Reviewed,
UniProtKB/Swiss-Prot Q6URB0 (CCPR_CRYNV)
Last modified
May 5, 2009.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome c peroxidase, mitochondrial Short name=CCP EC=1.11.1.5 | ||
| Gene names |
| ||
| Organism | Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii) | ||
| Taxonomic identifier | 178876 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex |
Protein attributes
| Sequence length | 377 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 | Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. |
| Catalytic activity | 2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. |
| Subunit structure | Forms a one-to-one complex with cytochrome c By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Cytochrome c peroxidase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stressInferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cytochrome-c peroxidase activity Inferred from electronic annotation. Source: EC heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 32 | 32 | Mitochondrion Potential | ||||||
| Chain | 33 – 377 | 345 | Cytochrome c peroxidase, mitochondrial | PRO_0000045290 | |||||
Sites | |||||||||
| Active site | 138 | 1 | Proton acceptor By similarity | ||||||
| Active site | 277 | 1 | Tryptophan radical intermediate By similarity | ||||||
| Metal binding | 261 | 1 | Iron (heme axial ligand) | ||||||
| Site | 134 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Cytochrome c peroxidase contributes to the antioxidant defense of Cryptococcus neoformans." Giles S.S., Perfect J.R., Cox G.M. Fungal Genet. Biol. 42:20-29(2005) [PubMed: 15588993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: H99. |
Cross-references
Sequence databases | |
|---|---|
| AY363612 Genomic DNA. Translation: AAR20479.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1APX based on UniProtKB P48534. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 3838. CnCcP01_grubiiH99. |
Family and domain databases | |
| InterPro | IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view] |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00459. ASPEROXIDASE. PR00458. PEROXIDASE. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CCPR_CRYNV | ||||||||
| Accession | Primary (citable) accession number: Q6URB0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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