ID Q0CSB9_ASPTN Unreviewed; 572 AA.
AC Q0CSB9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=ATEG_03415 {ECO:0000313|EMBL:EAU36689.1};
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:EAU36689.1, 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 -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; CH476597; EAU36689.1; -; Genomic_DNA.
DR RefSeq; XP_001212593.1; XM_001212593.1.
DR AlphaFoldDB; Q0CSB9; -.
DR STRING; 341663.Q0CSB9; -.
DR EnsemblFungi; EAU36689; EAU36689; ATEG_03415.
DR GeneID; 4317597; -.
DR VEuPathDB; FungiDB:ATEG_03415; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_4_1; -.
DR OMA; FKWVRID; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
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 InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF5; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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:UP000007963}.
FT DOMAIN 6..367
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 572 AA; 63358 MW; EC5023922A964CCB CRC64;
MATEFKTDVL VVGGGPVGLL IAYGLARQGV DSIVVEKHNK EQQAMYGRAT TLYPRTLEML
DQLELLDEMN QIGFVARNSV TYKDGKQVTS RGWHVMYERM HGTFLDYCLN IRQKFSESVF
RDAYSKIGGK LFIGWMLEDF TVDNSMEGDF KVTSRLTRVN SGEAVTVKRY YALRKYIVGA
DGGSSSVRRL AGIPFEGDHT NFKWVRIDGY FKTNMPNADI GYASIESKTH GNVLWVQLDH
GAKRIGFAMT EEMLAKYGNN LTEDQAVAEA IKSMEPFSLE IEKVEWWTLY SINQRVADAF
FVNDRVLLAG DACHTHSSGA AQGMNTGTHD AVNLAWKLGG VVKGWYGSEI LQTYEDERRP
AAQHLIELDK DFSATISGRV PEKYKGSLLD ANELFTKLFD ESNLFNIGLG ISYGENAINK
TPSTGMISAG RRGPDALIMA PGSRVPVRLY QVTKNTGQWC IIVFAGRPDV TREVMSKSVP
MLEALQSTLP KDMVRFITLA AGSVDDGDSA FGNPRIGNIY YDQDRSAHER YSIATSKGAV
VVLRPDGTLG YATSLDDMDG VKDFFAGFVL SA
//
