ID   A0A139H8P3_9PEZI        Unreviewed;       281 AA.
AC   A0A139H8P3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Heme haloperoxidase family profile domain-containing protein {ECO:0000259|PROSITE:PS51405};
GN   ORFNames=AC579_8935 {ECO:0000313|EMBL:KXS98789.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXS98789.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXS98789.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXS98789.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the chloroperoxidase family.
CC       {ECO:0000256|ARBA:ARBA00025795}.
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:KXS98789.1}.
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DR   EMBL; LFZO01000733; KXS98789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139H8P3; -.
DR   STRING; 113226.A0A139H8P3; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.489.10; Chloroperoxidase-like; 1.
DR   InterPro; IPR000028; Chloroperoxidase.
DR   InterPro; IPR036851; Chloroperoxidase-like_sf.
DR   PANTHER; PTHR33577:SF9; PEROXIDASE STCC; 1.
DR   PANTHER; PTHR33577; STERIGMATOCYSTIN BIOSYNTHESIS PEROXIDASE STCC-RELATED; 1.
DR   Pfam; PF01328; Peroxidase_2; 1.
DR   SUPFAM; SSF47571; Cloroperoxidase; 1.
DR   PROSITE; PS51405; HEME_HALOPEROXIDASE; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..281
FT                   /note="Heme haloperoxidase family profile domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007296954"
FT   DOMAIN          27..236
FT                   /note="Heme haloperoxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51405"
SQ   SEQUENCE   281 AA;  30464 MW;  120CBA1137E4B8EE CRC64;
     MFFRAELAFG ATLIASATAG PAASPGSFTN WQAPGPNDVR SPCPALNSLA NHGFIPHSGR
     GMTLPILLSG LSAGLNIGDD ATTVFWGGGV LSSPNPLGGQ FDLSDLKKHN FPIEHDASLS
     RQDFYFGNPQ PFNQTIFNSF FSYFSGQTTC TIPTTSKAKY SRVQDSQNRN PTFTYGPREF
     VLSYGEAALF LSTMGNPDTG NPPTKYVKIF FEQERLPYNE GWRRPDQATT LLSLGNLVNQ
     LYTASPEPLP EGLEVITVGA IKDAWEGINP VTGILGEWML V
//