ID G0UPZ7_TRYCI Unreviewed; 313 AA.
AC G0UPZ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative glutathione-S-transferase/glutaredoxin {ECO:0000313|EMBL:CCC91458.1};
GN ORFNames=TCIL3000_7_2720 {ECO:0000313|EMBL:CCC91458.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC91458.1};
RN [1] {ECO:0000313|EMBL:CCC91458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC91458.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; HE575320; CCC91458.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UPZ7; -.
DR VEuPathDB; TriTrypDB:TcIL3000_7_2720; -.
DR OrthoDB; 1226at2759; -.
DR UniPathway; UPA00662; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1.
DR PANTHER; PTHR12782:SF9; PROSTAGLANDIN E SYNTHASE 2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:CCC91458.1}.
FT DOMAIN 70..119
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 313 AA; 35601 MW; 77A7987433A51C0A CRC64;
MFSKGSTSRK ILCTTGAVVA VGFGGAYAAY HRRLKENSSC TAEEFNAAQN QEDLRLALTH
IADPKKCPPV LLYRYSTCPF CSTTKSFLDY NKVPHTCVEV EPMFKREISM NAYKKVPQLK
FCVKGDEGPF LVDSEIIVST IAKSVGMGRQ LDDPEVKRWR VWARGPLVRL LTLEFNSSLF
KAWRAYSYID DIETIPYRNK LFLKVVGAPV MYLVAHYVTK PRLIKSGHLL PTEDVKVRLH
GEVNRFVVEA LQDGKRKFHG GAKPDLADLD THGVLQSVRG HRIYEEIIKE TAIKQWLDHM
DEVMGREKYV SQQ
//
