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Database: UniProt
Entry: A0A1Y2FBX9_PROLT
LinkDB: A0A1Y2FBX9_PROLT
Original site: A0A1Y2FBX9_PROLT 
ID   A0A1Y2FBX9_PROLT        Unreviewed;       282 AA.
AC   A0A1Y2FBX9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORY81422.1};
GN   ORFNames=BCR37DRAFT_402850 {ECO:0000313|EMBL:ORY81422.1};
OS   Protomyces lactucae-debilis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Protomycetaceae; Protomyces.
OX   NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY81422.1, ECO:0000313|Proteomes:UP000193685};
RN   [1] {ECO:0000313|EMBL:ORY81422.1, ECO:0000313|Proteomes:UP000193685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-1054 {ECO:0000313|EMBL:ORY81422.1,
RC   ECO:0000313|Proteomes:UP000193685};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY81422.1}.
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DR   EMBL; MCFI01000011; ORY81422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2FBX9; -.
DR   STRING; 56484.A0A1Y2FBX9; -.
DR   OMA; EFHSCDV; -.
DR   OrthoDB; 5473331at2759; -.
DR   Proteomes; UP000193685; 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; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43008; BENZIL REDUCTASE; 1.
DR   PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
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:UP000193685}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  30144 MW;  A3C38CFA4F8C82CD CRC64;
     MALSDANMAS SAVDPTRPTR PEIPAAFKKF SLEGKVAVIT GGARGLGFSM AQAISSCNLA
     GIAILDVLQE AGDEAAAALH AEFGIPSAFY KIDVRDEKAV SETIQGIKHD FGRVDILICS
     AGICDNIKAE NYEADRFRRV MDINVTGSFL CAQACAREMI EQKQGGSIIF IASMSGHIVN
     YPQPQSAYNA SKAAVLMLAK SLAAEWSPYA IRVNTISPGY MATKLTDTEA FRELKTTWAA
     RTPLGRLGQD YELNGIAQFL ASDASSFSTG ADYLIDGGYT IM
//
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