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Q75CW5 (QCR2_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b-c1 complex subunit 2, mitochondrial
Alternative name(s):
Complex III subunit 2
Core protein II
Ubiquinol-cytochrome-c reductase complex core protein 2
Gene names
Name:QCR2
Ordered Locus Names:ACL199C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex By similarity.

Subunit structure

Fungi bc1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins By similarity.

Subcellular location

Mitochondrion inner membrane By similarity.

Sequence similarities

Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1515Mitochondrion By similarity
Chain16 – 366351Cytochrome b-c1 complex subunit 2, mitochondrial
PRO_0000026794

Sequences

Sequence LengthMass (Da)Tools
Q75CW5 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: B0A46B5B605A15D0

FASTA36639,229
        10         20         30         40         50         60 
MLSQRLQCSK QFARHLSVAA KDGSGKVSTL SVQVQGGSRY ATKDGVAHLL SRFNFHNTGN 

        70         80         90        100        110        120 
KSALRLVRES ELLGGRFQST VDREHITLSA TFLKEDLPYF VNALADVLYK TSFRPHELAE 

       130        140        150        160        170        180 
SVLPAATRDA AVARACPVAA AEEALYSVTY RHGLGKPVLY DGVEKVTLED IKAYADKVYT 

       190        200        210        220        230        240 
KENVTVLGQG INEADLKRFV NDSLLASLPS GTSLAGSGNA KTHSGEARLR HAGSSVAAIA 

       250        260        270        280        290        300 
VPVAKADFAT YEVLARYLTS DLYALSPLVH KAKLDKYTDG GLFSLYVKSA EAAKAAADIK 

       310        320        330        340        350        360 
KVVADLKAGK DISVARKYAA LQLAVENDSA ASPVSLKLEN AKDFKLGKFN YVAVGDVSNL 


PFADEL 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 19; 108; 110; 269; 274; 281; 283; 297; 313-314; 323; 330 AND 346.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016816 Genomic DNA. Translation: AAS51029.2.
RefSeqNP_983205.2. NM_208558.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_ACL199C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4619325.
KEGGago:AGOS_ACL199C.

Phylogenomic databases

eggNOGCOG0612.
HOGENOMHOG000159494.
KOK00415.
OrthoDBEOG7F51BJ.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 2 hits.
ProtoNetSearch...

Entry information

Entry nameQCR2_ASHGO
AccessionPrimary (citable) accession number: Q75CW5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 9, 2013
Last modified: April 16, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries