ID Q0CJM2_ASPTN Unreviewed; 403 AA.
AC Q0CJM2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=ATEG_06112 {ECO:0000313|EMBL:EAU33873.1};
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:EAU33873.1, 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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; CH476601; EAU33873.1; -; Genomic_DNA.
DR RefSeq; XP_001215290.1; XM_001215290.1.
DR AlphaFoldDB; Q0CJM2; -.
DR STRING; 341663.Q0CJM2; -.
DR EnsemblFungi; EAU33873; EAU33873; ATEG_06112.
DR GeneID; 4321393; -.
DR VEuPathDB; FungiDB:ATEG_06112; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_12_1_1; -.
DR OMA; GHIHRTH; -.
DR OrthoDB; 2332834at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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; PTHR47356:SF2; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..329
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 341..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 45864 MW; 1691BFBDE866FF8D CRC64;
MKPTDSDHLC ADRPRSRKDF RVIIVGGSIA GLTLAHSLRK YNIDYRVLEA YHDIAPQVGA
SIGLAPSGCG ILDQLGIFDA VLKEIEPLRL SQYWTATGRK IAENKAPTLL QERNGYPLSF
LDRHKVLAIL YDHLAEDQSK VFLNKRVVRV EDVPGGVVVH CKDGSQWTGD IAVGADGVHS
TIRNEIWNRL DKQQLGHDMI REKKEMISEY SCIFGISADM KELEPGHIHR THGKGFTTVI
MVGKNHRTFW FLFAKMDRKY TMRDLPRFTV EDRERHVAQY FDVRISSEVT FEDLYKRGVY
KTYVPLEEAF FEYWVVDRLV CIGDSVHKVR NGPNYDDRCL LTSEDDSKHG PGRELRNRER
SEPSKLPEAI HRYARSVLPY GGSARSFICV VEGTTAPSTE ALP
//
