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Q82AL0 (COX2_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Probable cytochrome c oxidase subunit 2

EC=1.9.3.1
Alternative name(s):
Cytochrome aa3 subunit 2
Cytochrome c oxidase polypeptide II
Gene names
Name:ctaC
Ordered Locus Names:SAV_6047
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) By similarity.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactor

Copper A By similarity.

Heme group By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 319286Probable cytochrome c oxidase subunit 2
PRO_0000006062

Regions

Transmembrane63 – 8321Helical; Potential
Transmembrane101 – 12121Helical; Potential

Sites

Metal binding2271Copper A Potential
Metal binding2621Copper A Potential
Metal binding2661Copper A Potential
Metal binding2701Copper A Potential

Sequences

Sequence LengthMass (Da)Tools
Q82AL0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CE85FD7EDCC1C39D

FASTA31935,494
        10         20         30         40         50         60 
MSPNGSDRSP RRPMRRKLLQ ALTAGLVLAT ATGCTYKDFP RLGMPTPVTE EAPRILSLWQ 

        70         80         90        100        110        120 
GSWAAALATG VLVWGLILWA TIFHRRSRTK VEVPPQTRYN MPIEALYTVV PLIIVSVLFY 

       130        140        150        160        170        180 
FTARDESKLL DLSKKPDVTV NVVGFQWSWG FNYIENVDGS TGNAKTDKNL AAIPDRFKEA 

       190        200        210        220        230        240 
FPANAGGVYD VGTPGTRNPQ TNNPGPTLWL PKGKTVRFVL TSRDVIHSFW VVPFLMKQDV 

       250        260        270        280        290        300 
IPGHTNSFQV TPNREGTFLG KCAELCGVDH SRMLFNVKVV SPERYQQHLK DLAKKGQTGY 

       310 
VPAGIAQTSH EKNRETNNL 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC73758.1.
RefSeqNP_827223.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82AL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_6047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC73758; BAC73758; SAV_6047.
GeneID1211381.
KEGGsma:SAV_6047.
PATRIC23726120. VBIStrAve112782_6413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000245527.
KOK02275.
OMAMRELWTW.
OrthoDBEOG68SVXT.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6127-MONOMER.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 2 hits.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_STRAW
AccessionPrimary (citable) accession number: Q82AL0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families