ID Q0CMW0_ASPTN Unreviewed; 474 AA.
AC Q0CMW0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ATEG_04974 {ECO:0000313|EMBL:EAU34043.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34043.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CH476600; EAU34043.1; -; Genomic_DNA.
DR RefSeq; XP_001214152.1; XM_001214152.1.
DR AlphaFoldDB; Q0CMW0; -.
DR STRING; 341663.Q0CMW0; -.
DR EnsemblFungi; EAU34043; EAU34043; ATEG_04974.
DR GeneID; 4321086; -.
DR VEuPathDB; FungiDB:ATEG_04974; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_10_0_1; -.
DR OMA; SLERWSE; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000007963; 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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
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:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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:UP000007963}.
FT DOMAIN 42..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 474 AA; 51308 MW; 056F60C54AD25EF9 CRC64;
MAAFPITLEQ AQDLRSRLAD SAIVLLPDSD GYDDSLKKWS TIGCQRSGVT VRPKNAQSIA
KAVLFASHHK IDLAVKGGGH STDTSSSTDG GILIDLSSMK EISVDESSKQ IAAQGGALWE
DVYQVTSQHG LAVVGATISC TGVGGLTLRG GYGYLTPQHG LVIDNLLEAH VVTADGSILT
ASAQQNPDLF WAVRGAGQNV GVVTELVFQA YDQKHMVWSG TRVYGSDKLS EIHEALDAAL
VHPHGKAAAQ CLYSLSPQPG NPPVVTIVLF FDGPEKEARS HFSRLLSIEC VTDDMRMRDY
AEANSMLNAG VPPGGRKVIL GVQWVSPVRL EFASAVMEEV SCHLAAETDM SQSVLVIDYF
DQKQACCTPM EATAFPARRD TLNGALILQW TDQEKDKDVL SWGQKIQMMC EDELRRCGRT
PDKLVSNFLG YTTGDSVSAV DMFGTNASRL LEIKKRYDPQ NLFNKLNPLN SGTK
//
