ID A0A0W0FVA0_9AGAR Unreviewed; 1094 AA.
AC A0A0W0FVA0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative heme peroxidase {ECO:0000313|EMBL:KTB40142.1};
GN ORFNames=WG66_7263 {ECO:0000313|EMBL:KTB40142.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB40142.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB40142.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB40142.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) 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:KTB40142.1}.
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; LATX01001604; KTB40142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FVA0; -.
DR eggNOG; KOG2408; Eukaryota.
DR Proteomes; UP000054988; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
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:0000256|ARBA:ARBA00022964};
KW Peroxidase {ECO:0000313|EMBL:KTB40142.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 385
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"
SQ SEQUENCE 1094 AA; 121701 MW; 18A7571E86D28D66 CRC64;
MALNISPLEK FALASDAVYL KGRPLPTAPD GKYDPPSQEP GQKQERSALG GIFKRLDAQA
KKGLITPDPT VVAGFLDTVL HPDATDDRKG AFSAGLTLLS RLPPNSDAAK KMSDGAVGLL
YNTLPHPPET LLGPQYSFRQ ADGGNNNIQV PSIGRAGEPY ARSVQGKWCV SPQDLPDPAL
VYDILLRRRK VVEHPNGNAS FTFAFASLVT HSLFRSRMGQ WHINDTSSYL DLSPLYGINQ
ETVDAVRNKD LGRGLLYPDT FSEERLLFLP PCASALLVIL SRNHNYIAEK LLKINERGRW
TDPPPEDKAK RDQQDEEIFQ TARLINGGHF MSLIMGDYVA GFLGLSEGNA WNMNAFDPIK
INDVEVKRGE GNHCSVEFNI LYRWHATTSE ADAKWINDFF ASEIPSAKSP EDITFGQFAQ
TFVRKLEEEK KKAPKDREFG GMKRGPDGHF SDDELANILH TATENPACSF GAHGTPDALK
IIEIMGINQA RQWGLCTMNE FRKFLGLKQF ETFEEWNPDP AVAGPARRLY KHIDNLELYT
GLQCESLMPL SGGLRFACGY TTTRAVLSDA IALIRGDRFY TTAFTPANLT TWGYQDCLRD
PNNGGFGGEM PKLLSRHLPR HYPYNSVYTC FPYFTPKKMH ESLTRLQLAD KYTFERPKPA
PVVKVLNTMQ AIKYVFSKPT EYPVVYDMKG LGGGYGFMLT FDEATKHDAD RNLALHALFP
TKDSLNEYRK WYRDQVTLRI RERSWKYDGV PGRFVDIVND VINSTSIAWA SERLCGLDMK
TKENPSGMYT EAEIYEMFTT MFTLIFLAIG DNEHGFSLRK QVLQAGGVTQ AMIAKNVFDC
APKAAGASNV FLGALSTVAS TVHSVIDNKP CYAFLRRLAE TGRPINEIVA MVVGLAVGSS
VNYAQAAVHV IDFYMAEERK AERAEIIKLS QSKDSEGKGW DTLVGYVREA MRLNPQVTGL
YRDALVDAVI SQGSGLPDIQ LKKGDRIFGS LKNAHLNPDD FPDPLTINPT RPASAYQYNG
SGFHQCPGVN YAEQTIAEIV KVVFSLPNIR RAPGNDGKLA GFEEIQNETK TKVYVTPDGE
TSPWPGKMYL VYDA
//
