ID M5DBK0_CHOCR Unreviewed; 163 AA.
AC M5DBK0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 02-DEC-2020, entry version 34.
DE SubName: Full=Cytochrome c550 {ECO:0000313|EMBL:CCP38047.1};
DE Flags: Precursor;
GN Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378,
GN ECO:0000313|EMBL:CCP38047.1};
GN ORFNames=CHC_60 {ECO:0000313|EMBL:CCP38047.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OG Plastid {ECO:0000313|EMBL:CCP38047.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CCP38047.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|EMBL:CCP38047.1, ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23536846; DOI=10.1371/journal.pone.0059001;
RA Janouskovec J., Liu S.-L., Martone P.T., Carre W., Leblanc C., Collen J.,
RA Keeling P.J.;
RT "Evolution of red algal plastid genomes: ancient architectures, introns,
RT horizontal gene transfer, and taxonomic utility of plastid markers.";
RL PLoS ONE 8:e59001-e59001(2013).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01378};
CC Note=Binds 1 heme group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01378};
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- SUBUNIT: The oxygen-evolving complex in red algae is composed of psbO
CC (OEC33), psbQ', cytochrome c-550 and psbU.
CC {ECO:0000256|ARBA:ARBA00011619}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01378}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01378}; Lumenal side {ECO:0000256|HAMAP-Rule:MF_01378}.
CC Note=Associated with photosystem II at the lumenal side of the
CC thylakoid membrane. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000256|ARBA:ARBA00010433, ECO:0000256|HAMAP-Rule:MF_01378}.
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DR EMBL; HF562234; CCP38047.1; -; Genomic_DNA.
DR RefSeq; YP_007627300.1; NC_020795.1.
DR EnsemblPlants; CCP38047; CCP38047; CHC_60.
DR GeneID; 14971012; -.
DR Gramene; CCP38047; CCP38047; CHC_60.
DR KEGG; ccp:CHC_60; -.
DR OMA; DYMKDPT; -.
DR OrthoDB; 1454992at2759; -.
DR Proteomes; UP000012073; Plastid.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IEA:UniProtKB-UniRule.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 1.
DR HAMAP; MF_01378; PSII_Cyt550; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR029490; Cytochrom_C550.
DR InterPro; IPR016003; PSII_cyt_c550.
DR InterPro; IPR017851; PSII_PsbV_cyt_c550.
DR Pfam; PF14495; Cytochrom_C550; 1.
DR PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR TIGRFAMs; TIGR03045; PS_II_C550; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01378};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01378,
KW ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01378,
KW ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01378};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01378, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01378};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_01378}; Plastid {ECO:0000313|EMBL:CCP38047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012073};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01378};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT CHAIN 27..163
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT /id="PRO_5009017464"
FT DOMAIN 50..149
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT METAL 67
FT /note="Iron (heme axial ligand)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT METAL 118
FT /note="Iron (heme axial ligand)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 63
FT /note="Heme (covalent)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 66
FT /note="Heme (covalent)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
SQ SEQUENCE 163 AA; 18115 MW; 695EDCB4158AD28F CRC64;
MLINNIWRSF AITSLIFGIL LKPVQAIELD EITRTVQLEE SGKTIILTRE QVKRGKRLFN
NSCAQCHNGG ITKTNPNIGL ELESLSLATP ARDNISSLIN YMKDPTSYDG ATSIAELHPS
IKSAEIFPKM RNLTDDDLFA IAGHILIQPK IVAEKWGGGK IYY
//
