ID   CCPR2_MAGO7             Reviewed;         300 AA.
AC   A4R606; G4NG79;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative heme-binding peroxidase;
DE            EC=1.11.1.-;
GN   ORFNames=MGG_10368;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   CLASSIFICATION.
RX   PubMed=17126331; DOI=10.1016/j.febslet.2006.11.017;
RA   Zamocky M., Dunand C.;
RT   "Divergent evolutionary lines of fungal cytochrome c peroxidases belonging
RT   to the superfamily of bacterial, fungal and plant heme peroxidases.";
RL   FEBS Lett. 580:6655-6664(2006).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM001236; EHA47036.1; -; Genomic_DNA.
DR   RefSeq; XP_003719403.1; XM_003719355.1.
DR   AlphaFoldDB; A4R606; -.
DR   SMR; A4R606; -.
DR   STRING; 318829.MGG_10368T0; -.
DR   PeroxiBase; 2342; MgrCcP01.
DR   EnsemblFungi; MGG_10368T0; MGG_10368T0; MGG_10368.
DR   GeneID; 2681979; -.
DR   KEGG; mgr:MGG_10368; -.
DR   VEuPathDB; FungiDB:MGG_10368; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_036959_0_1_1; -.
DR   InParanoid; A4R606; -.
DR   OMA; RTDYVDD; -.
DR   OrthoDB; 1228462at2759; -.
DR   Proteomes; UP000009058; Chromosome 6.
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; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
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; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Putative heme-binding peroxidase"
FT                   /id="PRO_0000363408"
FT   REGION          44..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        39
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   ACT_SITE        179
FT                   /note="Tryptophan radical intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   SITE            35
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   300 AA;  32999 MW;  3F86A645596DD8E6 CRC64;
     MASKPGDFDA VRKDIVSLLD QPEYDDGSAG PVLVRLAWHS AGTYDKSTDT GGSNGAGMRY
     EAEGGDPANA GLQNARQFLE PVKARHPWIT YADLRTLAGV VAVRAMGGPE IPWRAGRTDF
     ADDSRVPPRG RLPDATQGAA HVRDIFYRMG FDDREIVALS GAHSLGRCHP ANSGFEGKWV
     NNPTRFSNQY FRLLLSEDWR EKTVAGTGLK QFVAVDEVTG DELMMLPTDL SLTSDPVFAR
     WVKVYRDDQD LFFADFAKVF DKLMELGIKR DAEGKVINKE NVEGGYVSAP KKQGKIASKL