ID A0A0N0NK30_9EURO Unreviewed; 348 AA.
AC A0A0N0NK30;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized oxido {ECO:0000313|EMBL:KPI37671.1};
GN ORFNames=AB675_231 {ECO:0000313|EMBL:KPI37671.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI37671.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI37671.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI37671.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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:KPI37671.1}.
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DR EMBL; LFJN01000022; KPI37671.1; -; Genomic_DNA.
DR RefSeq; XP_017997634.1; XM_018142282.1.
DR AlphaFoldDB; A0A0N0NK30; -.
DR STRING; 1664694.A0A0N0NK30; -.
DR GeneID; 28734151; -.
DR OrthoDB; 2244365at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10366:SF562; ALDEHYDE REDUCTASE II (AFU_ORTHOLOGUE AFUA_1G11360); 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 12..137
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT REGION 162..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 37585 MW; 0E56F04CF7C9F098 CRC64;
MAPLPPSPDT IILISGINGY IASHIALCLL QQGYTVRGTS RSASAKDRLI SGPFKDYAST
YQHAVVTDIA APGAFDSAVQ GVHAIIHTAS PIDFSLKTLE DFVGPAVQGN TSILTSALNH
AGPQLQSFVL TSSVAAVVDR WAHPFTEPYA YSEADWNING PKIASSEPST PASRTALRKP
SPSARCGKKA EGLNLTVKPV WDIYTNNPSL NGKLPPPVGG ASWVDVRDVA EIHAWAAINP
DESKGQRYLA TNGKAPPQAI ADLLREEFPD RDIITEQPGY WYQSRDEEDK EKRGGLFGKK
WGWELEGQSV DAAKMRKALG GGREKELRGY REAVLDTVRA LEGHFGSL
//
