EF1A_HALWD
ID EF1A_HALWD Reviewed; 421 AA.
AC Q18EY5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=HQ_3385A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53482.1; -; Genomic_DNA.
DR RefSeq; WP_011572579.1; NC_008212.1.
DR AlphaFoldDB; Q18EY5; -.
DR SMR; Q18EY5; -.
DR STRING; 362976.HQ_3385A; -.
DR EnsemblBacteria; CAJ53482; CAJ53482; HQ_3385A.
DR GeneID; 4194747; -.
DR KEGG; hwa:HQ_3385A; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000001975; 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_0000337602"
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"
SQ SEQUENCE 421 AA; 45614 MW; 14F868054D79BEDE CRC64;
MSDKPHQNLA IIGHVDHGKS TLVGRLLFET GSVPEHVIEQ HREEAEEKGK GGFEFAYVMD
NLAEERERGV TIDIAHQEFD TEDYYFTIVD CPGHRDFVKN MITGASQADN AVLVVAADDG
VAPQTREHVF LARTLGINEL IIGVNKMDIV DYSEETYEDV KTEVDKLLKQ VQFNANDAKY
IPISAFEGDN VAESSDNTSW FDGPSLLEAL NNLPEPQPPT DAPLRLPIQD VYTISGIGTV
PVGRVETGTV SPGDDVSFQP SDVGGEVKTV EMHHEEVDQA GPGDNVGFNV RGIGKDDIRR
GDVCGPSSNA PTVAETFKAQ VVVMQHPSVI TAGYTPVFHA HTAQVACTIE SIDQKLDPAS
GEVAEEDPDF IKSGDAAVVT VRPQKPLSIE PSNEIPELGS FAVRDMGQTI AAGKVLEVDE
R
