Reviewed,
UniProtKB/Swiss-Prot Q59X94 (CCPR2_CANAL)
Last modified
June 16, 2009.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative heme-binding peroxidase EC=1.11.1.- | ||||
| Gene names |
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| Organism | Candida albicans (Yeast) | ||||
| Taxonomic identifier | 5476 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 291 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Cytochrome c peroxidase subfamily. |
Ontologies
| Keywords | |
|---|---|
| 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 |
| Molecular function | heme binding Inferred from electronic annotation. Source: InterPro peroxidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 291 | 291 | Putative heme-binding peroxidase | PRO_0000055584 | |||||
Sites | |||||||||
| Active site | 61 | 1 | Proton acceptor By similarity | ||||||
| Active site | 201 | 1 | Tryptophan radical intermediate By similarity | ||||||
| Metal binding | 185 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Site | 57 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314. |
Cross-references
Sequence databases | |
|---|---|
| AACQ01000109 Genomic DNA. Translation: EAK95087.1. AACQ01000108 Genomic DNA. Translation: EAK95134.1. | |
| RefSeq | XP_714170.1. XP_714211.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 2345. CalCcP01. |
Genome annotation databases | |
| GeneID | 3644127. 3644156. |
| KEGG | cal:CaO19.584. cal:CaO19.8216. |
Organism-specific databases | |
| CGD | CAL0000335. orf19.584. |
Phylogenomic databases | |
| OMA | Q59X94. IILRLAW. |
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. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CCPR2_CANAL | ||||||||
| Accession | Primary (citable) accession number: Q59X94 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Candida albicans Candida albicans: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


