ID   EF1A_TRYBB              Reviewed;         449 AA.
AC   P86933; P41166; Q38C32;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
GN   Name=TEF1;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LVH/75/USAMRU-K/18;
RX   PubMed=8083206; DOI=10.1016/s0021-9258(17)31617-4;
RA   Kaur K.J., Ruben L.;
RT   "Protein translation elongation factor-1 alpha from Trypanosoma brucei
RT   binds calmodulin.";
RL   J. Biol. Chem. 269:23045-23050(1994).
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. {ECO:0000250}.
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; U10562; AAA57476.1; -; mRNA.
DR   PIR; A54760; A54760.
DR   AlphaFoldDB; P86933; -.
DR   SMR; P86933; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:GeneDB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0019722; P:calcium-mediated signaling; TAS:GeneDB.
DR   GO; GO:0007017; P:microtubule-based process; TAS:GeneDB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..449
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090931"
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:0000250"
SQ   SEQUENCE   449 AA;  49034 MW;  F21113FB80A5116A CRC64;
     MGKEKVHMNL VVVGHVDAGK STATGHLIYK CGGIDKRTIE KFEKEAADIG KASFKYAWVL
     DKLKAERERG ITIDIALWKF ESPKSVFTII DAPGHRDFIK NMITGTSQAD AAILIIASAQ
     GEFEAGISKD GQTREHALLA FTLGVKQMVV CCNKMDDKTV NYGQERYDEI VKEVSAYIKK
     VGYNVEKVRF VPISGWQGDN MIEKSEKMPW YKGPTLLEAL DMLEPPVRPS DKPLRLPLQT
     CTKIGGIGTV PVGRVETGVM KPGDVVTFAP ANVTTEVKSI EMHHEQLAEA TPGDNVGFNV
     KNVSVKDIRR GNVCGNTKND PPKEAADFTA QVIILNHPGQ IGNGYAPVLD CHTSHIACKF
     AEIESKIDRR SGKELEKAPK SIKSGDAAIV RMVPQKPMCV EVFNDYAPLG RFAVRDMRQT
     VAVGIIKAVT KKDGSGGKVT KAAVKASKK