ID H0GI50_SACCK Unreviewed; 234 AA.
AC H0GI50;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Gtt1p {ECO:0000313|EMBL:EHN06530.1};
GN ORFNames=VIN7_2484 {ECO:0000313|EMBL:EHN06530.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN06530.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN06530.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN06530.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
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:EHN06530.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGVY01000032; EHN06530.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GI50; -.
DR HOGENOM; CLU_011226_15_1_1; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR CDD; cd03189; GST_C_GTT1_like; 1.
DR CDD; cd03046; GST_N_GTT1_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051:SF9; GLUTATHIONE S-TRANSFERASE 1; 1.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
FT DOMAIN 3..90
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 96..234
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT UNSURE 149
FT /note="E or Q"
FT /evidence="ECO:0000313|EMBL:EHN06530.1"
SQ SEQUENCE 234 AA; 26796 MW; 9D53C15929ECCDE5 CRC64;
MSLPIIKVHW LDHSRAFRLL WLLDHLNLEY EIVPYKRDAN FRAPPELKKI HPLGRSPLLE
VQDRETGKKK ILAESGFIFQ YVLQHFDHSH VLMSEDADIA DQINYYLFYV EGSLQPPLMI
EFILSKVKDS GMPFPISYLA RKVADKISEA YSSGEVKNQF DFVEGEISKN NGYLVDGKLS
GADILMSFPL QMAFERKFAA PEDYPAISKW LKTITSEESY AASKEKARAL GSNF
//