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Database: UniProt
Entry: A0A093XVM7_9PEZI
LinkDB: A0A093XVM7_9PEZI
Original site: A0A093XVM7_9PEZI 
ID   A0A093XVM7_9PEZI        Unreviewed;       434 AA.
AC   A0A093XVM7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=O988_06194 {ECO:0000313|EMBL:KFX94602.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX94602.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFX94602.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX94602.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFX94602.1}.
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DR   EMBL; JPJR01001318; KFX94602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093XVM7; -.
DR   SMR; A0A093XVM7; -.
DR   HOGENOM; CLU_018354_10_1_1; -.
DR   Proteomes; UP000029329; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   InterPro; IPR012951; BBE.
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:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029329}.
FT   DOMAIN          1..171
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   434 AA;  47182 MW;  F22CCA4D19542FB3 CRC64;
     MPLTVVLPRN TSHISAAVRC GVAAGVKVTP KAGGHSYAAL SLGGEDGHMV VEFEDMAAIS
     VDPETNIATV QPGARLGNIA TEIFKEGGRA FSHGTCPGVG IAGHALHGGY GMSSREHGLA
     LDWIDSLTVV LANGTAVDCS ASQHPDLFFA MLGAGSAFGI TTEFRFRTFA APETVTWFSA
     SLPWNRTTAV AGLEALEEFT RDTMPKELNM RLSASRGSSS LEGVYYGDRA GLDEVLGPLL
     NVTGGKVARA NTTGWIEGLE HYSEMGGRLT VPDPYDNHET FYSKSLELEG LNGTSAQNFV
     DYWFDDASDI NRIWWFQVDL QGGASSGIWA RDDGVTSYAH RDKLYIIQLY DRVFGGSYPK
     DGFEFLDGWV NTTTSPLEWG TWGMYVNYAD ARLERQDAEE LYWGKNLPRL RDIKAELDPT
     EVFFNPVSIE PSSG
//
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