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Database: UniProt
Entry: A1DLC6_NEOFI
LinkDB: A1DLC6_NEOFI
Original site: A1DLC6_NEOFI 
ID   A1DLC6_NEOFI            Unreviewed;       662 AA.
AC   A1DLC6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EAW15597.1};
GN   ORFNames=NFIA_049370 {ECO:0000313|EMBL:EAW15597.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW15597.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
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 PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007801}.
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DR   EMBL; DS027698; EAW15597.1; -; Genomic_DNA.
DR   RefSeq; XP_001257494.1; XM_001257493.1.
DR   AlphaFoldDB; A1DLC6; -.
DR   EnsemblFungi; EAW15597; EAW15597; NFIA_049370.
DR   GeneID; 4584008; -.
DR   KEGG; nfi:NFIA_049370; -.
DR   VEuPathDB; FungiDB:NFIA_049370; -.
DR   eggNOG; KOG3855; Eukaryota.
DR   HOGENOM; CLU_009665_9_2_1; -.
DR   OMA; WEVAFWN; -.
DR   OrthoDB; 1386239at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02979; PHOX_C; 1.
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; IPR012941; Phe_hydrox_C_dim_dom.
DR   InterPro; IPR038220; PHOX_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43004:SF15; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G03030)-RELATED; 1.
DR   PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF07976; Phe_hydrox_dim; 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:UP000006702}.
FT   DOMAIN          40..436
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          473..628
FT                   /note="Phenol hydroxylase C-terminal dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07976"
FT   REGION          284..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  73478 MW;  F1445259BE8D3257 CRC64;
     MPVFTEYAAS SRELRVLPSF APPLPRLSPR FTRPEGAEKY EVVIVGAGPA GLMLHLLLAR
     YGLNDDSLLC IDAKPGTLKS GQADGLQPRT LEVLKSLGLA DEILTDGCHM EEVAFWNPSP
     DKEKVIERTS IVPDVAVPAR FQHEVTIHQG RIERILETDL LRYSKRGVQR NTKLVDVKID
     EAGDAEFPVV AEIETDGTRR TIRSKHLVGA DGAHSVVRRC MGLKLVGESM DHIWGVVDLV
     IDTDFPDIRR RCAIHSPAGS VMVIPRERIA TGDYLTRLYV QVPEETPPEE DQKPVNGTTS
     QSKGDARARR SQVNQESIFR HAAQAFKPYY IRPKEEGAVD WWAAYQIGQR VTDNFTVKDS
     KGINRVFIVG DACHTHSPKA GQGMNVSMMD SYNLAWKLAY SLHGLTPSSA VPGQPDAIVD
     TYHSERHTIA QELIAFDRAF SSMFSGKIGA SEDGVEGLTH EQFLEVFSTG NGFTSGCGIE
     YPSSLMVDKA SDDGAENPVN GTDYLSGVLR PGRRLLDVRC KRHADGNRRH LHDDFLSTGR
     FRILCLTSSD LLDPKGVSAQ VLTSLGASVL PRFPPNIIEQ VVIHPRLGKT FMWQDVPNEL
     KKHSEMRFYS GYALDDVYKI YGVDETRGAL AVVRPDGYVG MVAELEDLKR VQEYLERCVR
     TI
//
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