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Q0H8Y7 (COX2_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:
Cytochrome c oxidase subunit 2

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:COX2
Encoded onMitochondrion
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activity

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

Cofactor

Copper A.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 By similarity
Chain17 – 255239Cytochrome c oxidase subunit 2
PRO_0000271142

Regions

Topological domain17 – 4327Mitochondrial intermembrane Potential
Transmembrane44 – 6421Helical; Potential
Topological domain65 – 8016Mitochondrial matrix Potential
Transmembrane81 – 10121Helical; Potential
Topological domain102 – 255154Mitochondrial intermembrane Potential

Sites

Metal binding1891Copper A By similarity
Metal binding2241Copper A By similarity
Metal binding2281Copper A By similarity
Metal binding2321Copper A By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0H8Y7 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 23B1FCAF85401052

FASTA25528,613
        10         20         30         40         50         60 
MFNLFPPFGA NTAIFNDAPQ PWQVGFQDGA SPTQEGITEL HDSIFFYLVI ICFGVLWVLS 

        70         80         90        100        110        120 
SVIVNFNSNK SQLVYKYANH GTLIELIWTI TPALVLIAIA FPSFKLLYLM DEVISPSMTV 

       130        140        150        160        170        180 
KVAGHQWYWS AEYSDFINED GESIEFDSYM VPETDLEDGQ LRLLEVDNRM VVPIDTHIRF 

       190        200        210        220        230        240 
IVTGADVIHD FAVPSLGLKI DAVPGRLNQT SVLIEREGVF YGQCSEICGV YHGFMPIAIE 

       250 
AVTPEKYLAW IDSQA 

« Hide

References

[1]"Annotation of mitochondrial genome of Ustilago maydis and comparative analysis of basidiomycete mtDNAs."
Kennell J.C., Boehmer C.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.
[2]"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ157700 Genomic DNA. Translation: AAZ67008.1.
AACP01000278 Genomic DNA. No translation available.
RefSeqYP_762685.1. NC_008368.1.

3D structure databases

ProteinModelPortalQ0H8Y7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UsmafMp05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4308289.
KEGGuma:UsmafMp05.

Phylogenomic databases

eggNOGCOG1622.
KOK02261.
OrthoDBEOG7WDNDC.

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.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_USTMA
AccessionPrimary (citable) accession number: Q0H8Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 59 of the entry and version 1 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