Reviewed,
UniProtKB/Swiss-Prot P56205 (CYC_ASPNG)
Last modified
November 25, 2008.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome c | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 111 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. |
| Subcellular location | |
| Post-translational modification | Binds 1 heme group per subunit. |
| Sequence similarities | Belongs to the cytochrome c family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Mitochondrion |
| Ligand | Heme Iron Metal-binding |
| PTM | Methylation |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 111 | 111 | Cytochrome c | PRO_0000108317 | |||||
Sites | |||||||||
| Metal binding | 26 | 1 | Iron (heme axial ligand) | ||||||
| Metal binding | 88 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Binding site | 22 | 1 | Heme (covalent) | ||||||
| Binding site | 25 | 1 | Heme (covalent) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 80 | 1 | N6,N6,N6-trimethyllysine By similarity | ||||||
Sequences
References
| [1] | "Amino acid sequence of cytochrome c from Aspergillus niger." Chin C.C.Q., Niehaus W.G., Wold F. J. Protein Chem. 8:165-171(1989) [PubMed: 2544196] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A61490. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CRH based on UniProtKB P00044. |
| SMR | P56205. Positions 6-109. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR009056. Cyt_c_monohaem. IPR003088. Cyt_CI. IPR002327. Cyt_CIAB. [Graphical view] |
| Gene3D | G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit. |
| PANTHER | PTHR11961. Cyt_CIAB. 1 hit. |
| Pfam | PF00034. Cytochrom_C. 1 hit. [Graphical view] |
| PRINTS | PR00604. CYTCHRMECIAB. |
| ProDom | PD000375. Cyt_CIAB. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS51007. CYTC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYC_ASPNG | ||||||||
| Accession | Primary (citable) accession number: P56205 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


