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Database: UniProt
Entry: A0A182M593_9DIPT
LinkDB: A0A182M593_9DIPT
Original site: A0A182M593_9DIPT 
ID   A0A182M593_9DIPT        Unreviewed;       214 AA.
AC   A0A182M593;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE   AltName: Full=GST class-theta {ECO:0000256|ARBA:ARBA00041523};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA009797-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA009797-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA009797-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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. Theta family.
CC       {ECO:0000256|ARBA:ARBA00009899}.
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DR   EMBL; AXCM01001801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182M593; -.
DR   STRING; 139723.A0A182M593; -.
DR   EnsemblMetazoa; ACUA009797-RA; ACUA009797-PA; ACUA009797.
DR   VEuPathDB; VectorBase:ACUA009797; -.
DR   OrthoDB; 2318861at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   CDD; cd03177; GST_C_Delta_Epsilon; 1.
DR   CDD; cd03045; GST_N_Delta_Epsilon; 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; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR43969:SF9; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-like; 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;
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          86..212
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   214 AA;  24466 MW;  90C674E228C79BBC CRC64;
     MDFYHLPLSA PCQSVRLVAK ALGLHLNLKE LDLLNGEHLK PEFLKINPQH TIPTLVDNDF
     VLWESRAILT YLCEKYGKND GLYPKDPKKR ALVNQRLFFD MGTLYQRFSQ AFYPVMMEGK
     ELNADNVVKL DEALEFLEIF LDKTAFAAGD KLTVADMTLL ATITTIDVTA GHDLSKYQNI
     QRWYAQLKES VAGYEEICVE GAKKFREAFN PINK
//
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