Reviewed, UniProtKB/Swiss-Prot P0C0V3 (CCPR_EMENI)

Names and origin

Protein names

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

Gene names

Name:	ccp1
ORF Names:	AN1630

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	361 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.
Sequence caution	The sequence EAA64750.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
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 – 41	41	Mitochondrion Potential
	Chain	42 – 361	320	Cytochrome c peroxidase, mitochondrial		PRO_0000045292
Sites
	Active site	122	1	Proton acceptor By similarity
	Active site	261	1	Tryptophan radical intermediate By similarity
	Metal binding	245	1	Iron (heme axial ligand)
	Site	118	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C0V3-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 5EF75C2E9EEDC530	FASTA	361	39,937
	10 20 30 40 50 60 MASAARSASR AFLRSSLRPA VRSSRFALPT QGLRVASRRG YSSEASSGKS SNTLLWAGVA 70 80 90 100 110 120 LAGGAGAYFY LQGGDVGAST KVFTPTKEDY QKVYNAIAER LANETDYDDG SYGPVLVRLA 130 140 150 160 170 180 WHASGTYDAE TGTGGSNGAT MRFAPESDHG ANAGLKYARD FLEPIKAKFP WITYSDLWTL 190 200 210 220 230 240 AGACAIQELG GPDIPWRPGR QDKDVSGCTP DGRLPDATKN QDHIRAIFGR MGFDDREMVA 250 260 270 280 290 300 LIGAHALGRA HTDRSGFDGP WNFSPTVFTN EFFRLLVEEK WQPRKWNGPK QFTDNTTKTL 310 320 330 340 350 360 MMFPTDLALV QDKGFRKHVE RYAKDSDAFF KEFSEVFVKL LELGVPFNSK VEDRYVFKRS E

References

[1]

"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACD01000026 Genomic DNA. Translation: EAA64750.1. Sequence problems.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2359. AniCcP02.
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_EMENI

Accession

Primary (citable) accession number: P0C0V3
Secondary accession number(s): Q5BCV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	November 25, 2008
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)