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Database: UniProt
Entry: A0A0F4Z786_9PEZI
LinkDB: A0A0F4Z786_9PEZI
Original site: A0A0F4Z786_9PEZI 
ID   A0A0F4Z786_9PEZI        Unreviewed;       467 AA.
AC   A0A0F4Z786;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TD95_001419 {ECO:0000313|EMBL:KKA26367.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26367.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA26367.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26367.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:KKA26367.1}.
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DR   EMBL; LAEV01002193; KKA26367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4Z786; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000033483; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033483}.
SQ   SEQUENCE   467 AA;  51329 MW;  3E1BC0AF9B60A9C2 CRC64;
     MPRLAVNSVA VIGAGPCGLA AAKYLLAEKA FSRIQVFDQR PIAGGLWNYT PLSVLDAGFT
     IPRTAPSTVL DTLVAQPGGP AQVVSPVYDL LETNIPKDLM GYTDGGFPSN EALFPHHTRV
     AAYLHSCAVP LQSVLRLQTQ VRDVRKVGGV WRVTIRDLVA DKETTEEFDA VVVASGHYND
     PYIPDIKGLK EFAEAYPGAV MHSKFYQRPD EFKDKKVIVV GNSASGIDLS AQISTFSKAP
     VLASERTATP ASASTNPLIR TVPEITSFSL PSRQAHFSDG SVESDIDAVV FCTGYFYSFP
     YLRDLPVPLG DGTHVAGLYE HVLYAADPSL SFLGVPQRIV PFPVAEAQSG LVARALAGRW
     EVPTRAEMEA WETELRAQLP DVRNLHTLKF PKDADYINRL YEMSASADKK EGLERDGMGK
     EPPYWGPEKQ WLREQFPMIK AVSRELGTKR MNIRTLKELG FEYPGKN
//
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