EF1A1_TRYB2
ID EF1A1_TRYB2 Reviewed; 449 AA.
AC P86934; P41166; Q38C32;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha 1;
GN Name=TEF1; ORFNames=Tb10.70.5650;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 18-415.
RX PubMed=8265589; DOI=10.1073/pnas.90.24.11558;
RA Baldauf S.L., Palmer J.D.;
RT "Animals and fungi are each other's closest relatives: congruent evidence
RT from multiple proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11558-11562(1993).
RN [3]
RP PROTEIN SEQUENCE OF 279-301 AND 360-366, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND ETHANOLAMINYLATION AT GLU-362.
RX PubMed=18499667; DOI=10.1074/jbc.m802430200;
RA Signorell A., Jelk J., Rauch M., Buetikofer P.;
RT "Phosphatidylethanolamine is the precursor of the ethanolamine
RT phosphoglycerol moiety bound to eukaryotic elongation factor 1A.";
RL J. Biol. Chem. 283:20320-20329(2008).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphatidylethanolamine (PE) is a direct precursor of the
CC ethanolamine-phosphoglycerol (EPG) moiety.
CC {ECO:0000269|PubMed:18499667}.
CC -!- MISCELLANEOUS: The Kennedy pathway is the major route for
CC phosphatidylethanolamine (PE) synthesis, as shown by reduced levels
CC after using RNAi against the first two enzymes of the Kennedy pathway.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; CM000208; EAN77638.1; -; Genomic_DNA.
DR EMBL; L25868; AAA16602.1; -; Unassigned_DNA.
DR RefSeq; XP_822465.1; XM_817372.1.
DR RefSeq; XP_822466.1; XM_817373.1.
DR AlphaFoldDB; P86934; -.
DR SMR; P86934; -.
DR STRING; 5691.EAN77637; -.
DR PaxDb; P86934; -.
DR GeneID; 3662245; -.
DR GeneID; 3662318; -.
DR KEGG; tbr:Tb10.70.5650; -.
DR KEGG; tbr:Tb10.70.5670; -.
DR VEuPathDB; TriTrypDB:Tb11.v5.1046; -.
DR VEuPathDB; TriTrypDB:Tb927.10.2090; -.
DR VEuPathDB; TriTrypDB:Tb927.10.2100; -.
DR VEuPathDB; TriTrypDB:Tb927.10.2110; -.
DR eggNOG; KOG0052; Eukaryota.
DR InParanoid; P86934; -.
DR OMA; VACTFES; -.
DR Proteomes; UP000008524; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005516; F:calmodulin binding; ISA:GeneDB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:GeneDB.
DR GO; GO:0007017; P:microtubule-based process; TAS:GeneDB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..449
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000412120"
FT DOMAIN 5..230
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 362
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:18499667"
SQ SEQUENCE 449 AA; 49106 MW; D597D39CE436660D CRC64;
MGKEKVHMNL VVVGHVDAGK STATGHLIYK CGGIDKRTIE KFEKEAADIG KASFKYAWVL
DKLKAERERG ITIDIALWKF ESPKSVFTII DAPGHRDFIK NMITGTSQAD AAILIIASAQ
GEFEAGISKD GQTREHALLA FTLGVKQMVV CCNKMDDKTV NYGQERYDEI VKEVSAYIKK
VGYNVEKVRF VPISGWQGDN MIEKSEKMPW YKGPTLLEAL DMLEPPVRPS DKPLRLPLQD
VYKIGGIGTV PVGRVETGVM KPGDVVTFAP ANVTTEVKSI EMHHEQLAEA TPGDNVGFNV
KNVSVKDIRR GNVCGNTKND PPKEAADFTA QVIILNHPGQ IGNGYAPVLD CHTSHIACKF
AEIESKIDRR SGKELEKAPK SIKSGDAAIV RMVPQKPMCV EVFNDYAPLG RFAVRDMRQT
VAVGIIKAVT KKDGSGGKVT KAAVKASKK
