ID A0A4Q4WPW3_9PEZI Unreviewed; 360 AA.
AC A0A4Q4WPW3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=DL768_004673 {ECO:0000313|EMBL:RYP49631.1};
OS Monosporascus sp. mg162.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=1081914 {ECO:0000313|EMBL:RYP49631.1, ECO:0000313|Proteomes:UP000292795};
RN [1] {ECO:0000313|EMBL:RYP49631.1, ECO:0000313|Proteomes:UP000292795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG162 {ECO:0000313|EMBL:RYP49631.1,
RC ECO:0000313|Proteomes:UP000292795};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00003917}.
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 Evidence={ECO:0000256|ARBA:ARBA00035967};
CC -!- SUBUNIT: Forms a one-to-one complex with cytochrome c.
CC {ECO:0000256|ARBA:ARBA00038574}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00005997}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYP49631.1}.
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DR EMBL; QJNY01000138; RYP49631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4WPW3; -.
DR STRING; 1081914.A0A4Q4WPW3; -.
DR Proteomes; UP000292795; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd00691; ascorbate_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
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:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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 {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000292795};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 100..359
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 360 AA; 39845 MW; AA44FCDDF62D4760 CRC64;
MSASTASRQF ARVALRTSAR NAIVTAPRHA FRQGGGRRFY SSESPKNSSS SALLYLAGAA
VAGAGGYWFY TQGGTSSASA KVFTPTKEDY QKVYDEIASR LEENDDYDDG SYGPVLVRLA
WHASGTYDKE TGTGGSNGAT MRFAPEGDHG ANAGLKIARD FLEPVKQKFP WISYSDLWIL
GGVCAIQEMQ GPIIPYRPGR TDRDAAACTP DGRLPDGAKG ADHLRGIFYR MGFNDQEIVA
LAGAHALGRC HTDRSGFDGP WTFSPTVLTN DYYTLLLKEK WSWRKWDGPK QLQDGSKSLM
MLPADYALIQ DKAMRQWVEK YAKDNDAFFN DFRDVIVKLF ELGVPFKEGT ERWTFKPTNA
//
