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Entry: R9ZTQ5_9EUKA
LinkDB: R9ZTQ5_9EUKA
Original site: R9ZTQ5_9EUKA 
ID   R9ZTQ5_9EUKA            Unreviewed;       163 AA.
AC   R9ZTQ5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
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};
DE   Flags: Precursor;
GN   Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378,
GN   ECO:0000313|EMBL:AGO44890.1};
OS   Phaeocystis globosa.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AGO44890.1}.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Phaeocystales;
OC   Phaeocystaceae; Phaeocystis.
OX   NCBI_TaxID=33658 {ECO:0000313|EMBL:AGO44890.1};
RN   [1] {ECO:0000313|EMBL:AGO44890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Pg-G {ECO:0000313|EMBL:AGO44890.1};
RX   PubMed=24216019; DOI=10.1016/j.ympev.2013.10.018;
RA   Smith D.R., Arrigo K.R., Alderkamp A.C., Allen A.E.;
RT   "Massive difference in synonymous substitution rates among mitochondrial,
RT   plastid, and nuclear genes of Phaeocystis algae.";
RL   Mol. Phylogenet. Evol. 71:36-40(2014).
RN   [2] {ECO:0000313|EMBL:QRN72635.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNS00062 {ECO:0000313|EMBL:QRN72635.1}, CNS00063
RC   {ECO:0000313|EMBL:QRN72743.1}, CNS00064 {ECO:0000313|EMBL:QRN72851.1},
RC   CNS00065 {ECO:0000313|EMBL:QRN72959.1}, CNS00066
RC   {ECO:0000313|EMBL:QRN73067.1}, CNS00075 {ECO:0000313|EMBL:QRN73283.1},
RC   CNS00076 {ECO:0000313|EMBL:QRN73391.1}, CNS00079
RC   {ECO:0000313|EMBL:QRN73499.1}, CNS00080 {ECO:0000313|EMBL:QRN73607.1},
RC   CNS00087 {ECO:0000313|EMBL:QRN73715.1}, and CNS00093
RC   {ECO:0000313|EMBL:QRN73823.1};
RA   Song H., Chen N.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QRN73175.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNS00067 {ECO:0000313|EMBL:QRN73175.1};
RX   PubMed=33218437;
RA   Song H., Liu F., Li Z., Xu Q., Chen Y., Yu Z., Chen N.;
RT   "Development of a high-resolution molecular marker for tracking Phaeocystis
RT   globosa genetic diversity through comparative analysis of chloroplast
RT   genomes.";
RL   Harmful Algae 99:0-0(0).
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; KC900889; AGO44890.1; -; Genomic_DNA.
DR   EMBL; MT471323; QRN72635.1; -; Genomic_DNA.
DR   EMBL; MT471324; QRN72743.1; -; Genomic_DNA.
DR   EMBL; MT471325; QRN72851.1; -; Genomic_DNA.
DR   EMBL; MT471326; QRN72959.1; -; Genomic_DNA.
DR   EMBL; MT471327; QRN73067.1; -; Genomic_DNA.
DR   EMBL; MT471328; QRN73175.1; -; Genomic_DNA.
DR   EMBL; MT471329; QRN73283.1; -; Genomic_DNA.
DR   EMBL; MT471330; QRN73391.1; -; Genomic_DNA.
DR   EMBL; MT471331; QRN73499.1; -; Genomic_DNA.
DR   EMBL; MT471332; QRN73607.1; -; Genomic_DNA.
DR   EMBL; MT471333; QRN73715.1; -; Genomic_DNA.
DR   EMBL; MT471334; QRN73823.1; -; Genomic_DNA.
DR   RefSeq; YP_008145428.1; NC_021637.1.
DR   AlphaFoldDB; R9ZTQ5; -.
DR   GeneID; 16028665; -.
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   NCBIfam; TIGR03045; PS_II_C550; 1.
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:AGO44890.1};
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:AGO44890.1};
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                   /note="Photosystem II extrinsic protein V"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT                   /id="PRO_5034793077"
FT   DOMAIN          50..149
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
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         66
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         67
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         118
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   163 AA;  17717 MW;  D7A1889964B08D89 CRC64;
     MLKNKFLLGS ILATFVLGTH ISAANALELD EDTRTVTLDS KGNTVVISVE QVKRGKRLFN
     NACGTCHVGG VTKTNPNVGL DVESLSLATP ARDNVTNLVS YFKDPMSYDG TDSISEIHPS
     IKSADIFPKM RSLTDEDLFA MAGHILIQPK VVNEKWGGGK IYY
//
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