ID A0A139HBV3_9PEZI Unreviewed; 429 AA.
AC A0A139HBV3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Heme haloperoxidase family profile domain-containing protein {ECO:0000259|PROSITE:PS51405};
GN ORFNames=AC578_901 {ECO:0000313|EMBL:KXS99929.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS99929.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS99929.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS99929.1,
RC ECO:0000313|Proteomes:UP000070133};
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:KXS99929.1}.
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DR EMBL; LFZN01000083; KXS99929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HBV3; -.
DR OrthoDB; 1782787at2759; -.
DR Proteomes; UP000070133; 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:SF1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..429
FT /note="Heme haloperoxidase family profile domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007806441"
FT DOMAIN 77..317
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
FT REGION 163..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 45551 MW; 8280B5CAC7DC4F5A CRC64;
MKFSTTQALL GAVPLAAAFP AAVFEAVAND PALAARAEEI RSQLDTRQVA ADGATKLFEP
VPIFDEKAQF VDVGPGSGHE YVAPGPNDLR GPCPGLNAFA NHGFLPHNGY ATITQFVDAT
TNVVGMGPVL AAFLAALGAG IDGDGLSWSI GGTPGPGIGG PLSSQGHGIS GSHNKYESDA
SPTRPDLYQS GNDYMTMANQ FQELIDASPG GVITLDSLTK HRSNRFDHQI ATNPYFFNGP
FTGVLVQPAA YTFIYRFMAN HSAENPYGEL TYDVLKAWFG ISGDSGSYVA NQGQEYIPMN
WYKRAVQYPY ENTYFLADAT NAALLYPKFL NVGGNTGTTN SFTGIDVRNI SGGLFNSGTL
AQDNNFACLA YQFAAQAKPD LALATVTQLT NAVGSLSSQL GCPQLQKVDD DQLMQFPGYA
RSTKDGITN
//
