Q6CAB5 (CCPR2_YARLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 57.
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: Putative cytochrome c peroxidase, mitochondrial Short name=CCP EC=1.11.1.5 | ||
| Gene names |
| ||
| Organism | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) | ||
| Taxonomic identifier | 284591 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia |
Protein attributes
| Sequence length | 285 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 |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | response to oxidative stress Inferred 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 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 285 | Putative cytochrome c peroxidase, mitochondrial | PRO_0000055590 | ||||||
Sites | |||||||||
| Active site | 37 | 1 | Proton acceptor By similarity | ||||||
| Active site | 177 | 1 | Tryptophan radical intermediate By similarity | ||||||
| Metal binding | 161 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Site | 33 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR382130 Genomic DNA. Translation: CAG80585.1. |
| RefSeq | XP_502397.1. XM_502397.1. |
3D structure databases | |
| ProteinModelPortal | Q6CAB5. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 2542. YlCcP01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2910632. |
| GenomeReviews | Gene locus YALI0D04268g in contig CR382130_GR. |
| KEGG | yli:YALI0D04268g. |
Phylogenomic databases | |
| eggNOG | fuNOG07575. |
| HOGENOM | HBG597790. |
| OMA | NNPTRFS. |
| OrthoDB | EOG45HW63. |
Family and domain databases | |
| InterPro | IPR002207. Asc_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. [Graphical view] |
| KO | K00428. |
| Pfam | PF00141. peroxidase. 1 hit. [Graphical view] |
| PRINTS | PR00459. ASPEROXIDASE. PR00458. PEROXIDASE. |
| SUPFAM | SSF48113. Peroxidase_super. 1 hit. |
| 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_YARLI | ||||||||
| Accession | Primary (citable) accession number: Q6CAB5 | ||||||||
| 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 |

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