ID A0A0D9WRD8_9ORYZ Unreviewed; 696 AA.
AC A0A0D9WRD8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glutathione transferase {ECO:0008006|Google:ProtNLM};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR06G15660.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR06G15660.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR06G15660.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR06G15660.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000256|ARBA:ARBA00003468}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000256|ARBA:ARBA00011237}.
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DR AlphaFoldDB; A0A0D9WRD8; -.
DR STRING; 77586.A0A0D9WRD8; -.
DR EnsemblPlants; LPERR06G15660.2; LPERR06G15660.2; LPERR06G15660.
DR Gramene; LPERR06G15660.2; LPERR06G15660.2; LPERR06G15660.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR HOGENOM; CLU_396079_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 6.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 2.
DR CDD; cd03044; GST_N_EF1Bgamma; 2.
DR Gene3D; 1.20.1050.10; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR044628; EF-1-gamma_plant.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
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; PTHR44372; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR PANTHER; PTHR44372:SF1; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 2.
DR Pfam; PF02798; GST_N; 2.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 2.
DR SFLD; SFLDG00358; Main_(cytGST); 2.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 2.
DR PROSITE; PS50404; GST_NTER; 2.
PE 4: Predicted;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..215
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 256..416
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT DOMAIN 475..556
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 561..696
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 213..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 78099 MW; 5E89E00A6E238F99 CRC64;
MALVLHSGSG NKNAFKALIA AEYTGVKVEL TKNFEMGVSN KTPEFLKMNP LGKIPVLETP
DGAVFESNAI ARYVARLKDN NSLCGSSLIE YAHIEQWIDF SATEVDANIG RWLYPRLGFV
PHVPVHEEHA IASLKRSLGA LNTHLASNTY LVGHSVTLAD IVMTCNLYFG FVRILTKSFT
SEFPHVERYL WTMVNQPNFK KVIGEVKQAE SVPPVQKKAA APKEPKAKEV KKEAPKEAPK
PKVEAPEEEE APKPKPKNAL DLLPPSKMIL DEWKRLYSNT KTNFREIAIK GFWDMYDPEG
YSLWFCNYKY NDENTVSFVT MNKVGGFLQR MDLCRKYAFG KMLVIGSTPP FKVKGLWLFR
GQDIPKFVMD EVYDMELYEW TKVDLSDEAQ KERVNAMIED QEPFEGEELL DAKCFNVRMS
GKCHANDLHT IGPRFSFHPL PRAAINPQLP TPANPLSDLY SAGVFAAAAD LVSRLLSVLH
SGSGNKNAFK ALIAAEYTGV KVELVKNFEM GVSNKTPEFL KMNPLGKIPV LETPDGAVFE
SNAIARYVAR LKDNNSLCGS SLIEYGHIEQ WIDFSATEVD ANIARWLYPR LGFGGPHVPV
LEEFAITSLK RSLGALNTHL AANTYLVGHS VTLADIVMTC NLYLGFVRIL TKSFTSEFPH
VERYLWTMAQ KERVNAMIED QEPFEGEELL DAKCFK
//
