ID EF1A_PYRFU Reviewed; 428 AA.
AC Q8U152;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=PF1375;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81499.1; -; Genomic_DNA.
DR RefSeq; WP_011012522.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U152; -.
DR SMR; Q8U152; -.
DR IntAct; Q8U152; 1.
DR STRING; 186497.PF1375; -.
DR PaxDb; 186497-PF1375; -.
DR GeneID; 41713182; -.
DR KEGG; pfu:PF1375; -.
DR PATRIC; fig|186497.12.peg.1438; -.
DR eggNOG; arCOG01561; Archaea.
DR HOGENOM; CLU_007265_3_5_2; -.
DR OrthoDB; 371718at2157; -.
DR PhylomeDB; Q8U152; -.
DR Proteomes; UP000001013; 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 CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..428
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090989"
FT DOMAIN 5..217
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; 47635 MW; BDB7A52BEC528366 CRC64;
MPKDKPHVNI VFIGHVDHGK STTIGRLLYD TGNIPEQIIK KFEEMGEKGK SFKFAWVMDR
LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM ITGASQADAA VLVVAATDGV
MPQTKEHAFL ARTLGIKHII VAINKMDMVN YNQKRFEEVK AQVEKLLKML GYKDFPVIPI
SAWEGENVVK KSDKMPWYNG PTLIEALDQI PEPEKPVDKP LRIPIQDVYS IKGVGTVPVG
RVETGKLRVG EVVIFEPAST IFHKPIQGEV KSIEMHHEPL EEALPGDNIG FNVRGVSKND
IKRGDVAGHT TNPPTVVRTK DTFKAQIIVL NHPTAITVGY SPVLHAHTAQ VPVRFEQLLA
KLDPKTGNIV EENPQFIKTG DAAIVILRPM KPVVLEPVKE IPQLGRFAIR DMGMTIAAGM
VISIQRGE
//
