ID A0A1Y2FTZ5_9BASI Unreviewed; 578 AA.
AC A0A1Y2FTZ5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:ORY87419.1};
DE Flags: Fragment;
GN ORFNames=BCR35DRAFT_277290 {ECO:0000313|EMBL:ORY87419.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY87419.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY87419.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY87419.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY87419.1}.
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DR EMBL; MCGR01000013; ORY87419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2FTZ5; -.
DR STRING; 106004.A0A1Y2FTZ5; -.
DR InParanoid; A0A1Y2FTZ5; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000193467; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000313|EMBL:ORY87419.1};
KW Peroxidase {ECO:0000313|EMBL:ORY87419.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467}.
FT BINDING 299
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT NON_TER 578
FT /evidence="ECO:0000313|EMBL:ORY87419.1"
SQ SEQUENCE 578 AA; 64466 MW; D423F07FB6ADE897 CRC64;
MLLEQVVIML STLPPNSVIG TSLTNTLIRF LWADLDHPPV AYVGANRYRQ ADGSGNSPWD
VQLGASHTAY ARSVPPMHPL PPNLPDPGTL FDALLKRDEF VPHPSGISSL LFNFATTIIH
SCFQTSLADP NINEASSYLD LSIFYGNNQD EQNKVRTGKL GLMHPDVVSS SRLFLMPAAV
TTLAVVFTRN HNLIAEKLLG INEGDHPDVV KYKEDTEKDP KGLVQQDEDL FQTARLVNCG
WFLNVIFQDY IRAILNINRS NSLWSLVPTG VIRPPLQGPF PRGVGNAVAV EFNILYRWHA
AISAQDEEWI EMEMKKWGPR GKQPVDYTEE DFFTVYFNMT KALGESQFSP LLLRERWNIP
GIKRKSDGYF EDRDLVNILS AATKNVAGAF KARGSPAAMR IIDMMGISAA RSTWGTCSLN
EFRKFLGLEQ FTQFKQWNSD PKIIDIASQL YTHVDNIELF PGLLAEEAKP SMPGSGLGPG
YTVSRAILSD AAALVRGDRY LTLPRLSNSM NANNFTVYQF EELTPDLEGG SFGGVLGKLF
MRVFPEQYSF NSAYALFAFS TPATTEDILR KLGIKQQY
//
