ID   A0A1Y2GJ69_9FUNG        Unreviewed;       303 AA.
AC   A0A1Y2GJ69;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=BCR41DRAFT_308542 {ECO:0000313|EMBL:ORZ10632.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ10632.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ10632.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ10632.1,
RC   ECO:0000313|Proteomes:UP000193648};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:ORZ10632.1}.
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DR   EMBL; MCFF01000030; ORZ10632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GJ69; -.
DR   STRING; 64571.A0A1Y2GJ69; -.
DR   InParanoid; A0A1Y2GJ69; -.
DR   OrthoDB; 2332834at2759; -.
DR   Proteomes; UP000193648; 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; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR   PANTHER; PTHR47356:SF3; FAD-DEPENDENT MONOOXYGENASE SRDH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
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:UP000193648}.
FT   DOMAIN          44..214
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   303 AA;  33284 MW;  0C03DA5ED8253E40 CRC64;
     MTERRLTNPS SFTRTTSSIS TVHSASSSTI FQYPGFHEET PTFKVLIVGA GIGGLMLGLC
     LERAGIDYVI LERMHDLLDA PRSTVKLAAN TLGVVEQLGL LDEVMKIAMP ISGLTLRKHN
     MSAVGKIDFS FHKERHGHYS FIVQRTELCQ LLISRMRNDR IQWGRKVLEI VSGNAGVQCR
     CANGHVVQGD VLVGADGAHS AVRQNLFKTL KSKSLLPKQD MESLKFSQNA LNGLTNPLDP
     ARFPDVAKTF CEVHIIIGKD SPSPHTVSTL HCFNSNLSRA LWLSLALSRS LSLSLSLSLC
     IVY
//