ID A1CUS2_ASPCL Unreviewed; 460 AA.
AC A1CUS2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Monooxygenase, putative {ECO:0000313|EMBL:EAW07059.1};
GN ORFNames=ACLA_087650 {ECO:0000313|EMBL:EAW07059.1};
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:EAW07059.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07059.1, 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; DS027060; EAW07059.1; -; Genomic_DNA.
DR RefSeq; XP_001268485.1; XM_001268484.1.
DR AlphaFoldDB; A1CUS2; -.
DR STRING; 344612.A1CUS2; -.
DR EnsemblFungi; EAW07059; EAW07059; ACLA_087650.
DR GeneID; 4699916; -.
DR KEGG; act:ACLA_087650; -.
DR VEuPathDB; FungiDB:ACLA_087650; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_5_1; -.
DR OMA; PPTHESM; -.
DR OrthoDB; 5491711at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase 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:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-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 Monooxygenase {ECO:0000313|EMBL:EAW07059.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 4..376
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 406..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 51175 MW; C6506E89D2928248 CRC64;
MSYRILIAGG GIAGLTASIA LAKELAEEPE VQIAVFESRT EDAIGDGGAI SLTPIAQYHL
DELGVLAELN RMGDDGGVEV DEINILSLRS GRSLGPLRFA DDTGRGYGRY KSRRVLRHAL
FRAMLAVARK YACISVVCDK KLVTATKTAD AVTLRFEDGT TATGDLLLGC DGVHSVVRTQ
LVDPGNHSEY TGISFIQSLA PTDRVTRPPH FDQTAIHLTR QGSLLASHCN ASRQTTFVAA
IMRVNEFIVE RYRAMASPDS TSAAHKSARM ALRYQVRSKF GVSAFPWVRD WIDQTHDWVL
YPIYQVQQRR KWYIDRVLLL GDAAHAMPPR EESAAYAIED AMLFARILAE DRDRALSEVF
LDYEDARRSL VDKAFDTTRK LWQSDLDKGF FPGHFRDCMS SIQLAPGSPR DIPSDRDCDP
SRKRIFPPPT HESMSDLSVY SLTSELEGMI QAEEVGITKR
//
