C550A_CYACA
ID C550A_CYACA Reviewed; 164 AA.
AC Q9TLW2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE Flags: Precursor;
GN Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01378};
CC Note=Binds 1 heme c group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01378};
CC -!- SUBUNIT: The oxygen-evolving complex in red algae is composed of psbO
CC (OEC33), psbQ', cytochrome c-550 and psbU. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01378}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01378}; Lumenal side {ECO:0000255|HAMAP-
CC Rule:MF_01378}. Note=Associated with photosystem II at the lumenal side
CC of the thylakoid membrane. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01378}.
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; AF022186; AAF12938.1; -; Genomic_DNA.
DR RefSeq; NP_045156.1; NC_001840.1.
DR AlphaFoldDB; Q9TLW2; -.
DR SMR; Q9TLW2; -.
DR GeneID; 800220; -.
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; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Plastid; Signal; Thylakoid; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT CHAIN 28..164
FT /note="Cytochrome c-550"
FT /id="PRO_0000006514"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 68
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 119
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
SQ SEQUENCE 164 AA; 18212 MW; 38828BA2920913C5 CRC64;
MNRISIYRIK VLAFLFAVST YVYPASSLEL NEEARTVKLN SEGQSLTLNE EQIKKGKRLF
NSHCGSCHVG GITKTNPNVG LDLESLNGAN PPRNNINALV EYMKDPKTYD GSESIAEIHP
SIKSADIFPK MRDLSDDDLK VIAGHILVQP KINSEKWGGG KIYY