ID A0A1J7FM97_LUPAN Unreviewed; 913 AA.
AC A0A1J7FM97;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=GST C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TanjilG_07646 {ECO:0000313|EMBL:OIV89022.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV89022.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV89022.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV89022.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000256|ARBA:ARBA00009899}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|ARBA:ARBA00008361}.
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DR EMBL; KV862927; OIV89022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7FM97; -.
DR STRING; 3871.A0A1J7FM97; -.
DR EnsemblPlants; OIV89022; OIV89022; TanjilG_07646.
DR Gramene; OIV89022; OIV89022; TanjilG_07646.
DR Proteomes; UP000188354; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03183; GST_C_Theta; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR040077; GST_C_Theta.
DR InterPro; IPR004159; Put_SAM_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10108:SF1072; PMT16, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR10108; SAM-DEPENDENT METHYLTRANSFERASE; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF03141; Methyltransf_29; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 645..745
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 752..909
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 52..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 103908 MW; 5B43AB6951A9ABC7 CRC64;
MAPPPKSRNN RRSSSSSSYT STLTTLLFVS ICVLAIWMLS SNSAVSPNIH NNDSITDDLP
QTTTTTTTTT SAATARSRDQ KDPDDPIKSA DRNKHHEVDN DLKTTIQDNS IQHIQSHQNP
EQSIGGEQDV PSFDTQGYKN NELEVKQNEQ KQNLVDDSVE IEKPKEEKKR RKPKKESKKP
EGDESEGEKE RQREESDGNE EMQHLEWHLC NVTAGADFIP CLDNEKYLKT SHRRHYEHRE
RHCPEDAPTC LVPLPQGYKT PVQWPNSRDK IWYHNVPHTK LAEVKGHQNW VKLTGEFLTF
PGGGTQFIHG ALHYIDFLQQ AEPGIAWGKH TRVILDVGCG VGSFGGFLFE RDVIAMSFAP
KDEHEAQVQF ALERGIPAIS AVMGTQRLQF PSSVFDLVHC ARCRVPWHED GGLLLLELNR
VLRPGGFFVW SATPVYQTLE EDVDIWKKMS ALTKAMCWEL VTIKRDKLNQ VGAAFYRKPT
TNECYEQREK NEPPMCKDDD DPNDAWYVPL QACMHRLPVD KAERGTRWPE TWPLRLQKAP
YWLNKSQKGV SGKLIPQDFA ADNERWKNVV DELSTIGISW SNVRNIMDMH AVYGGFAAAL
KDLPVWVFNV VNTDSPNTLP IIYERGLIGI YHDWCESFST YPRTYDLLHA DHLFSKLKKR
CNLVLVIAEV DRIVRPGGKL IVRDDSSALE EVENLLKSLH WEITSKNQEA INPFNKLPAI
ADGSFKLFES HAILIYIASA FPGVANHWYP ADLTRRAKIH SVLDWHHLNL RQGAAPYVLH
TVLAPVLGLP SNRQAQAEAD KILTSSLSKI ETIWLKGNGR YLLGSFQPSI ADLSMVCEIM
QLELLDEKDR NRILSPHKKV QQWIESTRNA TKPHFDEVHN VLYKMKLKLS LQRSNQVDGM
AESRIKTPLT SKM
//
