[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2176595 [NCBI, ExPASy, EBI, Israel, Japan] Yun C.-H., Beci R., Crofts A.R., Kaplan S., Gennis R.B.; "Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1 complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant."; Eur. J. Biochem. 194:399-411(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95. DOI=10.1016/0022-2836(87)90324-X; PubMed=2821272 [NCBI, ExPASy, EBI, Israel, Japan] Davidson E., Daldal F.; "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is from Rhodopseudomonas capsulata."; J. Mol. Biol. 195:25-29(1987).

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: The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein.
SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
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

X56157; CAA39623.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18577; AAA26150.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S13868; S13868.

3D structure databases

PDB

2FYN; X-ray; 3.20 A; C/F/I/L/O/R=1-187.	[ExPASy / RCSB / EBI]
2NUK; X-ray; 1.20 A; A=47-187.	[ExPASy / RCSB / EBI]
2NUM; X-ray; 1.50 A; A=47-187.	[ExPASy / RCSB / EBI]
2NVE; X-ray; 1.50 A; A=47-187.	[ExPASy / RCSB / EBI]
2NVF; X-ray; 1.50 A; A=47-187.	[ExPASy / RCSB / EBI]
2NVG; X-ray; 1.35 A; A=47-187.	[ExPASy / RCSB / EBI]
2NWF; X-ray; 1.10 A; A=47-187.	[ExPASy / RCSB / EBI]
2QJK; X-ray; 3.10 A; C/F/I/L/O/R=9-187.	[ExPASy / RCSB / EBI]
2QJP; X-ray; 2.60 A; C/F/I/L=9-187.	[ExPASy / RCSB / EBI]
2QJY; X-ray; 2.40 A; C/F/I/L/O/R=1-187.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2FYN; -.
2NUK; -.
2NUM; -.
2NVE; -.
2NVF; -.
2NVG; -.
2NWF; -.
2QJK; -.
2QJP; -.
2QJY; -.

ModBase

Q02762.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR014349; Rieske.
IPR005805; Rieske_C.
IPR006317; Rieske_proteo.
IPR005806; Rieske_reg.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

PANTHER

PTHR10134; Rieske; 1.

Pfam

PF00355; Rieske; 1.
Pfam graphical view of domain structure.

PRINTS

PR00162; RIESKE.

TIGRFAMs

TIGR01416; Rieske_proteo; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS51296; RIESKE; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3D-structure; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 187`	`187`	`Ubiquinol-cytochrome c reductase iron-sulfur subunit.`	`PRO_0000127764`
`TRANSMEM`	`15 35`	`21`	`Potential.`
`DOMAIN`	`89 185`	`97`	`Rieske.`
`METAL`	`129 129`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`131 131`		`Iron-sulfur (2Fe-2S) (via pros nitrogen) (By similarity).`
`METAL`	`149 149`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`152 152`		`Iron-sulfur (2Fe-2S) (via pros nitrogen) (By similarity).`
`DISULFID`	`134 151`		`By similarity.`
`HELIX`	`10 36`	`27`
`TURN`	`42 44`	`3`
`STRAND`	`50 53`	`4`
`STRAND`	`61 67`	`7`
`STRAND`	`70 76`	`7`
`HELIX`	`79 86`	`8`
`HELIX`	`90 92`	`3`
`HELIX`	`111 114`	`4`
`STRAND`	`115 117`	`3`
`STRAND`	`122 126`	`5`
`TURN`	`130 132`	`3`
`STRAND`	`137 141`	`5`
`TURN`	`142 145`	`4`
`STRAND`	`146 149`	`4`
`TURN`	`150 153`	`4`
`STRAND`	`154 156`	`3`
`STRAND`	`162 166`	`5`
`STRAND`	`175 186`	`12`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 19910 Da [This is the MW of the unprocessed precursor]

CRC64: 575B47EEEECD74D2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNAEDHAGT RRDFLYYATA GAGAVATGAA VWPLINQMNP SADVQALASI FVDVSSVEPG 

        70         80         90        100        110        120 
VQLTVKFLGK PIFIRRRTEA DIELGRSVQL GQLVDTNARN ANIDAGAEAT DQNRTLDEAG 

       130        140        150        160        170        180 
EWLVMWGVCT HLGCVPIGGV SGDFGGWFCP CHGSHYDSAG RIRKGPAPEN LPIPLAKFID 


ETTIQLG

Q02762 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools