EF1A_THEAC
ID EF1A_THEAC Reviewed; 424 AA.
AC P19486;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=Ta0444;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=2272495; DOI=10.1016/0378-1097(90)90236-j;
RA Tesch A., Klink F.;
RT "Cloning and sequencing of the gene coding for the elongation factor 1
RT alpha from the archaebacterium Thermoplasma acidophilum.";
RL FEMS Microbiol. Lett. 59:293-297(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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|HAMAP-Rule:MF_00118}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X53866; CAA37860.1; -; Genomic_DNA.
DR EMBL; AL445064; CAC11586.1; ALT_INIT; Genomic_DNA.
DR PIR; S12090; S12090.
DR RefSeq; WP_048161592.1; NC_002578.1.
DR AlphaFoldDB; P19486; -.
DR SMR; P19486; -.
DR STRING; 273075.Ta0444; -.
DR EnsemblBacteria; CAC11586; CAC11586; CAC11586.
DR GeneID; 1456053; -.
DR KEGG; tac:Ta0444; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; 13117at2157; -.
DR Proteomes; UP000001024; 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..424
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090996"
FT DOMAIN 5..223
FT /note="tr-type G"
FT REGION 14..21
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 148..151
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 187..189
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 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 120
FT /note="E -> D (in Ref. 1; CAA37860)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="R -> L (in Ref. 1; CAA37860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47026 MW; 49A71BABDEA1EF50 CRC64;
MASQKPHLNL ITIGHVDHGK STLVGRLLYE HGEIPAHIIE EYRKEAEQKG KATFEFAWVM
DRFKEERERG VTIDLAHRKF ETDKYYFTLI DAPGHRDFVK NMITGTSQAD AAILVISARE
GEGVMEQTRE HAFLARTLGV PQMVVAINKM DATSPPYSEK RYNEVKADAE KLLRSIGFKD
ISFVPISGYK GDNVTKPSPN MPWYKGPTLL QALDAFKVPE KPINKPLRIP VEDVYSITGI
GTVPVGRVET GVLKPGDKVI FLPADKQGDV KSIEMHHEPL QQAEPGDNIG FNVRGIAKND
IKRGDVCGHL DTPPTVVKAF TAQIIVLNHP SVIAPGYKPV FHVHTAQVAC RIDEIVKTLN
PKDGTTLKEK PDFIKNGDVA IVKVIPDKPL VIEKVSEIPQ LGRFAVRDMG QTVAAGQCID
LEKR
