ID A0A1I8I051_9PLAT Unreviewed; 658 AA.
AC A0A1I8I051;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0009092-snap-gene-0.4-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0009092-snap-gene-0.4-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|ARBA:ARBA00003701}.
CC -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC detoxification system. Other functions are also suspected including a
CC role in increasing the solubility of haematin in the parasite gut.
CC {ECO:0000256|ARBA:ARBA00002446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC {ECO:0000256|ARBA:ARBA00005861}.
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DR AlphaFoldDB; A0A1I8I051; -.
DR WBParaSite; maker-uti_cns_0009092-snap-gene-0.4-mRNA-1; maker-uti_cns_0009092-snap-gene-0.4-mRNA-1; maker-uti_cns_0009092-snap-gene-0.4.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IEA:InterPro.
DR GO; GO:0030431; P:sleep; IEA:InterPro.
DR CDD; cd14978; 7tmA_FMRFamide_R-like; 1.
DR CDD; cd03192; GST_C_Sigma_like; 1.
DR CDD; cd03039; GST_N_Sigma_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR031424; QVR.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF17064; QVR; 1.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 385..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..233
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 235..357
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 401..658
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 658 AA; 74016 MW; 92348A359D0D7CBF CRC64;
MSSCSTLCKS RASLERLFKQ YSLPNHSSAI MCYQCDSQED SSCPDSRYFD QRTNALIDCT
SFQARVPGTF CVKIYQESTG WHSWIKVTRR CGSRPERIAW GCNYRFVDMG VYRETCYCSD
KDGCNSSKSL AASASTLCLT GLLLLSRLNM STAKPKLYYF GVRGRGELIR LVFAAGKIDF
EDIRLTKEQW AEQKKNSPTG VMPFVDTGDK SKGLLAQSGA IARYYAKKAG LMGSNDWEYY
LVERAMCQLD DIFMELVKFM MAPEDKKPDL LKEFQAEKGP KLLSGLVDFL KQAGGQYFAG
KSLSLADLGC LNILDSLANM PDLLAKYPEL TELKKRVLAG NAKLAEYIKK SAGDSDAMSS
LTALCPNETA EDLAERSSIL NISRMFLVCI TPGLALLGIA ANSVNIVVLT RKWMASSTNY
YLTALAITDV IYLLLFYLIT VKVYPGVRYQ AWFFHLLAAM FPLANLFSNF ATWLTCFFTF
ERWVVVYKPM FGRKYCTKER AKHTIAVIFL ATLFFTFPNF LEYQVDSQNK GNSTSAPAVY
TLGKTQAYLV MKQYGYYHLL PIVFIFGPLV FLAVFNSLLI GSVVRAKKKQ EELSAALIPR
RPSSTPRPSQ QYAQIPMLTV ATPRASVCSS VGLTAGSSGK QRRRQRRRRW ARIRRRFG
//
