ID B3S5H7_TRIAD Unreviewed; 231 AA.
AC B3S5H7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Glutathione transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_59619 {ECO:0000313|EMBL:EDV22042.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22042.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV22042.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22042.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU003494}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS985251; EDV22042.1; -; Genomic_DNA.
DR RefSeq; XP_002115679.1; XM_002115643.1.
DR AlphaFoldDB; B3S5H7; -.
DR STRING; 10228.B3S5H7; -.
DR EnsemblMetazoa; TriadT59619; TriadP59619; TriadG59619.
DR GeneID; 6756890; -.
DR KEGG; tad:TRIADDRAFT_59619; -.
DR CTD; 6756890; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_2_0_1; -.
DR InParanoid; B3S5H7; -.
DR OMA; YHDEMLA; -.
DR OrthoDB; 1199296at2759; -.
DR PhylomeDB; B3S5H7; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; PTHR43917; -; 1.
DR PANTHER; PTHR43917:SF8; GH16740P-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 89..229
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 231 AA; 26490 MW; 2E797142407E3723 CRC64;
MAKLNFYFDP LSEPCRSVQL FLEANKIPYE TKHTDLITAA TRTEEYRKIS PTQTVPAIVH
GEFKLFESVA ILQYLAGAFS TPDHWYPSEA KKRARINEYL HWHHLNSRWK GGLLVVMKYI
YLPHFYKQEV SEEDKKGSII ALKQTLDTFE NYFLKDNRFI AGDEISIADL MAVGELIAPD
IIGVYVGKGR PRVQAWHQNI KAALGAVYDS VHAAMYKHMD DIKGLVPPID Y
//
