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Database: UniProt
Entry: A0A3B4WJI5_SERLL
LinkDB: A0A3B4WJI5_SERLL
Original site: A0A3B4WJI5_SERLL 
ID   A0A3B4WJI5_SERLL        Unreviewed;       246 AA.
AC   A0A3B4WJI5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000001673.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000001673.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000256|ARBA:ARBA00011055}.
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DR   AlphaFoldDB; A0A3B4WJI5; -.
DR   STRING; 1841481.ENSSLDP00000001673; -.
DR   Ensembl; ENSSLDT00000001757.1; ENSSLDP00000001673.1; ENSSLDG00000001369.1.
DR   GeneTree; ENSGT00940000161750; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03208; GST_C_Alpha; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF230; GLUTATHIONE TRANSFERASE; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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          26..106
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          108..228
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   246 AA;  28215 MW;  04B9762AD02C31F1 CRC64;
     MFLQRTFTAP QSFTDIHSQN KIAMAEKVVL HYFNGRGKME TIRWLLTVAE VDFDEVHLTT
     REQYEKLLSD GSLMFQQVPM VEIDGMRLVQ TKAILNYIAE KYNLHGQNLK DRVLINMYSE
     GLIDLMEMIM ILPFSSDVEA KLKNIQTKAK ERYLPVFEKA LSGPIYLVGG KLSCADVELL
     ECTLMLEEKF PGILADFPNV KSFQGRMTQI PAISRFLQPG SKRKPQPDET YVKTVMEVFN
     VKLPLP
//
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