ID A0A397HKE4_9EURO Unreviewed; 568 AA.
AC A0A397HKE4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV56_107973 {ECO:0000313|EMBL:RHZ63447.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ63447.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ63447.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ63447.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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 FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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:RHZ63447.1}.
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DR EMBL; NKHU02000029; RHZ63447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HKE4; -.
DR STRING; 41047.A0A397HKE4; -.
DR VEuPathDB; FungiDB:CDV56_107973; -.
DR OrthoDB; 2041362at2759; -.
DR Proteomes; UP000215305; 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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00411; PNDRDTASEI.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305}.
SQ SEQUENCE 568 AA; 64337 MW; 11A1736999CF136D CRC64;
MGSLGETVSR PKKYNTELTD YSAVHADKTG PYAENLEVDA LIVGAGFAGV FMLKTLRDRG
LKTVIFEAGN DTGGTWRWNC YPGAGVDSEV PEYEFSWPEV YKTWNWPNNY PDYKNLRAYF
DHVDKVIGIK KDCAFNTVVI GAQFDTGEGK WNIKTADGRT TKAKYLVLGT GFAAKRYIPP
WPGMDKFKGI VHHSSFWPEE EVDVKNKRCA VIGTGASGVQ ITQAWGPVAG DLKVFQRTPN
LAVPMRKRDL TVEEQERIKP YYPELFRYRE TTFAGFMYDW CERNTFDDTP EEREALYERV
WQDGGFRFWV SLYKDNLVNP EANKESYDFW AKKTRARIGD PKLRELLAPR EMPHYFGIKR
PCLEQTYFEQ FNRESVHLVD IKNNPIKEFT ETGITLEDGT HHELDVVAVA TGFDVVTGVM
TQLGLRSIDG AELETEWIPG AKTYLGTTVS GYPNMFHIYG PHGPTLLSNG PTSVAVQGRW
IADAIAKIEA NGIKYINPKI EAANKWKKHV VELNDRTLFP TTRSTYMGGS IPGKVYEPVC
YAGGIPTYAM EIRRALDNWE EGFDVVKA
//
