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 05-JUL-2017, entry version 84. 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 mobilis. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Desulfurococcus. OX NCBI_TaxID=2274; 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 RT S10 of the hyperthermophilic archaeum Desulfurococcus mobilis."; RL Mol. Gen. Genet. 246:687-696(1995). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. {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 ProteinModelPortal; P41203; -. DR SMR; P41203; -. DR PRIDE; P41203; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 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; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. 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. FT CHAIN 1 438 Elongation factor 1-alpha. FT /FTId=PRO_0000090976. FT DOMAIN 6 229 tr-type G. FT NP_BIND 15 22 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 92 96 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 154 157 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT REGION 15 22 G1. {ECO:0000250}. FT REGION 71 75 G2. {ECO:0000250}. FT REGION 92 95 G3. {ECO:0000250}. FT REGION 154 157 G4. {ECO:0000250}. FT REGION 195 197 G5. {ECO:0000250}. 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 //