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Database: UniProt
Entry: I2H2V2_TETBL
LinkDB: I2H2V2_TETBL
Original site: I2H2V2_TETBL 
ID   I2H2V2_TETBL            Unreviewed;       199 AA.
AC   I2H2V2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 68.
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   Name=TBLA0D01970 {ECO:0000313|EMBL:CCH60704.1};
GN   ORFNames=TBLA_0D01970 {ECO:0000313|EMBL:CCH60704.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60704.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH60704.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE806319; CCH60704.1; -; Genomic_DNA.
DR   RefSeq; XP_004180223.1; XM_004180175.1.
DR   AlphaFoldDB; I2H2V2; -.
DR   STRING; 1071380.I2H2V2; -.
DR   GeneID; 14495740; -.
DR   KEGG; tbl:TBLA_0D01970; -.
DR   eggNOG; KOG1671; Eukaryota.
DR   HOGENOM; CLU_055690_0_1_1; -.
DR   InParanoid; I2H2V2; -.
DR   OMA; KRTWLIA; -.
DR   OrthoDB; 166674at2759; -.
DR   Proteomes; UP000002866; Chromosome 4.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd03470; Rieske_cytochrome_bc1; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 1.20.5.270; Ubiquinol cytochrome reductase, transmembrane domain; 1.
DR   InterPro; IPR037008; bc1_Rieske_TM_sf.
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; IPR004192; Rieske_TM.
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   Pfam; PF02921; UCR_TM; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF81502; ISP transmembrane anchor; 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:UP000002866};
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          103..198
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   199 AA;  21511 MW;  66817ADC88A021A1 CRC64;
     MINKRCLSST NKAQISTYKT PDFGDAVKKD KSTDKGRSYA YFMIGSLGML SAAGGKSTVE
     TFLGSMSASA DVLAMAKVEV NLASIPEGKN AVVKWQGKPV FIRHRTAHEI EEANQVDITS
     LKDPQADADR VKNPSWLVML GVCTHLGCVP IGEAGDFGGW FCPCHGSHYD ISGRIRKGPA
     PLNLEIPTYE FQDDTLIVG
//
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