ID   A0A178AE00_9PLEO        Unreviewed;       426 AA.
AC   A0A178AE00;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Cloroperoxidase {ECO:0000313|EMBL:OAK95783.1};
GN   ORFNames=IQ06DRAFT_283601 {ECO:0000313|EMBL:OAK95783.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95783.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK95783.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95783.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441721; OAK95783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AE00; -.
DR   STRING; 765868.A0A178AE00; -.
DR   InParanoid; A0A178AE00; -.
DR   OrthoDB; 1830290at2759; -.
DR   Proteomes; UP000077206; 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:SF15; HEME_HALOPEROXIDASE DOMAIN-CONTAINING PROTEIN; 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, ECO:0000313|EMBL:OAK95783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..426
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008081661"
FT   DOMAIN          88..328
FT                   /note="Heme haloperoxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51405"
FT   REGION          43..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  45293 MW;  0683CC0E02AC0D46 CRC64;
     MHTLSSILLL SSATTAWGYG WVAGQAGVDS SLLRNARYAN QRRQSSCPFN SDHKGAAPYS
     DDYPYTGAKN GVPGSGKGGI KVPADGDTAH QYTAPGPNDI RGPCPGLNAA ANHNFLSHDG
     ITNFNELVDA QQNVYNVGYD LAVLLAVLGI VADGDPVTTK LSIGCDATSR TALLPLLGNQ
     PGLNGHNKFE GDTSLTRNDY FLANGDDYSF NGSLFAEMKS YADSVSGGNF DLNALAAYRS
     KRYDESVQTN ANFFFGPLSL LLYGAASFLY ELFPSFGNTG TPDLETMKSF FGAVEDSSAP
     GGWAHVPERI PENWFSRTAP YTNNDVTLQI LEMYVKYPKL FGGNVGTNNF DALSTPFGII
     TNGKLPDAAT AGDVLCLLYQ LGTMAVPSSL SVVTDITADI LNFSVGKLNP VFANQGCALK
     PDQTQG
//