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Database: UniProt
Entry: M5DBK0_CHOCR
LinkDB: M5DBK0_CHOCR
Original site: M5DBK0_CHOCR 
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
//
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