EF1A_HALSA
ID EF1A_HALSA Reviewed; 421 AA.
AC Q9HM89; P48863;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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}; Synonyms=eef1a;
GN OrderedLocusNames=VNG_2649G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A9;
RX PubMed=8653072;
RA Fujita T., Itoh T.;
RT "Organization and nucleotide sequence of a gene cluster comprising the
RT translation elongation factor 1 alpha, ribosomal protein S10 and tRNA(Ala)
RT from Halobacterium halobium.";
RL Biochem. Mol. Biol. Int. 37:107-115(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; D32120; BAA06845.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG20682.1; -; Genomic_DNA.
DR PIR; F84414; F84414.
DR PIR; T09379; T09379.
DR RefSeq; WP_010903986.1; NC_002607.1.
DR AlphaFoldDB; Q9HM89; -.
DR SMR; Q9HM89; -.
DR STRING; 64091.VNG_2649G; -.
DR PaxDb; Q9HM89; -.
DR EnsemblBacteria; AAG20682; AAG20682; VNG_2649G.
DR GeneID; 5954258; -.
DR GeneID; 62887863; -.
DR KEGG; hal:VNG_2649G; -.
DR PATRIC; fig|64091.14.peg.2058; -.
DR HOGENOM; CLU_007265_3_5_2; -.
DR InParanoid; Q9HM89; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; 13117at2157; -.
DR PhylomeDB; Q9HM89; -.
DR Proteomes; UP000000554; 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..421
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090978"
FT DOMAIN 4..220
FT /note="tr-type G"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 69..73
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 145..148
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 184..186
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 90..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 48
FT /note="K -> E (in Ref. 1; BAA06845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 45479 MW; CDB76D625C18C224 CRC64;
MSDNRHQNLA VIGHVDHGKS TMVGRLLYET GSVPEHVIEQ HKEEAEEKGK GGFEFAYVMD
NLAEERERGV TIDIAHQEFT TDEYEFTIVD CPGHRDFVKN MITGASQADN AVLVVAADDG
VAPQTREHVF LSRTLGIDEL IVAVNKMDVV DYDESKYNEV VSGVKDLFGQ VGFNPDDAKF
IATSAFEGDN VSDHSDNTPW YDGPTLLEAL NGLPVPQPPT DADLRLPIQD VYTISGIGTV
PVGRIETGVM NTGDNVSFQP SDVGGEVKTI EMHHEEVPNA EPGDNVGFNV RGIGKDDIRR
GDVCGPADDP PSVADTFQAQ VVVMQHPSVI TAGYTPVFHA HTAQVACTIE SIDKKMDPAS
GETQEENPDF IQSGDAAVVT VRPQKPLSLE PSSEIPELGS FAVRDMGQTI AAGKVLDVDE
A
