ID A0A317X8S7_9EURO Unreviewed; 609 AA.
AC A0A317X8S7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Short-chain dehydrogenase/reductase {ECO:0000313|EMBL:PWY94685.1};
GN ORFNames=BO94DRAFT_563252 {ECO:0000313|EMBL:PWY94685.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY94685.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY94685.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY94685.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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:PWY94685.1}.
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DR EMBL; MSFK01000004; PWY94685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317X8S7; -.
DR STRING; 1450535.A0A317X8S7; -.
DR OrthoDB; 3088985at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10293; GST_C_Ure2p; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR24320:SF272; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR00081; GDHRDH.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 395..535
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 609 AA; 67348 MW; 858A68FD6B3795A4 CRC64;
MSCYTAAHAN PQGPGDSRPT ALQIIQDNNM EGKLVGKVAI VTGVSSGIGV ETVRALAATG
ATLYLTARNP DKARAALGDI FQPETMELVQ MDQTSLSSVR QAAAAILAKT DQVNILIANA
GVMAVRDLQL TEDGYELQFA TNHLAHFLFF QLLKPALLAG SSPTFQSRVV MVASSGHRVH
GINESDNYHF QKGAYEPWVA YGQSKTANIY MASEIERRYG SRGLHATSLH PGVIATSLGR
HMTEEQIHDL VHDETVAKVL KSPAQGAATT IWGAVGSEWE GKGGKFLADC AEAVQAEYDG
HIGRTFVSYT YSPEEEDRLW RDSLEMVVII LEELSIPYTI RSFKFDDVKK PPFIDINPNG
RVPDPNTNLT LWESGAIIQY LIDIYDTTHK ISYETLNEKH LLNQYLQFQM SGQGPYYGQC
GWFNVLSPEK LPSAITRYQN EVHRVLGVLN TILTNKTWLV GDKCTYADLA FLPWNNRLDM
LIPRDEGGEI LEAYPWVQGW QKRMEERESW KRSMEVRAGL MDEQGLMVNG MPKGVNNIRE
YEELIAKSEG GKLEGKGEGV DEQEGVLGCV GIGKNVKMGK VIVDEKKEDE DERSDEDAGV
LGCVAIGRV
//
