ID   A0A0F8VDA5_9EURO        Unreviewed;       483 AA.
AC   A0A0F8VDA5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=ARAM_004309 {ECO:0000313|EMBL:KKK21076.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK21076.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK21076.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK21076.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK21076.1}.
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DR   EMBL; JZBS01001863; KKK21076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8VDA5; -.
DR   STRING; 308745.A0A0F8VDA5; -.
DR   OrthoDB; 879734at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
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.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          62..238
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   483 AA;  52823 MW;  D8E8699E48F5E25E CRC64;
     MKVCANSIVS VLDTVLKTCP ANGSVSACCV ALKSTSLSDR VFYPTSDVYH QSIGSYWRAD
     NQQLYPSCVV QPHSAQDVSL AVSTLVKAND NSPRCQFAVR SGGHGTVTGS TNGDYAVTID
     LSQMNQTVYH ADTCTASIQA GARWKSVYKT LSQHNMAVPG GRSGMVGVGG FVTGGGNSFH
     SAQYGLVCDA VVNFEIVLAN GQITTANEHT NPDLFKVLRG GSNNFGIVTR IDLEAFEQES
     LWGGVVTYNQ STAAQQIPAF VDFTSDLHKD PHASLIALYT YSSELGVPVI SNALEYTKPV
     EFPAAFARFY ALPNISSTMR IADLDDVTSE FEPPGGVHHN FFTLTFANDP RILHRAVEIQ
     TKAIEEIKHS VKSSAWSIMS LYQPFPALFT HLVDLLWFTW DEIEDTPLFD SVGYAMVEEI
     ESYARSRGGG NRYIYLNYAA GLQNPLRGYG EDNLREMRRV AEKYDPLGVF QYQVPGGFKL
     SQA
//