5":"5A8FF438701438B56E513D8C59EA0187"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Non-terminal residue":2},"uniParcId":"UPI0011620D70"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B2D2G4","uniProtkbId":"B2D2G4_CAPSN","entryAudit":{"firstPublicDate":"2008-05-20","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2008-05-20","entryVersion":40,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Capparis spinosa","commonName":"Caper","taxonId":65558,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70176.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Capparaceae","Capparis"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70176.1"}],"value":"Small heat shock protein"}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00285"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003616"}],"value":"Belongs to the small heat shock protein (HSP20) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"SHSP","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS01031"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70176.1"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AOMBF3PD79TAI","citationType":"submission","authors":["Luan D.","Dong Y."],"title":"Cloning and sequence analysis of the gene encoding a small heat shock protein of Capparis spinosa.","publicationDate":"MAR-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACB70176.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"EU574935","properties":[{"key":"ProteinId","value":"ACB70176.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"B2D2G4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009408","properties":[{"key":"GoTerm","value":"P:response to heat"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06464","properties":[{"key":"EntryName","value":"ACD_sHsps-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.790:FF:000059","properties":[{"key":"EntryName","value":"26.5 kDa heat shock protein, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.790","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002068","properties":[{"key":"EntryName","value":"A-crystallin/Hsp20_dom"}]},{"database":"InterPro","id":"IPR008978","properties":[{"key":"EntryName","value":"HSP20-like_chaperone"}]},{"database":"InterPro","id":"IPR044587","properties":[{"key":"EntryName","value":"HSP21-like"}]},{"database":"PANTHER","id":"PTHR46733","properties":[{"key":"EntryName","value":"26.5 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46733:SF4","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 21, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00011","properties":[{"key":"EntryName","value":"HSP20"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49764","properties":[{"key":"EntryName","value":"HSP20-like chaperones"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01031","properties":[{"key":"EntryName","value":"SHSP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASTLTVSSGSPLVSPTSRRATSKAVGSCSVSFPRRDSRRLSVVRAQDHKDNSVDVRVNKDNQGSAVEKSPRRLAVDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDAMTVPGRNRGGGEVRAPWDIKDDEHEIKMRFDMPGLSKDDVKVSVEDDILAIRGEHKKEEDGTDDSWSSRSYSSYDTRLSKLPDNCEKDKIKAELKNGVLLISIPKAKVDRKVIDVQIQ","length":225,"molWeight":25119,"crc64":"460F6D2288409FF7","md5":"AE8E8799B13B5802503F17622EC38BDD"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":3},"uniParcId":"UPI000172CADC"}}]}