ID   M0MZS7_9EURY            Unreviewed;       336 AA.
AC   M0MZS7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Glutathione transferase {ECO:0000313|EMBL:EMA49925.1};
GN   ORFNames=C450_16670 {ECO:0000313|EMBL:EMA49925.1};
OS   Halococcus salifodinae DSM 8989.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227456 {ECO:0000313|EMBL:EMA49925.1, ECO:0000313|Proteomes:UP000011625};
RN   [1] {ECO:0000313|EMBL:EMA49925.1, ECO:0000313|Proteomes:UP000011625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8989 {ECO:0000313|EMBL:EMA49925.1,
RC   ECO:0000313|Proteomes:UP000011625};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA49925.1}.
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DR   EMBL; AOME01000076; EMA49925.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0MZS7; -.
DR   STRING; 1227456.C450_16670; -.
DR   PATRIC; fig|1227456.3.peg.3391; -.
DR   Proteomes; UP000011625; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   CDD; cd03190; GST_C_Omega_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; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR32419:SF6; GLUTATHIONE S-TRANSFERASE OMEGA-LIKE 1-RELATED; 1.
DR   PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:EMA49925.1}.
FT   DOMAIN          164..294
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          314..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        59
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        190
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   336 AA;  38142 MW;  9E70793653CC71CE CRC64;
     MAVNQLIDGE WVTDAYESTN DDGEFDRQET SFRDWIEPDP DAEFPAEAGR YHLYVSLACP
     WAHRTLVTRA LRGLEDVISV DIVDPYRAED GWQFTPEREG ATPDMVNGFD YLREAYVAAD
     PEVTGRVTVP VLWDTEQDTI VNNESAEIMR MLDTAFGEFA NDATLYPDGH RDEIDETIDA
     VYEPINNGVY RAGFAGTQDA YENAVAELFD ALDHWEDVLA DQRYLCGDVL TEADICLFTT
     LIRFDDVYHT HFKCNVRKIA EYPNLWNYLK ELYQLPGVAA TVNMDHITEH YYETHTDLNP
     KRIVAVGPNH DFGAEHDRER LAGGPPQSVT ARAADD
//