ID A0A0D4KG20_YEASX Unreviewed; 215 AA. AC A0A0D4KG20; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 22-JUL-2015, entry version 3. DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial {ECO:0000256|RuleBase:RU004494}; DE EC=1.10.2.2 {ECO:0000256|RuleBase:RU004494}; GN Name=RIP1 {ECO:0000313|EMBL:AJU49095.1}; GN ORFNames=H804_YJM1383E00053 {ECO:0000313|EMBL:AJU49095.1}; OS Saccharomyces cerevisiae YJM1383. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=1294356 {ECO:0000313|EMBL:AJU49095.1}; RN [1] {ECO:0000313|EMBL:AJU49095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YJM1383 {ECO:0000313|EMBL:AJU49095.1}; RX PubMed=25840857; DOI=10.1101/gr.185538.114; RA Strope P.K., Skelly D.A., Kozmin S.G., Mahadevan G., Stone E.A., RA Magwene P.M., Dietrich F.S., McCusker J.H.; RT "The 100-genomes strains, an S. cerevisiae resource that illuminates RT its natural phenotypic and genotypic variation and emergence as an RT opportunistic pathogen."; RL Genome Res. 25:762-774(2015). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. {ECO:0000256|RuleBase:RU004494}. CC -!- CATALYTIC ACTIVITY: Quinol + 2 ferricytochrome c = quinone + 2 CC ferrocytochrome c + 2 H(+). {ECO:0000256|RuleBase:RU004494}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|RuleBase:RU004494}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000256|RuleBase:RU004494}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU004495}. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S CC protein. {ECO:0000256|RuleBase:RU004494}. CC -!- SIMILARITY: Contains 1 Rieske domain. CC {ECO:0000256|RuleBase:RU004493}. 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; CP004814; AJU49095.1; -; Genomic_DNA. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; 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 Gene3D; 1.20.5.270; -; 1. DR Gene3D; 2.102.10.10; -; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. 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 InterPro; IPR004192; Ubiquinol_cyt_Rdtase_TM. DR PANTHER; PTHR10134; PTHR10134; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF02921; UCR_TM; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; SSF50022; 1. DR TIGRFAMs; TIGR01416; Rieske_proteo; 1. DR PROSITE; PS51296; RIESKE; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU004492}; KW Electron transport {ECO:0000256|RuleBase:RU004494}; KW Iron {ECO:0000256|RuleBase:RU004492}; KW Iron-sulfur {ECO:0000256|RuleBase:RU004492}; KW Metal-binding {ECO:0000256|RuleBase:RU004492}; KW Mitochondrion {ECO:0000256|RuleBase:RU004495}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004494}; KW Respiratory chain {ECO:0000256|RuleBase:RU004495}; KW Transport {ECO:0000256|RuleBase:RU004494}. SQ SEQUENCE 215 AA; 23365 MW; 21981BD8492E86F3 CRC64; MLGIRSSVKT CFKPMSLTSK RLISQSLLAS KSTYRTPNFD DVLKENNDAD KGRSYAYFMV GAMGLLSSAG AKSTVETFIS SMTATADVLA MAKVEVNLAA IPLGKNVVVK WQGKPVFIRH RTPHEIQEAN SVDMSALKDP QTDADRVKDP QWLIMLGICT HLGCVPIGEA GDFGGWFCPC HGSHYDISGR IRKGPAPLNL EIPAYEFDGD KVIVG //