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Database: UniProt
Entry: A0SZK4_TRYCR
LinkDB: A0SZK4_TRYCR
Original site: A0SZK4_TRYCR 
ID   A0SZK4_TRYCR            Unreviewed;       445 AA.
AC   A0SZK4;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Thiol transferase Tc52 {ECO:0000313|EMBL:ABK58598.1};
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693 {ECO:0000313|EMBL:ABK58598.1};
RN   [1] {ECO:0000313|EMBL:ABK58598.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tep23 cl4 {ECO:0000313|EMBL:ABK58598.1};
RX   PubMed=17659387; DOI=10.1007/s00436-007-0651-3;
RA   Mathieu-Daude F., Bosseno M.F., Garzon E., Lelievre J., Sereno D.,
RA   Ouaissi A., Breniere S.F.;
RT   "Sequence diversity and differential expression of Tc52 immuno-regulatory
RT   protein in Trypanosoma cruzi: potential implications in the biological
RT   variability of strains.";
RL   Parasitol. Res. 101:1355-1363(2007).
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DR   EMBL; EF065176; ABK58598.1; -; mRNA.
DR   VEuPathDB; TriTrypDB:BCY84_11003; -.
DR   VEuPathDB; TriTrypDB:C3747_167g15; -.
DR   VEuPathDB; TriTrypDB:C4B63_113g42; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_3573; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0015080; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM13180; -.
DR   VEuPathDB; TriTrypDB:TcCLB.503419.30; -.
DR   VEuPathDB; TriTrypDB:TcCLB.509105.70; -.
DR   VEuPathDB; TriTrypDB:TCDM_06784; -.
DR   VEuPathDB; TriTrypDB:TcG_07430; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_004831; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00299; GST_C_family; 2.
DR   CDD; cd00570; GST_N_family; 1.
DR   Gene3D; 1.20.1050.10; -; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
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; IPR041695; GST_C_5.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF6; GLUTATHIONE S-TRANSFERASE OMEGA; 1.
DR   Pfam; PF16865; GST_C_5; 2.
DR   Pfam; PF13409; GST_N_2; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 2.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 2.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50405; GST_CTER; 2.
DR   PROSITE; PS50404; GST_NTER; 2.
PE   2: Evidence at transcript level;
KW   Transferase {ECO:0000313|EMBL:ABK58598.1}.
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..218
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          226..305
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          286..440
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   445 AA;  50718 MW;  A65BC104939E12D7 CRC64;
     MKALKLFKDR MCPYCQRVLI TAKEKRVKLE EVEVPLGDDM PQWYKELNPR ETVPTLQVDG
     KKCMIESDLI SRYIDRISSP ANALIGSSPY QRHRVEFFLS EIGDLIKAYF GLLRDPFNEE
     KRKSVDHNTA YIEGIIAEHQ GDGPYFLDDT FSMAEVMVVP FLACFRPVLS YYCGYDIFHE
     APRLKKMYVT SMQRTTVKET VLKPEEYIIG FKRKVPTSHV TWSLAPGYVL FVNKYSPFSD
     RPRLACALKN IDLPMLEIDL KQLPSWFRWF NQRETVPALL TPQGTHVHES QLIVHYLDDG
     FPEHGPALLP KDADGLYHVS FVESNVDYFM DAMFSXIKDP KNRNAKEEFD WAAGELEKLL
     AEHQFGEGPF FGGASMNAAD VSLVPMLVHL KACTPDLTEG QDLLANYKLL TAAAEAGLTS
     EAGKKVFFSL SEYSSIYKTF LRPSS
//
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