ID A0A2S1RIH3_9MAGN Unreviewed; 473 AA. AC A0A2S1RIH3; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 08-MAY-2019, entry version 6. DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00198301}; DE AltName: Full=PSII 43 kDa protein {ECO:0000256|HAMAP-Rule:MF_01496}; DE AltName: Full=Protein CP-43 {ECO:0000256|HAMAP-Rule:MF_01496}; GN Name=psbC {ECO:0000256|HAMAP-Rule:MF_01496, GN ECO:0000313|EMBL:AWH99627.1}; GN ORFNames=CU047_0029 {ECO:0000313|EMBL:AWH99627.1}; OS Dysosma difformis. OG Plastid; Chloroplast {ECO:0000313|EMBL:AWH99627.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Ranunculales; Berberidaceae; OC Berberidoideae; Dysosma. OX NCBI_TaxID=335806 {ECO:0000313|EMBL:AWH99627.1}; RN [1] {ECO:0000313|EMBL:AWH99627.1} RP NUCLEOTIDE SEQUENCE. RA Ye W.Q.; RT "Plastome organization, genome-based phylogeny and evolution of RT plastid genes in Podophylloideae species adapted to contrasting RT habitats."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: One of the components of the core complex of photosystem CC II (PSII). It binds chlorophyll and helps catalyze the primary CC light-induced photochemical processes of PSII. PSII is a light- CC driven water:plastoquinone oxidoreductase, using light energy to CC abstract electrons from H(2)O, generating O(2) and a proton CC gradient subsequently used for ATP formation. {ECO:0000256|HAMAP- CC Rule:MF_01496, ECO:0000256|RuleBase:RU004533, CC ECO:0000256|SAAS:SAAS00944813}. CC -!- COFACTOR: CC Note=Binds multiple chlorophylls and provides some of the ligands CC for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may CC also provide a ligand for a Cl- that is required for oxygen CC evolution. PSII binds additional chlorophylls, carotenoids and CC specific lipids. {ECO:0000256|HAMAP-Rule:MF_01496}; CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins CC PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, CC PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral CC proteins of the oxygen-evolving complex and a large number of CC cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP- CC Rule:MF_01496, ECO:0000256|RuleBase:RU004533}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01496, CC ECO:0000256|RuleBase:RU004533}. CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01496, ECO:0000256|RuleBase:RU004533, CC ECO:0000256|SAAS:SAAS00569542}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG593056; AWH99627.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule. DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR HAMAP; MF_01496; PSII_PsbC_CP43; 1. DR InterPro; IPR000932; PS_antenna-like. DR InterPro; IPR036001; PS_II_antenna-like_sf. DR InterPro; IPR005869; PSII_PsbC. DR PANTHER; PTHR33180; PTHR33180; 1. DR Pfam; PF00421; PSII; 1. DR SUPFAM; SSF161077; SSF161077; 1. DR TIGRFAMs; TIGR01153; psbC; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_01496}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944814}; KW Chloroplast {ECO:0000256|RuleBase:RU004533, KW ECO:0000313|EMBL:AWH99627.1}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944827}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00198307}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944818, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00198298}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01496}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944815}; KW Photosystem II {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00198310}; KW Plastid {ECO:0000256|RuleBase:RU004533, ECO:0000313|EMBL:AWH99627.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|RuleBase:RU004533, ECO:0000256|SAAS:SAAS00944816, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01496, KW ECO:0000256|SAAS:SAAS00944822, ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 233 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 292 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 367 367 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01496}. FT METAL 367 367 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000256|HAMAP-Rule: FT MF_01496}. FT MOD_RES 15 15 N-acetylthreonine. {ECO:0000256|HAMAP- FT Rule:MF_01496}. FT MOD_RES 15 15 Phosphothreonine. {ECO:0000256|HAMAP- FT Rule:MF_01496}. SQ SEQUENCE 473 AA; 51894 MW; 85665AD1249E8DDF CRC64; MKTLYSPRRF YPVETLFNGT LALAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI SSAVLGFGGI YHSLLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGL GAFLLVLKAL YFGGIYDTWA PGGGDVRKIT NLTLSPSVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL GSICIFGGIW HILTKPFAWA RRALVWSGEA YLSYSLAALS IFGFTACCFV WFNNTAYPSE FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV SPRSWLSTSH FVLGFFLFVG HLWHAGRARA AAAGFEKGID RDLEPVLFMT PLN //