ID Q0CRU5_ASPTN Unreviewed; 388 AA.
AC Q0CRU5;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=FAD linked oxidase N-terminal domain-containing protein {ECO:0000259|Pfam:PF01565};
GN ORFNames=ATEG_03589 {ECO:0000313|EMBL:EAU35391.1};
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:EAU35391.1, 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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CH476598; EAU35391.1; -; Genomic_DNA.
DR RefSeq; XP_001212767.1; XM_001212767.1.
DR AlphaFoldDB; Q0CRU5; -.
DR STRING; 341663.Q0CRU5; -.
DR EnsemblFungi; EAU35391; EAU35391; ATEG_03589.
DR GeneID; 4318249; -.
DR VEuPathDB; FungiDB:ATEG_03589; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_4_1; -.
DR OrthoDB; 879734at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR Gene3D; 3.40.462.20; -; 1.
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:SF27; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..388
FT /note="FAD linked oxidase N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004170568"
FT DOMAIN 24..89
FT /note="FAD linked oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01565"
SQ SEQUENCE 388 AA; 42267 MW; E71C881E05AF64EF CRC64;
MDLSAANLLY AAAAILLGPA QLAAKGVVMI DLSMMNSTVF NAQSAIASIE AGARWSSVYH
TLKQYGVAVT GGRADSVGVG GLVIGANGTL VVANSTTHSR LFRALKGGSN NFGIVTKIDM
TTFPQGDLWG GIVRHHISSI PLQISALVNF TNRLVDDPLA SVVGIWQYSS DIERLEAATG
IQYAQPVEEP PIFHETGRIG ESNTTRVADI QDLMMETAPP SGRRVLLLTL TFKNDARVVH
KILEEQGEVI ENAKAHVRGD SWNVVSFLQP FPAFFGNLST KNLGNVLGLE NMGNNHLLYL
LFVSWGSKRD DSLFHEQGHR LIERIRGFSH EIGAENDFIY LNYAGKAQNP LRSYGEHNLR
EILRVANEYD PDGVFQIQAP GGFKAHMA
//