Reviewed, UniProtKB/Swiss-Prot Q4WPF8 (CCPR_ASPFU)

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:	AFUA_4G09110

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	366 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 + H2O2 = 2 ferricytochrome c + 2 H2O.
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 matrix By 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Mitochondrion Potential
	Chain	47 – 366	320	Cytochrome c peroxidase, mitochondrial		PRO_0000045286
Sites
	Active site	127	1	Proton acceptor By similarity
	Active site	266	1	Tryptophan radical intermediate By similarity
	Metal binding	250	1	Iron (heme axial ligand)
	Site	123	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WPF8-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 7E4567F4D0B438C7	FASTA	366	40,379
	10 20 30 40 50 60 MASAARSASR AFLRSTPTTS SFRPAVRAAR FALPAQGFRA AGRRGYASEA NSGKSSSNVF 70 80 90 100 110 120 LWAGLAVAGG AGAYLYLNGS DSVTSKTFVP GKEDYQKVYD AIARRLADET DYDDGSYGPV 130 140 150 160 170 180 LVRLAWHASG TYDKETGTGG SNGATMRFAP ESDHGANAGL KIARDFLEPI KAQFPWISYS 190 200 210 220 230 240 DLWTLAGACA IQELGGPTIP WRPGRQDKDV AACTPDGRLP DASKDQRHIR DIFYRMGFND 250 260 270 280 290 300 QEIVALIGAH ALGRAHPDRS GYDGPWDFSP TVFTNEFFRL LVDEKWQNRK WNGPAQFTDK 310 320 330 340 350 360 TTKTLMMLPA DLALIKDKEF KKHVERYARD SDAFFKDFSD AFVKLLELGV PFTSKAEDRY VFKTSE

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000005 Genomic DNA. Translation: EAL89876.1.
RefSeq	XP_751914.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	2363. AfumCcP02.
Genome annotation databases
GeneID	3509520.
GenomeReviews	Gene locus ccp1 in contig CM000172_GR.
KEGG	afm:AFUA_4G09110.
Phylogenomic databases
OMA	ATMRFAP.
Enzyme and pathway databases
BRENDA	1.11.1.5. 18841.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [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_ASPFU

Accession

Primary (citable) accession number: Q4WPF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 5, 2005
Last modified:	November 3, 2009
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)