ID   CCPR_NEUCR              Reviewed;         358 AA.
AC   Q7SDV9; V5IPZ8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE            Short=CCP;
DE            EC=1.11.1.5;
DE   Flags: Precursor;
GN   Name=ccp-1; ORFNames=NCU03297;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM002236; ESA44097.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44098.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44099.1; -; Genomic_DNA.
DR   RefSeq; XP_011393142.1; XM_011394840.1.
DR   RefSeq; XP_011393143.1; XM_011394841.1.
DR   RefSeq; XP_011393144.1; XM_011394842.1.
DR   AlphaFoldDB; Q7SDV9; -.
DR   SMR; Q7SDV9; -.
DR   STRING; 5141.EFNCRP00000002864; -.
DR   PeroxiBase; 1989; NcCcP.
DR   EnsemblFungi; ESA44097; ESA44097; NCU03297.
DR   EnsemblFungi; ESA44098; ESA44098; NCU03297.
DR   EnsemblFungi; ESA44099; ESA44099; NCU03297.
DR   GeneID; 3880372; -.
DR   KEGG; ncr:NCU03297; -.
DR   VEuPathDB; FungiDB:NCU03297; -.
DR   HOGENOM; CLU_036959_1_1_1; -.
DR   InParanoid; Q7SDV9; -.
DR   OMA; NGPKQYE; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356; PTHR31356; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
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   Reference proteome; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..358
FT                   /note="Cytochrome c peroxidase, mitochondrial"
FT                   /id="PRO_0000045295"
FT   REGION          192..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   ACT_SITE        258
FT                   /note="Tryptophan radical intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   SITE            115
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   358 AA;  39818 MW;  8F9E48B7328CD87B CRC64;
     MAASRTATRT LRALRTSTRP ALTAAPRAAF RQGGRRLYSS EPAKSGGSNI WAWAIGAGAL
     GAGGLWYLNQ DGASATPKVF APKFDDYQAV YNEIASRLEE KDDYDDGSYG PVLVRLAWHA
     SGTYDKETGT GGSNGATMRF APESDHGANA GLKAARDFLE PVKAKFPWIT YSDLWILGGV
     CAIQEMLGPQ IPYRPGRQDR DAAGCTPDGR LPDASQAQDH LRNIFYRMGF NDQEIVALSG
     AHALGRCHAD RSGFDGPWTF SPTVLTNDYY KLLLDEKWQW KKWNGPKQYE DKKTKSLMML
     PADMALIQDK KFKQWVEKYA ADNELFFKDF SNVIVKLFEL GVPFAENSER WVFKTVNA