ID   UCRI_SCHPO              Reviewed;         228 AA.
AC   Q09154; O42942;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE            EC=1.10.2.2;
DE   AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE   AltName: Full=Rieske iron-sulfur protein;
DE            Short=RISP;
DE   AltName: Full=Complex III subunit 5;
DE   Flags: Precursor;
GN   Name=rip1; ORFNames=SPBC16H5.06;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96279043; PubMed=8663290; DOI=10.1074/jbc.271.26.15341;
RA   Dirago J., Bruel C., Graham L.A., Slonimski P., Trumpower B.L.;
RT   "Heterologous complementation of a Rieske iron-sulfur protein-
RT   deficient Saccharomyces cerevisiae by the Rip1 gene of
RT   Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 271:15341-15345(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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.
CC   -!- CATALYTIC ACTIVITY: QH(2) + 2 ferricytochrome c = Q + 2
CC       ferrocytochrome c + 2 H(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC   -!- SUBUNIT: Fungal bc1 complex contains 10 subunits; 3 respiratory
CC       subunits, 2 core proteins and 5 low-molecular weight proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S
CC       protein.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; U40480; AAC49359.1; -; mRNA.
DR   EMBL; CU329671; CAA17904.1; -; Genomic_DNA.
DR   PIR; T39619; T39619.
DR   RefSeq; NP_595941.1; -.
DR   HSSP; P13272; 1RIE.
DR   SMR; Q09154; 51-228.
DR   GeneID; 2540075; -.
DR   KEGG; spo:SPBC16H5.06; -.
DR   NMPDR; fig|4896.1.peg.1807; -.
DR   GeneDB_Spombe; SPBC16H5.06; -.
DR   OMA; Q09154; AYFMVGS.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004006-MON; -.
DR   BRENDA; 1.10.2.2; 653.
DR   ArrayExpress; Q09154; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IGI:GeneDB_SPombe.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IGI:GeneDB_SPombe.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol...; IGI:GeneDB_SPombe.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   InterPro; IPR004192; Ubiquinol_cyt_Rdtase_TM.
DR   PANTHER; PTHR10134; Rieske; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF02921; UCR_TM; 1.
DR   TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Complete proteome; Disulfide bond; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Respiratory chain;
KW   Transit peptide; Transmembrane; Transport.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    228       Cytochrome b-c1 complex subunit Rieske,
FT                                mitochondrial.
FT                                /FTId=PRO_0000030682.
FT   DOMAIN      139    227       Rieske.
FT   METAL       172    172       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       174    174       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       191    191       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       194    194       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   DISULFID    177    193       By similarity.
FT   CONFLICT    183    183       A -> R (in Ref. 1; AAC49359).
SQ   SEQUENCE   228 AA;  24740 MW;  C50CC8BA159E31B2 CRC64;
     MLAKQFISKS LASSLRRLLP VSSTASSLKG SMMTIPKFTS IRTYTDSPEM PDFSEYQTKS
     TGDRSRVISY AMVGTMGALT AAGAQATVHD FLASWSASAD VLAMSKAEVD LSKIPEGKNL
     VVKWQGKPVF IRHRTPEEIQ EANSVDISTL RDPQADSDRV QKPEWLVMIG VCTHLGCVPI
     GEAGDYGGWF CPCHGSHYDI SGRIRRGPAP LNLAIPAYTF EGSKIIIG
//