Reviewed, UniProtKB/Swiss-Prot Q6CAB5 (CCPR2_YARLI)

Names and origin

Protein names

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

Gene names

Ordered Locus Names:

YALI0D04268g

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	285 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 – ?		Mitochondrion Potential
	Chain	? – 285		Putative cytochrome c peroxidase, mitochondrial		PRO_0000055590
Sites
	Active site	37	1	Proton acceptor By similarity
	Active site	177	1	Tryptophan radical intermediate By similarity
	Metal binding	161	1	Iron (heme axial ligand) By similarity
	Site	33	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CAB5-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 2992816B06FD806E	FASTA	285	32,388
	10 20 30 40 50 60 MAEGDYNAVR EAIADILDND DYDDGSIGPV LVRLAWHASG TYDKATGTGG SNGATMRYMK 70 80 90 100 110 120 EAKDEANNGL ENARQFLEPI KAKFPWITYA DLWTLAGVVA IEEMDGPKVP WKPGRQDYVD 130 140 150 160 170 180 ETNVPPNGRL PDGAQGQDHL RDIFYRMGFN DQEIVALCGA HNMGRCHMDR SGFEGAWVPN 190 200 210 220 230 240 PIRFANTYFK LLMNEEWKLT TLKNGVKQYF NEDEELMMLP ADYSLMQDPE FHKWVEIYAA 250 260 270 280 DKEKFFEDFS KVFAKLIELG VRRGPDGKAK TNFIDRNNND PNPRL

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	CR382130 Genomic DNA. Translation: CAG80585.1.
RefSeq	XP_502397.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2542. YlCcP01.
Genome annotation databases
GeneID	2910632.
KEGG	yli:YALI0D04268g.
Phylogenomic databases
HOGENOM	Q6CAB5.
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. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CCPR2_YARLI

Accession

Primary (citable) accession number: Q6CAB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)