ID G2QW53_THETT Unreviewed; 264 AA. AC G2QW53; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 51. DE RecName: Full=Glutathione S-transferase {ECO:0008006|Google:ProtNLM}; GN ORFNames=THITE_2083750 {ECO:0000313|EMBL:AEO62224.1}; OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia OS terrestris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides; OC Thermothielavioides terrestris. OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO62224.1, ECO:0000313|Proteomes:UP000008181}; RN [1] {ECO:0000313|EMBL:AEO62224.1, ECO:0000313|Proteomes:UP000008181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181}; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P., RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., RA Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi RT Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|ARBA:ARBA00007409}. 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; CP003009; AEO62224.1; -; Genomic_DNA. DR RefSeq; XP_003648560.1; XM_003648512.1. DR AlphaFoldDB; G2QW53; -. DR STRING; 578455.G2QW53; -. DR GeneID; 11521347; -. DR KEGG; ttt:THITE_2083750; -. DR eggNOG; ENOG502S090; Eukaryota. DR HOGENOM; CLU_039475_0_0_1; -. DR OrthoDB; 313646at2759; -. DR Proteomes; UP000008181; Chromosome 1. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR CDD; cd03192; GST_C_Sigma_like; 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; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF161; GLUTATHIONE S-TRANSFERASE; 1. DR Pfam; PF14497; GST_C_3; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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:UP000008181}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 17..105 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 110..251 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 264 AA; 29611 MW; 505A7CE73C053AB8 CRC64; MASEVPPKRQ KSAKDVPYHL IYWPGIPGRG EHVRLALEEA GAEYTDTAFT DGGVDEVLAY VQGKIPDDGL NPPPCAPPIL KHGDLVISQT PNILLYLGNR LGLVPDADQD PDAMYKINAL ALTALDGLSN EPHDCHHPIA SGLYYEDQKE EAKRRSEDYV KNRLPKFLSY FERVLESKAS GDGPWLYGGA LTYADLVLFQ CVDGVKFMFP KAMAKLERGG KHAKVFQLYQ AVAERPKIKA YLQSDRRQKY SNGIYRYYEE LDFA //