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UniProtKB/Swiss-Prot entry Q6BKY9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCPR_DEBHA
Primary accession number Q6BKY9
Secondary accession numbers None
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on August 16, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 32)
Name and origin of the protein
Protein name Cytochrome c peroxidase, mitochondrial [Precursor]
Synonyms CCP
EC 1.11.1.5
Gene name
Name: CCP1
OrderedLocusNames: DEHA0F19173g
From
Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [TaxID: 4959] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Debaryomyces.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
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., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
Comments
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
CR382138; CAG89515.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_461132.1; -.
3D structure databases
ModBase Q6BKY9.
Protein family/group databases
PeroxiBase 3061; DhCcP02.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0004130; Molecular function: cytochrome-c peroxidase activity (inferred from electronic annotation from EC).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
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; FALSE_NEG.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q6BKY9.
Genome annotation databases
GeneID 2904292; -.
KEGG dha:DEHA0F19173g; -.
Phylogenomic databases
HOGENOM Q6BKY9; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   360        Cytochrome c peroxidase, mitochondrial. PRO_0000045291
ACT_SITE   118   118        Proton acceptor (By similarity). 
ACT_SITE   258   258        Tryptophan radical intermediate (By similarity). 
METAL   242   242        Iron (heme axial ligand). 
SITE   114   114  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 360 AA [This is the length of the unprocessed precursor] Molecular weight: 40439 Da [This is the MW of the unprocessed precursor] CRC64: 98033D6DF83F33C0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTAAFKRQS VPLSKLFQSY GKNNSQSKYG GYFLATLIGS GILATSYFNN NKNGNTPSNN 

        70         80         90        100        110        120 
HKKLLAGSGI VNTAAIPKGK SIKDYQSLYN EIAEKVRDQD DADDGAGRYG LLTRLAWHTS 

       130        140        150        160        170        180 
GTYKKEDNTG GSYGGTMIYK PESTDGENSG LNHGRDFLQE FKDKYSWLSH GDLWTLGGVV 

       190        200        210        220        230        240 
AVQECGGPKI KWRPGRQDIS DKTRVPENGR LPDASKDADY VKGVFGRMGF NERETVCLIG 

       250        260        270        280        290        300 
AHCLGKCHKE NTNYDGPWGP SFNMFTNDFF VRLLQNWHVK KWDGKKQYED DETNSFMMLP 

       310        320        330        340        350        360 
TDMALKEDSS FLKYVKMYAD DEKLFFSDFA KNFSTLLELG VTFPDSIKPT EFKTLDEQDK
Q6BKY9 in FASTA format

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