EF1A_THEGJ
ID EF1A_THEGJ Reviewed; 428 AA.
AC C5A5P4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=TGAM_1054;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33556.1; -; Genomic_DNA.
DR RefSeq; WP_015858670.1; NC_012804.1.
DR AlphaFoldDB; C5A5P4; -.
DR SMR; C5A5P4; -.
DR STRING; 593117.TGAM_1054; -.
DR PaxDb; C5A5P4; -.
DR EnsemblBacteria; ACS33556; ACS33556; TGAM_1054.
DR GeneID; 7986928; -.
DR KEGG; tga:TGAM_1054; -.
DR PATRIC; fig|593117.10.peg.1051; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_0_0_2; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; 13117at2157; -.
DR Proteomes; UP000001488; 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.
FT CHAIN 1..428
FT /note="Elongation factor 1-alpha"
FT /id="PRO_1000203022"
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; 47515 MW; 80D6C0BD1E8B1910 CRC64;
MAKEKPHVNI VFIGHVDHGK STTIGRLLFD TANIPENIIK KFEEMGEKGK SFKFAWVMDR
LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM ITGASQADAA VLVVAATDGV
MPQTKEHAFL ARTLGINHII VAINKMDMVN YDQKVFEKVK AQVEKLLKML GYKDFPVIPI
SAWEGDNVVK KSDKMPWYKG PTLIEALDQI PEPPKPIDKP LRIPIQDVYS IKGVGTVPVG
RVETGVLRVG DVVIFEPAST IFHKPIQGEV KSIEMHHEPL QEAYPGDNIG FNVRGVGKND
IKRGDVAGHT TNPPTVVRPK DTFKAQIIVL NHPTAITVGY TPVLHAHTTQ VAVRFEQLLA
KLDPRTGNIV EENPQFIKTG DSAIVILRPT KAMVIEPVKE IPQMGRFAIR DMGQTVAAGM
VISIQKAE
