NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=H99;
DOI=10.1016/j.fgb.2004.09.003; PubMed=15588993 [NCBI, ExPASy, EBI, Israel, Japan]
Giles S.S., Perfect J.R., Cox G.M.;
"Cytochrome c peroxidase contributes to the antioxidant defense of Cryptococcus neoformans.";
Fungal Genet. Biol. 42:20-29(2005).

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: Forms a one-to-one complex with cytochrome c (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY363612; AAR20479.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P48534; 1APX. [HSSP ENTRY / PDB]

ModBase

Q6URB0.

Protein family/group databases

PeroxiBase

3838; CnCcP01_grubiiH99.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 32`	`32`	`Mitochondrion (Potential).`
`CHAIN`	`33 377`	`345`	`Cytochrome c peroxidase, mitochondrial.`	`PRO_0000045290`
`ACT_SITE`	`138 138`		`Proton acceptor (By similarity).`
`ACT_SITE`	`277 277`		`Tryptophan radical intermediate (By similarity).`
`METAL`	`261 261`		`Iron (heme axial ligand).`
`SITE`	`134 134`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 377 AA [This is the length of the unprocessed precursor]

Molecular weight: 42088 Da [This is the MW of the unprocessed precursor]

CRC64: 0B41F38D621D78B4 [This is a checksum on the sequence]

        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

Q6URB0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools