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Reviewed, UniProtKB/Swiss-Prot Q5AEN1 (CCPR_CANAL)

Last modified May 5, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytochrome c peroxidase, mitochondrial
      Short name=CCP
    EC=1.11.1.5
Gene names
Name: CCP1
ORF Names: CaO19.238, CaO19.7868
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 componentMitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncytochrome-c peroxidase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 366Cytochrome c peroxidase, mitochondrialPRO_0000045287

Sites

Active site1231Proton acceptor By similarity
Active site2631Tryptophan radical intermediate By similarity
Metal binding2471Iron (heme axial ligand)
Site1191Transition state stabilizer By similarity

Natural variations

Natural variant581E → G in allele CaO19.7868.

Sequences

Sequence LengthMass (Da)Tools
Q5AEN1-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 826D6ED25355E801

FASTA36640,754
        10         20         30         40         50         60 
MATFAPHISK ITKSSTKFNY GRIAKTFLGV AGSAAIATYF YNNGNPFNNN NNNNNNNEGS 

        70         80         90        100        110        120 
KNAAKALFGA SAGANVKIAK VPEGKSASDY QKVYNDIATK ISENLEFDEN AGYYGQLLRL 

       130        140        150        160        170        180 
AWHTSGTYDK SDNSGGSYGG TMIFAPEEFD PENAGLQVGR EFLMEFLVKY PWISRGDLWT 

       190        200        210        220        230        240 
LGGVAAVQES GGPKIEWRPG RVDDNTASKV PPNGRLPDAS KDGKYVKDLF ARMGFNERET 

       250        260        270        280        290        300 
VALLGAHVLG RCHKHNSGYD GPWGPSFNQF TNVFYTTLLG DWHVKKWDGK KQYEDDETGE 

       310        320        330        340        350        360 
FMMLPTDMAL KEESYFLKYV KMYADDQDLF FKDFAKAFSK LISNGIKYPA DSKPILFKTL 


DEQDEE 

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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

AACQ01000027 Genomic DNA. Translation: EAL01077.1.
AACQ01000026 Genomic DNA. Translation: EAL01211.1.
RefSeqXP_719937.1.
XP_720067.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

PeroxiBase3406. CalCcP02.

Genome annotation databases

GeneID3638289.
3638350.
KEGGcal:CaO19.238.
cal:CaO19.7868.

Organism-specific databases

CGDCAL0003960. CCP1.

Enzyme and pathway databases

BRENDA1.11.1.5. 1124.

Family and domain databases

InterProIPR002207. Asc_perxdse.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. False negative.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCCPR_CANAL
AccessionPrimary (citable) accession number: Q5AEN1
Secondary accession number(s): Q5AF18
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: April 26, 2005
Last modified: May 5, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents