ID A0A0N1HSK9_9EURO Unreviewed; 489 AA.
AC A0A0N1HSK9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aromatic peroxygenase {ECO:0000313|EMBL:KPI39203.1};
GN ORFNames=AB675_4726 {ECO:0000313|EMBL:KPI39203.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI39203.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI39203.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI39203.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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:KPI39203.1}.
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; LFJN01000016; KPI39203.1; -; Genomic_DNA.
DR RefSeq; XP_017999166.1; XM_018144885.1.
DR AlphaFoldDB; A0A0N1HSK9; -.
DR GeneID; 28736764; -.
DR OrthoDB; 1782787at2759; -.
DR Proteomes; UP000038010; 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:UP000038010};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005873541"
FT DOMAIN 84..341
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 489 AA; 53212 MW; 8C75133F27DE5C24 CRC64;
MKYQSLALAA TTFLTCASAF PRMDAEQLKA YNEASKRSAE PAACPYAKRE AEAAADPSCP
FAKIANKFKR STFNAEQQHI RTDGEYAFVP PNFQSGDQRG PCPGLNALAN HGYLPHSGVA
DMQTIIKATN EVYGMSLDLG GFLAVYGTVF DGNPLSTSPG YSIGGPSKDS QNILNGVGLL
GTPSGLSGSH NKYESDVSPT RADLYLTGNN FHNVKDRFVD YYYALKENTP APEQYTALAP
FHAQRYEESL MSNPYFFYSP FAGILVSPAG YSFPPRMMAN HSEEYPEGYL SRETFSTFFG
VDTHESQNPQ DFEVKQGWER IPDNWYKRPI NDEFSIPDFL LDVLQHAEYD PRLLSFGGNT
NGVNTFAGLD IGDLTGGVLN FANLLDPNNL LCVALQIAEA AAPDVLGSLY TDVKKAMTPL
TDKVTQLLAG KGCPQLQKIN SELFEKYPGY TESYGSYAGF SEIGTDPVDG VLEGVTGVLG
GLIPTGQKV
//
