Q7YFV7 (COX2_ASHGO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome c oxidase subunit 2 EC=1.9.3.1 Alternative name(s): Cytochrome c oxidase polypeptide II | ||||||||
| Gene names |
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| Encoded on | Mitochondrion | ||||||||
| Organism | Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome] | ||||||||
| Taxonomic identifier | 284811 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium › ![]() |
Protein attributes
| Sequence length | 248 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred 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. |
| Subunit structure | Composed of at least 11 subunits. |
| Subcellular location | |
| Post-translational modification | The signal sequence of COX2 is processed by IMP1 By similarity. |
| Sequence similarities | Belongs to the cytochrome c oxidase subunit 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Signal Transmembrane Transmembrane helix |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | aerobic respiration Inferred from electronic annotation. Source: EnsemblFungi mitochondrial electron transport, cytochrome c to oxygenInferred from electronic annotation. Source: EnsemblFungi |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex IVInferred from electronic annotation. Source: EnsemblFungi |
| Molecular_function | copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 12 | 12 | By similarity | ||||||
| Chain | 13 – 248 | 236 | Cytochrome c oxidase subunit 2 | PRO_0000006037 | |||||
Regions | |||||||||
| Topological domain | 13 – 39 | 27 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 40 – 61 | 22 | Helical; Potential | ||||||
| Topological domain | 62 – 79 | 18 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 80 – 104 | 25 | Helical; Potential | ||||||
| Topological domain | 105 – 248 | 144 | Mitochondrial intermembrane Potential | ||||||
Sites | |||||||||
| Metal binding | 183 | 1 | Copper A By similarity | ||||||
| Metal binding | 218 | 1 | Copper A By similarity | ||||||
| Metal binding | 222 | 1 | Copper A By similarity | ||||||
| Metal binding | 226 | 1 | Copper A By similarity | ||||||
Sequences
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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] | "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses." Kurtzman C.P., Robnett C.J. FEMS Yeast Res. 3:417-432(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-233. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016821 Genomic DNA. Translation: AAS50168.1. AF442273 Genomic DNA. Translation: AAP57840.1. |
| RefSeq | NP_987078.1. NC_005789.1. |
3D structure databases | |
| ProteinModelPortal | Q7YFV7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 33169.AGOS_AMI001W. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | AAS50168; AAS50168; AGOS_AMI001W. |
| GeneID | 2760769. |
| KEGG | ago:AGOS_AMI001W. |
Phylogenomic databases | |
| eggNOG | COG1622. |
| HOGENOM | HOG000264988. |
| KO | K02261. |
| OrthoDB | EOG4ZW8M5. |
| PhylomeDB | Q7YFV7. |
Family and domain databases | |
| Gene3D | 1.10.287.90. 1 hit. 2.60.40.420. 1 hit. |
| InterPro | IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR014222. Cyt_c_oxidase_su2. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view] |
| Pfam | PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view] |
| SUPFAM | SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit. |
| TIGRFAMs | TIGR02866. CoxB. 1 hit. |
| PROSITE | PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX2_ASHGO | ||||||||
| Accession | Primary (citable) accession number: Q7YFV7 Secondary accession number(s): Q75G36 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
