ID A0A423W927_9PEZI Unreviewed; 768 AA.
AC A0A423W927;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VSDG_02939 {ECO:0000313|EMBL:ROV99807.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV99807.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV99807.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV99807.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:ROV99807.1}.
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DR EMBL; LJZO01000010; ROV99807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423W927; -.
DR STRING; 252740.A0A423W927; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05374; 17beta-HSD-like_SDR_c; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44169; NADPH-DEPENDENT 1-ACYLDIHYDROXYACETONE PHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR44169:SF6; NADPH-DEPENDENT 1-ACYLDIHYDROXYACETONE PHOSPHATE REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
SQ SEQUENCE 768 AA; 84052 MW; 47C8B6DB212D3C5B CRC64;
MSVKPNQKTV LITGCTPGGI GFELCKEFHD RGLHVIATAR NPSVLSDLAG KPGFTYLPLD
VTKQSSIDAC RDEVVKLTGG KLDILVNNAG RTHTVPATDL DIDDVRATFE ANVFGVMAMV
QAFVHLLIPT KGLIINVSSV ASIAPYAFAS AYCASKGAVN SYSRTLRQEL RPYGVRVMVA
LPGTVKTNIN LQTDRKLPEG SLYTPIADVY KWRLMFSKDA SSSITPQRYA KQLVTDALKP
EWPLFLRGLF SMVGFCRPDW HYYGGLAKEA CLAKDVYRPF PYLPDNLPPP EEVNAPSLVA
KSLRSLTDAL GAEDVRKVKS CFLTVQSYWR DLLSFTYHFR TLNDAGVIAP AMVLLTKNRG
LLGGFELIPG SVQDVVVSPT LRWVEAMITF KTLMPKAKCE GRVMLFPEVD DSSEVVWKIW
SLSTWLEAFE EYPEDQHKLK AAGRDVKSPE HIETDVFIVG GGNAALTFSW HSAYPKDNPQ
ILTRQMLADH MENYAATFNI SILNSSTVES CSFNQPRGKW NSVIIVGSAN SAFDVMEDCA
TGGLRTTMIA RSPTYIFPWD YALAPQGLGV YEVTPADLAD KLQMSGPNAI GGQLAMALHT
HLAHQEKDRY KALAETGFPV YDSTEPGKGD LMHHLLERGG GHFNDIGDGV KMLVDGICAV
KGNVEPVEYA PTGLKLSDGS TVDADAIVWC TGFADKDPSV TAEILGGKTF HDEEASNDVL
GPRDIAILRD AIWGVDKEGE VRGFLALQIK AEIEGILPEA YRDSPETV
//
