ID   EF1A_PYRWO              Reviewed;         430 AA.
AC   P26751;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1723106; DOI=10.1007/bf02102864;
RA   Creti R., Citarella F., Tiboni O., Sanangelantoni A.M., Palm P.,
RA   Cammarano P.;
RT   "Nucleotide sequence of a DNA region comprising the gene for elongation
RT   factor 1 alpha (EF-1 alpha) from the ultrathermophilic archaeote Pyrococcus
RT   woesei: phylogenetic implications.";
RL   J. Mol. Evol. 33:332-342(1991).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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|HAMAP-Rule:MF_00118}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59857; CAA42517.1; -; Genomic_DNA.
DR   PIR; S19000; S19000.
DR   AlphaFoldDB; P26751; -.
DR   SMR; P26751; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; IPR005225; Small_GTP-bd_dom.
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   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..430
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090992"
FT   DOMAIN          7..219
FT                   /note="tr-type G"
FT   REGION          16..23
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          146..149
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          183..185
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         146..149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   430 AA;  47923 MW;  F471B48ED38A8059 CRC64;
     MKMPKDKPHV NIVFIGHVDH GKSTTIGRLL YDTGNIPEQI IKKFEEMGEK GKSFKFAWVM
     DRLREERERG ITIDVAHTKF ETPHRYITII DAPGHRDFVK NMITGASQAD AAVLVVAATD
     GVMPQTKEHA FLARTLGIKH IIVAINKMDM VNYNQKRFEE VKAQVEKLLK MLGYKDFPVI
     PISAWEGENV VKKSDKMPWY NGPTLIEALD QIPEPEKPVD KPLRIPIQDV YSIKGVGTVP
     VGRVETGKLR VGEVVIFEPA STIFHKPIQG EVKSIEMHHE PLEEALPGDN IGFNVRGVSK
     NDIKRGDVAG HTTNPPTVVR TKDTFKAQII VLNHPTAITV GYSPVLHAHT AQVPVRFEQL
     LAKLDPKTGN IVEENPQFIK TGDAAIVILR PMKPVVLEPV KEIPQLGRFA IRDMGMTIAA
     GMVISIQRGE