ID   EF1A_THEKO              Reviewed;         428 AA.
AC   Q5JFZ4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=TK0308;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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}.
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DR   EMBL; AP006878; BAD84497.1; -; Genomic_DNA.
DR   RefSeq; WP_011249263.1; NC_006624.1.
DR   AlphaFoldDB; Q5JFZ4; -.
DR   SMR; Q5JFZ4; -.
DR   IntAct; Q5JFZ4; 1.
DR   MINT; Q5JFZ4; -.
DR   STRING; 69014.TK0308; -.
DR   EnsemblBacteria; BAD84497; BAD84497; TK0308.
DR   GeneID; 3234817; -.
DR   KEGG; tko:TK0308; -.
DR   PATRIC; fig|69014.16.peg.307; -.
DR   eggNOG; arCOG01561; Archaea.
DR   HOGENOM; CLU_007265_0_0_2; -.
DR   InParanoid; Q5JFZ4; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; 13117at2157; -.
DR   PhylomeDB; Q5JFZ4; -.
DR   Proteomes; UP000000536; Chromosome.
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; Reference proteome.
FT   CHAIN           1..428
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090991"
FT   DOMAIN          5..215
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          68..72
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          89..92
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          144..147
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          181..183
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         89..93
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   428 AA;  47516 MW;  2A32B9CDBFCECE59 CRC64;
     MAKEKPHVNI VFIGHVDHGK STTIGRLLFD TANIPENIIK KFEEMGEKGK SFKFAWVMDR
     LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM ITGASQADAA VLVVAATDGV
     MPQTKEHAFL ARTLGINHII VAINKMDMVN YDEKKFKQVA EQVKKLLQML GYKDFPIIPI
     SAWEGDNVVK KSDKMPWYNG PTLLEALDQI PEPPKPVDKP LRIPIQDVYS IKGVGTVPVG
     RVETGVLRVG DVVIFEPAST IFHKPIQGEV KSIEMHHEPL QEAYPGDNIG FNVRGVGKND
     IKRGDVAGHT TNPPTVVRPK DTFKAQIIVL NHPTAITVGY TPVLHAHTTQ VAVRFEQLLA
     KLDPRTGNIV EENPQFIKTG DSAIVILRPT KAMVIEPVKE IPQMGRFAIR DMGQTVAAGM
     VISIQKAD