Q0H8Y7 (COX2_USTMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 54.
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 |
| ||
| Encoded on | Mitochondrion | ||
| Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome] | ||
| Taxonomic identifier | 237631 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › ![]() |
Protein attributes
| Sequence length | 255 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. |
| Subcellular location | |
| 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 | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 16 | 16 | By similarity | ||||||
| Chain | 17 – 255 | 239 | Cytochrome c oxidase subunit 2 | PRO_0000271142 | |||||
Regions | |||||||||
| Topological domain | 17 – 43 | 27 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 44 – 64 | 21 | Helical; Potential | ||||||
| Topological domain | 65 – 80 | 16 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 81 – 101 | 21 | Helical; Potential | ||||||
| Topological domain | 102 – 255 | 154 | Mitochondrial intermembrane Potential | ||||||
Sites | |||||||||
| Metal binding | 189 | 1 | Copper A By similarity | ||||||
| Metal binding | 224 | 1 | Copper A By similarity | ||||||
| Metal binding | 228 | 1 | Copper A By similarity | ||||||
| Metal binding | 232 | 1 | Copper A By similarity | ||||||
Sequences
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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. 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. |
| RefSeq | YP_762685.1. NC_008368.1. |
3D structure databases | |
| ProteinModelPortal | Q0H8Y7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5270.UsmafMp05. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4308289. |
| KEGG | uma:UsmafMp05. |
Phylogenomic databases | |
| eggNOG | COG1622. |
| KO | K02261. |
| OrthoDB | EOG4ZW8M5. |
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_USTMA | ||||||||
| Accession | Primary (citable) accession number: Q0H8Y7 | ||||||||
| 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
