ID S9X5T6_SCHCR Unreviewed; 180 AA.
AC S9X5T6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Glutathione S-transferase Gst2 {ECO:0000313|EMBL:EPY49156.1};
GN ORFNames=SPOG_04996 {ECO:0000313|EMBL:EPY49156.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49156.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY49156.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
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DR EMBL; KE547000; EPY49156.1; -; Genomic_DNA.
DR RefSeq; XP_013026026.1; XM_013170572.1.
DR AlphaFoldDB; S9X5T6; -.
DR STRING; 653667.S9X5T6; -.
DR EnsemblFungi; EPY49156; EPY49156; SPOG_04996.
DR GeneID; 25039307; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_2_1; -.
DR OMA; FPHFTRW; -.
DR OrthoDB; 1404190at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.130; -; 2.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF3; TRANSCRIPTIONAL REGULATOR URE2; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Transferase {ECO:0000313|EMBL:EPY49156.1}.
FT DOMAIN 1..66
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 47..180
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 180 AA; 20935 MW; B627926C978FD3BA CRC64;
MTQLTLFSCR GILYDVGKNE QKSEEHLDYN PNGRVPTLID HQNNGYAIWE SAAILAYLTD
KQGAIWGQAG WLNFFHPEPV ASAVTRYRNE TKRVLGVLER ILQNKDYLVT DKYTIADMSF
INWNDLLPPL FGKGRHEFKE DLPQLDFEKE FSKTYAWHQS LTERPAVAAI LKEWEQSRQQ
//