Reviewed, UniProtKB/Swiss-Prot Q6C0Z6 (CCPR_YARLI)

Names and origin

Protein names

Recommended name:
    Cytochrome c peroxidase, mitochondrial
      Short name=CCP
    EC=1.11.1.5

Gene names

Name:	CCP1
Ordered Locus Names:	YALI0F20504g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	340 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 + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
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 matrixBy 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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 17	17	Mitochondrion Potential
	Chain	18 – 340	323	Cytochrome c peroxidase, mitochondrial		PRO_0000045297
Sites
	Active site	101	1	Proton acceptor By similarity
	Active site	240	1	Tryptophan radical intermediate By similarity
	Metal binding	224	1	Iron (heme axial ligand)
	Site	97	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6C0Z6-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: EDFBCD9999EC9886	FASTA	340	37,646
	10 20 30 40 50 60 MRSFRAVRNF STTAKRLSQA PKASTPNASS GNGFVLAFVA AAAGAGAYYY YANSPAAKVE 70 80 90 100 110 120 TFNATKADYQ KVYDAIADKL IEDDDYDDGS YGPVLLRLAW HSSGTYNKSD NKFGSSGGTM 130 140 150 160 170 180 RFKPEASHAA NNGLVNARNF LKPIHEKFPW ISTGDLYTLG GVTAVQELGG PIIPWKRGRV 190 200 210 220 230 240 DEPESASPPD GSLPDASQGA THVRNVFNRQ GFNDQEMVAL IGAHALGRCH KQNSGFEGPW 250 260 270 280 290 300 TFSPTMFTND FYKLLLDDKW QWKKWDGNPQ YEDVKTKSLM MLPTDMALAT DKNFKKWATA 310 320 330 340 YAKDQDLFFK DFSAAFSKML NNGVDFPQGT EIWEFKPKNA

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. , 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. 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
EMBLGenBankDDBJ	CR382132 Genomic DNA. Translation: CAG78475.1.
RefSeq	XP_505666.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2343. YlCcP02.
Genome annotation databases
GeneID	2908688.
KEGG	yli:YALI0F20504g.
Phylogenomic databases
HOGENOM	Q6C0Z6.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCPR_YARLI

Accession

Primary (citable) accession number: Q6C0Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)