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Database: UniProt
Entry: A0A0F0I456_ASPPU
LinkDB: A0A0F0I456_ASPPU
Original site: A0A0F0I456_ASPPU 
ID   A0A0F0I456_ASPPU        Unreviewed;       559 AA.
AC   A0A0F0I456;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Alcohol dehydrogenase GroES-like domain protein {ECO:0000313|EMBL:KJK61946.1};
GN   ORFNames=P875_00086532 {ECO:0000313|EMBL:KJK61946.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61946.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61946.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK61946.1}.
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DR   EMBL; JZEE01000654; KJK61946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I456; -.
DR   STRING; 1403190.A0A0F0I456; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08243; quinone_oxidoreductase_like_1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          216..526
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62068 MW;  8D32341AB2D53EA5 CRC64;
     MASSAENSPF PGPESSNEPT PQLNIPPDIL RLRAEIFALE APITVSVTEF NNAWKYLDNI
     YVRNQARYGQ KKTTTYYWCR LWRTKAYEPS VSDEQRKRKR TVREPIGCPC RIRIVSDGYY
     MTITRGKEPH NHDISALDYK LTTAARELAA QAVAKGSRPS LVARELKNSG IGGQITSKDA
     WNAGNVWVSR KEGRPAWQKH YPKNSVMEAI VANEPGPPDV LHVETYPRPP PKSGEILIEV
     KAFGLSRSDI LARQGHTADA KFPQIMGREA VGIVTAGEGT VTPGTRVIAM ITDLLPEYPG
     SYAQYTRVPA THVRRVHPLC KLSWEHLAVF SEMIPTAWNA LFRALRLHPD DRLLIRGGTT
     SIGLAAACIA KRHCSFIAST TRQESRKELL EGVGVHKILI DDGSVSQQIK SEGLEFTKVL
     DLIGAKTIAD SLQCVRPYGI VCQAGAIGGD STISDFNPMD AVPSTVSFTT YKSSAEDFIN
     FPLDVLCHEV ETGHLKLPNI RIYFSNQIVQ AHRSIEENRA EGKVVVLWKP YNLLNYGAVL
     PFEEFELLAS RPQILISPV
//
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