ID EF1A_DESMO Reviewed; 438 AA. AC P41203; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 02-OCT-2024, entry version 103. 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=tux; OS Desulfurococcus mucosus (Desulfurococcus mobilis). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Desulfurococcus. OX NCBI_TaxID=2275; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35582 / DSM 2161 / JCM 9186 / Hvv 3/9; RX PubMed=7898436; DOI=10.1007/bf00290714; RA Ceccarelli E., Bocchetta M., Creti R., Sanangelantoni A.M., Tiboni O., RA Cammarano P.; RT "Chromosomal organization and nucleotide sequence of the genes for RT elongation factors EF-1 alpha and EF-2 and ribosomal proteins S7 and S10 of RT the hyperthermophilic archaeum Desulfurococcus mobilis."; RL Mol. Gen. Genet. 246:687-696(1995). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X73582; CAA51984.1; -; Genomic_DNA. DR AlphaFoldDB; P41203; -. DR SMR; P41203; -. 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; IPR050100; TRAFAC_GTPase_members. 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 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; PF22594; GTP-eEF1A_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 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. FT CHAIN 1..438 FT /note="Elongation factor 1-alpha" FT /id="PRO_0000090976" FT DOMAIN 6..229 FT /note="tr-type G" FT REGION 15..22 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 71..75 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 92..95 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 154..157 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 195..197 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 15..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 92..96 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 154..157 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 438 AA; 48737 MW; 4A4955EE6CB39427 CRC64; MSAPQKPHLN IVIIGHVDHG KSTMTGHILY RLGYFDEKTV KMIEEESKKM GKESFKFAWL LDRMKEERER GVTISLSYMK FETKKYFFTI IDAPGHRDFV KNMITGASQA DAAILVVSAR KGEFEAGMSA EGQTREHAIL ARTMGINQLI VAINKMDATE PPYSEKRYNE IKEILGKFLK GLGYDVSKIP FIPISAWTGE NLIERSPNMP WYNGPTLVEA LDTLEVPPKP INKPLRIPIQ DVYNISGIGV VPVGRVETGV LKVGDKLVFM PAGLVAEVKT IETHHTKIEK AEPGDNIGFN VKGVEKKDIK RGDVAGSLDV PPTVADEFTA RIMVMWHPTA IAVGYTPVIH VHTASVACRI TEIIAKIDPR TGKEIEKNPH FLKQGDIAIV KFKPIKPLVV EKYSDFQGLG RFAMRDMGKT IGIGQVLEIK PAQVNIKK //