ID   CCPR_EMENI              Reviewed;         361 AA.
AC   P0C0V3; Q5BCV0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-MAY-2009, entry version 27.
DE   RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE            Short=CCP;
DE            EC=1.11.1.5;
DE   Flags: Precursor;
GN   Name=ccp1; ORFNames=AN1630;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 4;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 ferrocytochrome c + H(2)O(2) = 2
CC       ferricytochrome c + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit (By similarity).
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c
CC       peroxidase subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64750.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AACD01000026; EAA64750.1; ALT_SEQ; Genomic_DNA.
DR   PeroxiBase; 2359; AniCcP02.
DR   BRENDA; 1.11.1.5; 3859.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR002207; Asc_perxdse.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Transit peptide.
FT   TRANSIT       1     41       Mitochondrion (Potential).
FT   CHAIN        42    361       Cytochrome c peroxidase, mitochondrial.
FT                                /FTId=PRO_0000045292.
FT   ACT_SITE    122    122       Proton acceptor (By similarity).
FT   ACT_SITE    261    261       Tryptophan radical intermediate (By
FT                                similarity).
FT   METAL       245    245       Iron (heme axial ligand).
FT   SITE        118    118       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   361 AA;  39937 MW;  5EF75C2E9EEDC530 CRC64;
     MASAARSASR AFLRSSLRPA VRSSRFALPT QGLRVASRRG YSSEASSGKS SNTLLWAGVA
     LAGGAGAYFY LQGGDVGAST KVFTPTKEDY QKVYNAIAER LANETDYDDG SYGPVLVRLA
     WHASGTYDAE TGTGGSNGAT MRFAPESDHG ANAGLKYARD FLEPIKAKFP WITYSDLWTL
     AGACAIQELG GPDIPWRPGR QDKDVSGCTP DGRLPDATKN QDHIRAIFGR MGFDDREMVA
     LIGAHALGRA HTDRSGFDGP WNFSPTVFTN EFFRLLVEEK WQPRKWNGPK QFTDNTTKTL
     MMFPTDLALV QDKGFRKHVE RYAKDSDAFF KEFSEVFVKL LELGVPFNSK VEDRYVFKRS
     E
//