EF1A_THECE
ID EF1A_THECE Reviewed; 428 AA.
AC P17197;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Thermococcus celer.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115672; DOI=10.1093/nar/18.13.3989;
RA Auer J., Spicker G., Boeck A.;
RT "Nucleotide sequence of the gene for elongation factor EF-1 alpha from the
RT extreme thermophilic archaebacterium Thermococcus celer.";
RL Nucleic Acids Res. 18:3989-3989(1990).
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; X52383; CAA36610.1; -; Genomic_DNA.
DR PIR; S10248; S10248.
DR AlphaFoldDB; P17197; -.
DR SMR; P17197; -.
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_0000090997"
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; 47505 MW; 682E5A55C05DEC70 CRC64;
MAKEKPHINI VFIGHVDHGK STTIGRLLFD TANIPENIIK KFEEMGEKGK SFKFAWVMDR
LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM ITGASQADAA VLVVAVTDGV
MPQTKEHAFL ARTLGINNIL VAVNKMDMVN YDEKKFKAVA EQVKKLLMML GYKNFPIIPI
SAWEGDNVVK KSDKMPWYNG PTLIEALDQM PEPPKPTDKP LRIPIQDVYS IKGVGTVPVG
RVETGVLRVG DVVIFEPAST IFHKPIQGEV KSIEMHHEPM QEALPGDNIG FNVRGVGKND
IKRGDVAGHT NNPPTVVRPK DTFKAQIIVL NHPTAITVGY TPVLHAHTLQ VAVRFEQLLA
KLDPRTGNIV EENPQFIKTG DSAIVVLRPT KPMVIEPVKE IPQMGRFAIR DMGQTVAAGM
VISIQKAE
