ID A1D2P0_NEOFI Unreviewed; 688 AA.
AC A1D2P0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=NFIA_013720 {ECO:0000313|EMBL:EAW22683.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22683.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027688; EAW22683.1; -; Genomic_DNA.
DR RefSeq; XP_001264580.1; XM_001264579.1.
DR AlphaFoldDB; A1D2P0; -.
DR EnsemblFungi; EAW22683; EAW22683; NFIA_013720.
DR GeneID; 4591439; -.
DR KEGG; nfi:NFIA_013720; -.
DR VEuPathDB; FungiDB:NFIA_013720; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_023116_0_0_1; -.
DR OMA; GQFPMGD; -.
DR OrthoDB; 1557755at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF110; DUF6314 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
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:UP000006702}.
FT DOMAIN 93..170
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 688 AA; 75961 MW; 5DAD1904F0465EAB CRC64;
MRTNLSRFTV SFSDLAWESV LGGTDVPMFP QAWQVGRYLE TYAERYLSDQ VVRLGCEVVR
AVREVVGGQP RWTVQWVQRS GNEEQGDDTE QRAVETEYFD FLVVASGYFS RPYTPDIPEL
AAFADRTVHS SALRSLEDLD AIVEKGSDGG RLVVVGGSMS GVEAASSLAL HVSSLRYAPG
SSVQTGSFPE VYHISSRPFW TVPTYIPHAQ RDNATGTETV SLLPLDLAMY DLARRPPGPV
EYAFGPVSAA QVAKVNDYFR SVLGEDYTSI GPGDNGLKGG EEETLQPRWV GIGNDYAEFV
RSKAIRTVIG RVSAVHASSP GPAKVDIELP GKESMSLYDV AGIVLATGFR PFPSLAFLPE
DVLSALEYSP DDSFFPLILD PKGASNANIP DLGFVGFYRG PYWGVMEMQA RSLAQTWAGD
DTEHGIQFSA TELESKAQER QKVREYRSAD PNLHRGQFPM GDYTGLMESF ARDLGICCAP
LTELDERPGP VVPARYAMSG PGTADVQTSL QALQETLQPR RESASPAVTM AVFRALHGSW
DFTRSGQDGI TSGISTFFPR YPSSPAYEKE YLYEESGQKL ASFVYRLTDS PQDAQITIWS
VDSQDKTAVA LLYGLRILNQ EGSSTSRQGE YTIRATSSQW SSNCTYEYVF RFNGVAISSW
EYTVRRPLDH GFVLNRTIYR RVQKCDGH
//
