ID A0A139HR34_9PEZI Unreviewed; 441 AA.
AC A0A139HR34;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Heme haloperoxidase family profile domain-containing protein {ECO:0000259|PROSITE:PS51405};
GN ORFNames=AC578_3442 {ECO:0000313|EMBL:KXT04896.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT04896.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT04896.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT04896.1,
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:KXT04896.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZN01000017; KXT04896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HR34; -.
DR OrthoDB; 1830290at2759; -.
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:SF16; 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}.
FT DOMAIN 56..289
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 441 AA; 47106 MW; 8C1F93724159885D CRC64;
MKLSPTLALP ALAAAFPGVV KDRGLTNDLN ILVGDVEGLL GSVASGIDPN NYRPEPEYPF
IAPGPNDSRG PCPGLNLLAN HGYLPRDGHV NGAQVLEAVS RGFNMAADLA TVLIVFAVLT
DGDIETESWY LGSAPTHIGG LNRHSTVEAD ISPNREDYYL GCGDNHHLSS RIFKQNVQFA
AQDPEKQFNY DVMARHYGAN SRFSQQYNPY IYYFPFPSIV SVVAFNFYPE YFSNGTYGFG
GVANYESISS IVGAKFDKET GNFEYVPERY PEQGWYRRAT PYGAIQALTD GFTRIYPANP
VPMPIAQLGT PNLNVSTILC DVFMGLNSIT PLPLAGEAEA VDAGITWALA KLGAVGLSGT
ILGCPTSAIS TNYLYPNSTT IGGPLGPPPA AVANAGNNVY NKTYFTTAPT TPQCNHVSEP
GAKKGVFGGS IGAFPLFGKS S
//
