ID EF1A_DESMO STANDARD; PRT; 438 AA. AC P41203; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE ELONGATION FACTOR 1-ALPHA (EF-1-ALPHA) (ELONGATION FACTOR TU) (EF-TU). GN TUF OR TUX. OS Desulfurococcus mobilis. OC Archaea; Crenarchaeota; Thermoproteales; Desulfurococcaceae; OC Desulfurococcus. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSM 2126; RX MEDLINE; 95206243. 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. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY. CC EF-TU/EF-1A SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR HSSP; P07157; 1AIP. DR PFAM; PF00009; GTP_EFTU; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Elongation factor; Protein biosynthesis; GTP-binding. FT NP_BIND 15 22 GTP (BY SIMILARITY). FT NP_BIND 92 96 GTP (BY SIMILARITY). FT NP_BIND 154 157 GTP (BY SIMILARITY). SQ SEQUENCE 438 AA; 48737 MW; B78E2BF6 CRC32; 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 //