ID   EF1A_GIAIN              Reviewed;         396 AA.
AC   Q08046; Q94838;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   AltName: Full=14 nm filament-associated protein;
DE   Flags: Fragment;
GN   Name=TEF1;
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8121287; DOI=10.1093/oxfordjournals.molbev.a040093;
RA   Hashimoto T., Nakamura Y., Nakamura F., Shirakura T., Adachi J., Goto N.,
RA   Okamoto K., Hasegawa M.;
RT   "Protein phylogeny gives a robust estimation for early divergences of
RT   eukaryotes: phylogenetic place of a mitochondria-lacking protozoan, Giardia
RT   lamblia.";
RL   Mol. Biol. Evol. 11:65-71(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-273.
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).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; D14342; BAA03276.1; -; mRNA.
DR   EMBL; L23957; AAA16601.1; -; Genomic_DNA.
DR   PIR; A49394; A49394.
DR   AlphaFoldDB; Q08046; -.
DR   SMR; Q08046; -.
DR   PRIDE; Q08046; -.
DR   VEuPathDB; GiardiaDB:DHA2_153303; -.
DR   VEuPathDB; GiardiaDB:GL50581_413; -.
DR   VEuPathDB; GiardiaDB:GL50803_00112312; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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   Protein biosynthesis.
FT   CHAIN           <1..>396
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090925"
FT   DOMAIN          <1..211
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         396
SQ   SEQUENCE   396 AA;  43951 MW;  3C16F5E3DDD83EBD CRC64;
     STLTGHLIYK CGGIDQRTID EYEKRATEMG KGSFKYAWVL DQLKDERERG ITINIALWKF
     ETKKYIVTII DAPGHRDFIK NMITGTSQAD VAILVVAAGQ GEFEAGISKD GQTREHATLA
     NTLGIKTMII CVNKMDDGQV KYSKERYDEI KGEMMKQLKN IGWKKAEEFD YIPTSGWTGD
     NIMEKSDKMP WYEGPCLIDA IDGLKAPKRP TDKPLRLPIQ DVYKISGVGT VPAGRVETGE
     LAPGMKVVFA PTSQVSEVKS VEMHHEELKK AGPGDNVGFN VRGLAVKDLK KGYVVGDVTN
     DPPVGCKSFT AQVIVMNHPK KIQPGYTPVI DCHTAHIACQ FQLFLQKLDK RTLKPEMENP
     PDAGRGDCII VKMVPQKPLC CETFNDYAPL GPFAVR