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 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE ELONGATION FACTOR 1-ALPHA (EF-1-ALPHA). GN TUX. OS DESULFUROCOCCUS MOBILIS. OC ARCHAEBACTERIA; CRENARCHAEOTA; THERMOPROTEALES; DESULFUROCOCCACEAE. 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.; 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 --------------------------------------------------------------------------- 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; E80508; -. DR PROSITE; PS00301; EFACTOR_GTP. 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 //