EF1G_TRYCR
ID EF1G_TRYCR Reviewed; 411 AA.
AC P34715;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Y;
RX PubMed=8367313; DOI=10.1093/nar/21.16.3901;
RA Billaut-Mulot O., Pommier V., Schoeneck R., Plumas-Marty B., Taibi A.,
RA Loyens M., Capron A., Ouaissi M.A.;
RT "Nucleotide sequence of a Trypanosoma cruzi cDNA encoding a protein
RT homologous to mammalian EF1 gamma.";
RL Nucleic Acids Res. 21:3901-3901(1993).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma.
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DR EMBL; L17307; AAA02936.1; -; mRNA.
DR PIR; S41648; S41648.
DR AlphaFoldDB; P34715; -.
DR SMR; P34715; -.
DR PRIDE; P34715; -.
DR VEuPathDB; TriTrypDB:BCY84_19291; -.
DR VEuPathDB; TriTrypDB:C3747_8g439; -.
DR VEuPathDB; TriTrypDB:C4B63_138g2; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_5290; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0053310; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM09704; -.
DR VEuPathDB; TriTrypDB:TcCLB.508221.670; -.
DR VEuPathDB; TriTrypDB:TcCLB.508261.140; -.
DR VEuPathDB; TriTrypDB:TcCLB.508761.229; -.
DR VEuPathDB; TriTrypDB:TcCLB.510037.5; -.
DR VEuPathDB; TriTrypDB:TcCLB.510163.20; -.
DR VEuPathDB; TriTrypDB:TcCLB.510463.160; -.
DR VEuPathDB; TriTrypDB:TCDM_05825; -.
DR VEuPathDB; TriTrypDB:TCDM_13097; -.
DR VEuPathDB; TriTrypDB:TcG_09233; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_006565; -.
DR VEuPathDB; TriTrypDB:TcYC6_0037310; -.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR Gene3D; 3.30.70.1010; -; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
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 Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF89942; SSF89942; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Elongation factor; Protein biosynthesis.
FT CHAIN 1..411
FT /note="Elongation factor 1-gamma"
FT /id="PRO_0000208825"
FT DOMAIN 3..84
FT /note="GST N-terminal"
FT DOMAIN 90..216
FT /note="GST C-terminal"
FT DOMAIN 255..411
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 212..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46567 MW; F61463694B73CD80 CRC64;
MSLTLWSGVN PENARTHKLL AAAALANVAV TLKACEYGRE NETAEYCRNC SPCGRYPVLQ
TEEGCVFESN AILRHIARLD RSGGFLYGRT PLEGSQVDMW LDFSATELDA ASEPFVHHAF
RGEPLPANAM DRVHEVLRAL EAWLETRTFL VGERMTVADV AVAFALQWHY RLNGAEGEAL
TKKYRNAYRM YNTVMQQPKT VEVLRSQGAT FGAREGGAKG QGRGCARPGR EEAERAAAAA
DGAEEEDEAP REKKKPNPLD ELPPSPFVLD AFKREYSNTD TRTVAAPYFF QHYDAAGYTT
FWCRYKYNED NKMQFMTANL IRGWFQRMEH VRKYAFGVAL IIGEERRHDI VALWVFRGRG
MPAIVEDVED TELFDWEEVA DVAAQRERIT DYLSWEGPTI PRPVLEGRVF K
