ID A1CN64_ASPCL Unreviewed; 490 AA.
AC A1CN64;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EAW07085.1};
GN ORFNames=ACLA_017880 {ECO:0000313|EMBL:EAW07085.1};
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:EAW07085.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07085.1, 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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; DS027059; EAW07085.1; -; Genomic_DNA.
DR RefSeq; XP_001268511.1; XM_001268510.1.
DR AlphaFoldDB; A1CN64; -.
DR STRING; 344612.A1CN64; -.
DR EnsemblFungi; EAW07085; EAW07085; ACLA_017880.
DR GeneID; 4701354; -.
DR KEGG; act:ACLA_017880; -.
DR VEuPathDB; FungiDB:ACLA_017880; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_1_1; -.
DR OMA; FENHHSY; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF32; FAD-LINKED OXIDOREDUCTASE AFOF; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..490
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633302"
FT DOMAIN 65..236
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 490 AA; 54078 MW; B151E9E65A9D4A3A CRC64;
MISYIVPLLA TLPGLVASAA TLAPRDDGPA DFKAIFDPVL SPGARLYLPG DPEYFNMTSR
WSNLFDPSYI AAIQPANEKD VQNIIKAANK HDIPFLATGS AHSVKPGYTT VKNAINIDLS
LLKNACLDYE KDTITIGPGV LNGEVYDMVY NVKKELPLST DRCISALGTM IGGGLGTLYS
VRGILADSLV SAHVVTAEGE LVTASATENP DLFWAIRGAG HNFGVITSAT LKMYDLTNGG
NSVFGDFVIP NARNASAFEL LKSVDEDLPA GVFWGILGDF NHTTKQPGLH VRLLVFGDDA
VAAPHLDKIM ALDPEVTFWK NTTWNTYGEE TPIMCNRRWN SNMYSMGLKH TDVDTMVAAF
TNWSTFAAEH DWFNGLLMIE RHSEATVMAV PEKERGVFPW RDTKIQMVFV NYMDDPKYAA
PLDDFIQPTR AEIQSVMGFE NHHSYVNEAY GDEGPAVWYG EWNLPRLVEL KRKWDPKRQF
GAGMPIPLSL
//
