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Database: UniProt
Entry: B3SEN8_TRIAD
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Original site: B3SEN8_TRIAD 
ID   B3SEN8_TRIAD            Unreviewed;       158 AA.
AC   B3SEN8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial {ECO:0000256|RuleBase:RU004494};
DE            EC=7.1.1.8 {ECO:0000256|RuleBase:RU004494};
GN   ORFNames=TRIADDRAFT_34599 {ECO:0000313|EMBL:EDV18806.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV18806.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV18806.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV18806.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC         Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:132124; EC=7.1.1.8;
CC         Evidence={ECO:0000256|RuleBase:RU004494};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|RuleBase:RU004494};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU004494};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|RuleBase:RU004495}.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC       {ECO:0000256|RuleBase:RU004494}.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000256|ARBA:ARBA00010651}.
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DR   EMBL; DS985571; EDV18806.1; -; Genomic_DNA.
DR   RefSeq; XP_002118707.1; XM_002118671.1.
DR   AlphaFoldDB; B3SEN8; -.
DR   STRING; 10228.B3SEN8; -.
DR   EnsemblMetazoa; TriadT34599; TriadP34599; TriadG34599.
DR   GeneID; 6759922; -.
DR   KEGG; tad:TRIADDRAFT_34599; -.
DR   CTD; 6759922; -.
DR   eggNOG; KOG1671; Eukaryota.
DR   HOGENOM; CLU_055690_0_2_1; -.
DR   InParanoid; B3SEN8; -.
DR   OMA; ETHTVMW; -.
DR   OrthoDB; 166674at2759; -.
DR   PhylomeDB; B3SEN8; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   NCBIfam; TIGR01416; Rieske_proteo; 1.
DR   PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10134:SF20; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|RuleBase:RU004494};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|RuleBase:RU004495};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Respiratory chain {ECO:0000256|RuleBase:RU004495};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU004494}.
FT   DOMAIN          69..156
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   158 AA;  16915 MW;  FACD509D00DE4EB2 CRC64;
     MSASAVAGVG AVAAAIPIVT SLKPDKGVLA AGSTEVDISN IKKGETHTVM WRGKPIFITH
     RTEEEIKEAE DVNLADLRDP EPDKDRVKPG KPEWLITVGI CTHLGCVPIG NKGEFGGWFC
     PCHGSHYDSS GRIRKGPAPK NLAIPPYEFI SDSKIMIG
//
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