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Reviewed, UniProtKB/Swiss-Prot Q6URB0 (CCPR_CRYNV)

Last modified May 5, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismCryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii)
Taxonomic identifier178876 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length377 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 – 3232Mitochondrion Potential
Chain33 – 377345Cytochrome c peroxidase, mitochondrial
PRO_0000045290

Sites

Active site1381Proton acceptor By similarity
Active site2771Tryptophan radical intermediate By similarity
Metal binding2611Iron (heme axial ligand)
Site1341Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6URB0-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0B41F38D621D78B4

FASTA37742,088
        10         20         30         40         50         60 
MSFRAPNLIR STVGRRAGQT LNLRSQVIRR RFATEGGPEI TKPSAPRSSN TGYIFAGLGV 

        70         80         90        100        110        120 
AAVGAAYYFY GTGRTEHDST NKADTVVREA VATVEAKTGL RRGKDEYQKV YNRIAETLDK 

       130        140        150        160        170        180 
EGYDDGSLAP VLLRLAWHAS GTYSKADGTG GSNFATMRFK PEAEHSANNG LHVAREHMEK 

       190        200        210        220        230        240 
IKQEFPWISY GDLWTLGGVC AIQESGGPTI PWRPGRIDGY AAQVTPDGRL PDATQAQDHL 

       250        260        270        280        290        300 
RFIFNRMGFN DQEIVALSGA HAMGRCHPNR SGFDGPWTFS PVTFSNQYFA LLRDEPWQWK 

       310        320        330        340        350        360 
KWTGPAQFED KKTKTLMMLP TDMALVKDKS FKKYVDIYAD NEEKFFSDFA KAFSKLIELG 

       370 
VPERQWAGEP WTMATSD 

« Hide

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

HSSPHSSP built from PDB template 1APX based on UniProtKB P48534.
ModBaseSearch...

Protein family/group databases

PeroxiBase3838. CnCcP01_grubiiH99.

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. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCCPR_CRYNV
AccessionPrimary (citable) accession number: Q6URB0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 5, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

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