ID D9Q2Q0_ACIS3 Unreviewed; 436 AA. AC D9Q2Q0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-SEP-2017, entry version 51. DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-1-alpha {ECO:0000256|HAMAP-Rule:MF_00118}; DE AltName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=ASAC_1183 {ECO:0000313|EMBL:ADL19588.1}; OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / OS 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19588.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL19588.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; 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. {ECO:0000256|HAMAP-Rule:MF_00118, CC ECO:0000256|SAAS:SAAS00088930}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118, CC ECO:0000256|SAAS:SAAS00384784}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000256|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; CP001742; ADL19588.1; -; Genomic_DNA. DR RefSeq; WP_013267100.1; NC_014374.1. DR ProteinModelPortal; D9Q2Q0; -. DR STRING; 666510.ASAC_1183; -. DR EnsemblBacteria; ADL19588; ADL19588; ASAC_1183. DR GeneID; 9499435; -. DR KEGG; asc:ASAC_1183; -. DR eggNOG; arCOG01561; Archaea. DR eggNOG; COG5256; LUCA. DR HOGENOM; HOG000229291; -. DR KO; K03231; -. DR OMA; AIRDMGM; -. DR OrthoDB; POG093Z025H; -. DR Proteomes; UP000000346; Chromosome. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000000346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118, KW ECO:0000256|SAAS:SAAS00088926}; KW Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118, KW ECO:0000313|EMBL:ADL19588.1}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118}; KW Hydrolase {ECO:0000313|EMBL:ADL19588.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}. FT DOMAIN 4 227 Tr-type G. {ECO:0000259|PROSITE:PS51722}. FT NP_BIND 13 20 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}. FT NP_BIND 90 94 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}. FT NP_BIND 152 155 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}. 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 //