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UniProtKB/Swiss-Prot entry Q09154


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UCRI_SCHPO
Primary accession number Q09154
Secondary accession number O42942
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 67)
Name and origin of the protein
Protein name Cytochrome b-c1 complex subunit Rieske, mitochondrial [Precursor]
Synonyms EC 1.10.2.2
Ubiquinol-cytochrome c reductase iron-sulfur subunit
Rieske iron-sulfur protein
RISP
Complex III subunit 5
Gene name
Name: rip1
ORFNames: SPBC16H5.06
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.271.26.15341; PubMed=8663290 [NCBI, ExPASy, EBI, Israel, Japan]
Dirago J., Bruel C., Graham L.A., Slonimski P., Trumpower B.L.;
"Heterologous complementation of a Rieske iron-sulfur protein-deficient Saccharomyces cerevisiae by the Rip1 gene of Schizosaccharomyces pombe.";
J. Biol. Chem. 271:15341-15345(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Comments
  • FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
  • CATALYTIC ACTIVITY: QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+.
  • COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
  • SUBUNIT: Fungal bc1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins (By similarity).
  • SUBCELLULAR LOCATION: Mitochondrion inner membrane.
  • MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
  • SIMILARITY: Contains 1 Rieske domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U40480; AAC49359.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAA17904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39619; T39619.
RefSeq NP_595941.1; -.
3D structure databases
HSSP P13272; 1RIE. [HSSP ENTRY / PDB]
SMR Q09154; 51-228.
ModBase Q09154.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004006-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC16H5.06; -.
Gene expression databases
ArrayExpress Q09154; -.
Ontologies
GO
GO:0005750; Cellular component: mitochondrial respiratory chain complex III (inferred from genetic interaction from GeneDB_SPombe).
GO:0008121; Molecular function: ubiquinol-cytochrome-c reductase activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0006122; Biological process: mitochondrial electron transport, ubiquinol to cytochrome c (inferred from genetic interaction from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR014349; Rieske.
IPR005805; Rieske_C.
IPR006317; Rieske_proteo.
IPR005806; Rieske_reg.
IPR004192; UCR_TM_region.
Graphical view of domain structure.
PANTHER PTHR10134; Rieske; 1.
Pfam PF00355; Rieske; 1.
PF02921; UCR_TM; 1.
Pfam graphical view of domain structure.
PRINTS PR00162; RIESKE.
TIGRFAMs TIGR01416; Rieske_proteo; 1.
PROSITE PS51296; RIESKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q09154.
Genome annotation databases
GeneID 2540075; -.
KEGG spo:SPBC16H5.06; -.
NMPDR fig|4896.1.peg.1807; -.
Other
ProtoNet Q09154.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Complete proteome; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Respiratory chain; Transit peptide; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   228        Cytochrome b-c1 complex subunit Rieske, mitochondrial. PRO_0000030682
DOMAIN   139   227  89     Rieske. 
METAL   172   172        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   174   174        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   191   191        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   194   194        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
DISULFID   177   193        By similarity. 
CONFLICT   183   183        A -> R (in Ref. 1; AAC49359). 
Sequence information
Length: 228 AA [This is the length of the unprocessed precursor] Molecular weight: 24740 Da [This is the MW of the unprocessed precursor] CRC64: C50CC8BA159E31B2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLAKQFISKS LASSLRRLLP VSSTASSLKG SMMTIPKFTS IRTYTDSPEM PDFSEYQTKS 

        70         80         90        100        110        120 
TGDRSRVISY AMVGTMGALT AAGAQATVHD FLASWSASAD VLAMSKAEVD LSKIPEGKNL 

       130        140        150        160        170        180 
VVKWQGKPVF IRHRTPEEIQ EANSVDISTL RDPQADSDRV QKPEWLVMIG VCTHLGCVPI 

       190        200        210        220 
GEAGDYGGWF CPCHGSHYDI SGRIRRGPAP LNLAIPAYTF EGSKIIIG 

Q09154 in FASTA format

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