ID D9IXJ6_9ALVE Unreviewed; 160 AA.
AC D9IXJ6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Photosystem II extrinsic protein V {ECO:0000256|HAMAP-Rule:MF_01378};
DE Short=PsbV {ECO:0000256|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c-550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c550 {ECO:0000256|HAMAP-Rule:MF_01378};
GN Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378,
GN ECO:0000313|EMBL:ADJ66524.1};
OS Chromera velia.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADJ66524.1}.
OC Eukaryota; Sar; Alveolata; Colpodellida; Chromeraceae; Chromera.
OX NCBI_TaxID=505693 {ECO:0000313|EMBL:ADJ66524.1};
RN [1] {ECO:0000313|EMBL:ADJ66524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2878 {ECO:0000313|EMBL:ADJ66524.1};
RX PubMed=20534454; DOI=10.1073/pnas.1003335107;
RA Janouskovec J., Horak A., Obornik M., Lukes J., Keeling P.J.;
RT "A common red algal origin of the apicomplexan, dinoflagellate, and
RT heterokont plastids.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10949-10954(2010).
RN [2] {ECO:0000313|EMBL:ADJ66524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2878 {ECO:0000313|EMBL:ADJ66524.1};
RA Janouskovec J., Sobotka R., Lai D.-H., Flegontov P., Konik P., Komenda J.,
RA Ali S., Prasil O., Pain A., Obornik M., Lukes J., Keeling P.J.;
RT "Split photosystem protein, linear topology, and growth of structural
RT complexity in the recombination-driven plastid genome of Chromera velia.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the extrinsic, lumenal subunits of photosystem II
CC (PSII). PSII is a light-driven water plastoquinone oxidoreductase,
CC using light energy to abstract electrons from H(2)O, generating a
CC proton gradient subsequently used for ATP formation. The extrinsic
CC proteins stabilize the structure of photosystem II oxygen-evolving
CC complex (OEC), the ion environment of oxygen evolution and protect the
CC OEC against heat-induced inactivation. Low-potential cytochrome c that
CC plays a role in the OEC of PSII. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01378};
CC Note=Binds 1 heme c group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01378};
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {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; HM222967; ADJ66524.1; -; Genomic_DNA.
DR RefSeq; YP_003795282.1; NC_014340.2.
DR AlphaFoldDB; D9IXJ6; -.
DR GeneID; 9480909; -.
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: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; Cytochrome c-like domain; 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; IPR017851; PsbV_cyt_c550.
DR InterPro; IPR016003; PsbV_cyt_c550-like.
DR Pfam; PF14495; Cytochrom_C550; 1.
DR PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:ADJ66524.1};
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01378};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01378};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01378};
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};
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:ADJ66524.1};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT DOMAIN 47..146
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 60
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 64
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:0000256|HAMAP-Rule:MF_01378"
FT BINDING 115
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:0000256|HAMAP-Rule:MF_01378"
SQ SEQUENCE 160 AA; 17867 MW; 2A77A26154666481 CRC64;
MTERVFISED VFFSIPKILI YLNRSLTDSI RTVKLSENND KAIITPNELG RGKVLFAKTC
SACHTGGITK TNPNIGLALS TLKNAIPERD NVVNLVQYMK YPTAYDGTFT LNETHPNTTF
AVFFPSMRTL TEKDLYSIAG YILVQAQVLG EKWGGGKVYY
//
