ID D9Q2Q0_ACIS3 Unreviewed; 436 AA. AC D9Q2Q0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 06-MAR-2013, entry version 21. DE RecName: Full=Elongation factor 1-alpha; DE Short=EF-1-alpha; DE AltName: Full=Elongation factor Tu; GN Name=tuf; OrderedLocusNames=ASAC_1183; OS Acidilobus saccharovorans (strain DSM 16705 / VKM B-2471 / 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / VKM B-2471 / 345-15; RX PubMed=20581186; DOI=10.1128/AEM.00599-10; RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans RT supports a new order, Acidilobales, and suggests an important RT ecological role in terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. CC EF-Tu/EF-1A subfamily. 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; CP001742; ADL19588.1; -; Genomic_DNA. DR RefSeq; YP_003816619.1; NC_014374.1. DR ProteinModelPortal; D9Q2Q0; -. DR GeneID; 9499435; -. DR GenomeReviews; CP001742_GR; ASAC_1183. DR KEGG; asc:ASAC_1183; -. DR HOGENOM; HOG000229291; -. DR KO; K03231; -. DR OMA; DPYEQNR; -. DR BioCyc; ASAC666510:GH9G-1224-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP. DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC. DR HAMAP; MF_00118_A; EF_Tu_A; 1; -. DR InterPro; IPR000795; EF_GTP-bd_dom. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel. 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; Elong_init_C; 1. DR SUPFAM; SSF50447; Translat_factor; 1. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Hydrolase; Nucleotide-binding; Protein biosynthesis. FT NP_BIND 13 20 GTP (By similarity). FT NP_BIND 90 94 GTP (By similarity). FT NP_BIND 152 155 GTP (By similarity). SQ SEQUENCE 436 AA; 48023 MW; 2D3368DFC92E98B7 CRC64; MPEKPHLNLV VIGHIDHGKS TLTGSLLYRL GVIDPKIMQQ LEEQAKAAGK ESFKFAWLLD KMKEERERGI TIDLSFMKFE TKKYYFTIID APGHRDFVKN MITGASQADA ALLVISSRKG EFEAGMSAEG QTREHALLAK TLGIEQLIVV VNKMDAPDVN YSQQRYEEIV NTMKKFLKGL GYNVDAIPFV PVSAWTGENL IERSPNMPWY KGPTLVEALD NLKVPPKPVD KPLRLPVQSV LSIPGAGTVV TGRVETGVLK PGDKVIVMPE GVVADVKSIQ MHYQDLQQAE PGDNVGVALR GVEKNQVKRG DVIGKTDNPP TVAEEFTARV VVVWHPSAIA VGYTPVIHVH TASVACRITE IVAKLDPRTG NPIEQNPQFI KAGDTAIVKF KPIKPLVIEK FGEFPQLGRF AMRDMGRTIG IGIVTDIKPA KIEVKK //