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Database: UniProt
Entry: D1J771_ECTSI
LinkDB: D1J771_ECTSI
Original site: D1J771_ECTSI 
ID   D1J771_ECTSI            Unreviewed;       161 AA.
AC   D1J771;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   12-AUG-2020, entry version 54.
DE   RecName: Full=Cytochrome c-550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE   AltName: Full=Cytochrome c550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE   Flags: Precursor;
GN   Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378,
GN   ECO:0000313|EMBL:CAV31255.1};
GN   ORFNames=Es_cpDNA_112 {ECO:0000313|EMBL:CAV31255.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:CAV31255.1}.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CAV31255.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAV31255.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=19835607; DOI=10.1186/1471-2148-9-253;
RA   Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
RA   Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
RA   Leblanc C.;
RT   "Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
RT   vesiculosus: further insights on the evolution of red-algal derived
RT   plastids.";
RL   BMC Evol. Biol. 9:253-253(2009).
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: Part of the oxygen-evolving complex of photosystem II.
CC       {ECO:0000256|HAMAP-Rule:MF_01378}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01378}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01378}; Lumenal side {ECO:0000256|HAMAP-
CC       Rule:MF_01378}. Note=Associated with photosystem II at the lumenal side
CC       of the 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; FP102343; CAT18794.1; -; Genomic_DNA.
DR   EMBL; FP102296; CAV31255.1; -; Genomic_DNA.
DR   RefSeq; YP_003289224.1; NC_013498.1.
DR   STRING; 2880.D1J771; -.
DR   GeneID; 8594951; -.
DR   eggNOG; ENOG502RYSJ; Eukaryota.
DR   Proteomes; UP000002630; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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   Chloroplast {ECO:0000313|EMBL:CAV31255.1};
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:CAV31255.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
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..24
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   CHAIN           25..161
FT                   /note="Cytochrome c-550"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT                   /id="PRO_5009009144"
FT   DOMAIN          48..147
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   METAL           65
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   METAL           116
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         61
FT                   /note="Heme (covalent)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         64
FT                   /note="Heme (covalent)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
SQ   SEQUENCE   161 AA;  17583 MW;  E60E042D95EAEA7D CRC64;
     MFKKFFTSLI IVSLLNLGTS SVLAIELDEA TRTIPATSDG KTIVLTPEQV KRGKRLFNSS
     CGQCHVGGIT KTNPNLGLDT EALSLATPSR NNITGLVDYM KNPTTYDGLE SIAEIHPSIK
     SANIFTRMRS LDENDLVDIA GHILLQPKIL SEKWGGGKIY Y
//
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