ID A0A2V1DY28_9PLEO Unreviewed; 430 AA.
AC A0A2V1DY28;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PVI02999.1};
GN ORFNames=DM02DRAFT_699336 {ECO:0000313|EMBL:PVI02999.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI02999.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI02999.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI02999.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KZ805336; PVI02999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1DY28; -.
DR STRING; 97972.A0A2V1DY28; -.
DR Proteomes; UP000244855; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF172; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12410)-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855}.
FT DOMAIN 10..364
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 363..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47842 MW; 890E50C471645546 CRC64;
MTTHPGWKRL NVGVIGGGIG GQATALSLRR QGHHVTIYER GDFAGEVGAS ISCAANATKW
LIEWDVNIEM GDPVLLKQLI SRDWKTGEPL SVYDLSDYKQ KWGYNYYMFH RQYMHAMIMD
SAVGSRGEGE PAKLVVNHKA KDINLETGTI TFHNGNTATH DVVIGADGIG STVRTVIGIK
PETTAAGWSC LHANVDTDQV VKLGLVDYSK NSAIEYWGGY DTHYKVVLSP CNGGKLLSYY
CFFPREAGDY QNQSWDEAAT VEELLAPYSD LDRQVFKHFE IGYEVRPWRL WKHQPYSHWQ
KGLACVIGDA AHPMMPDQSQ GACQAIEDAA TIGLVFSKAN FNGDIREALQ VYEKVRKPRG
TKVQAASARA SENMSERIGF SSNTDNPKYK VTDEKNKLTI EEMNSYDMRN DVAEKFAEHR
AKHGSNGTAS
//
