ID A1CN67_ASPCL Unreviewed; 466 AA.
AC A1CN67;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EAW07088.1};
GN ORFNames=ACLA_017910 {ECO:0000313|EMBL:EAW07088.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07088.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07088.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
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).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; DS027059; EAW07088.1; -; Genomic_DNA.
DR RefSeq; XP_001268514.1; XM_001268513.1.
DR AlphaFoldDB; A1CN67; -.
DR STRING; 344612.A1CN67; -.
DR EnsemblFungi; EAW07088; EAW07088; ACLA_017910.
DR GeneID; 4701874; -.
DR KEGG; act:ACLA_017910; -.
DR VEuPathDB; FungiDB:ACLA_017910; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_1_1; -.
DR OMA; CAEGIHS; -.
DR OrthoDB; 1422702at2759; -.
DR Proteomes; UP000006701; 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; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF236; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G12060)-RELATED; 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:UP000006701}.
FT DOMAIN 10..348
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 466 AA; 50488 MW; 787670098F2441B7 CRC64;
MTRDASTGIT VIVVGLGIAG LSAAIECHRQ GHKVIGLEKK GDAHQLGDII GLSGNGLNVL
SRWSSADESI ISRLAAVGSE LSSVEVYSDA GECKHVIPFG ADDPAQGLFL RRSDLVDAMY
QYATTELGLD LRFGVTVDEY WETETEAGVT INGKEKITGH CVIAADGLYS KARAIITGEE
PLGDAAALLQ TGGAIFRSNF DASEVINDPD ARWVLEGTAE HDRHEIYFGR DVTILVGTIG
KGKYVWWNCP HRDVAKATEN WVQEATVDPV LAYIQDWPIA KKLSAVISKT PQGKCFNHAL
VTRKPLGTWV SPKGRMILIG DAAHPFLPHT GQGANQSIED AAVVAICLRL SSLAAEDGEG
DGVPLALRAM EKLRHKRVTV IQQGSIEAQE VTLEADLDQN ASNDRFNAIA RPGWIHCYDC
VSHTHEEFDR VAEAVRKGTE YIPTNVPVDG KFHAEDDYRL AKGTTE
//
