ID D8S6G0_SELML Unreviewed; 397 AA. AC D8S6G0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325}; GN ORFNames=SELMODRAFT_153081 {ECO:0000313|EMBL:EFJ20057.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ20057.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I., RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}. 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|ARBA:ARBA00007249, CC ECO:0000256|RuleBase:RU000325}. 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; GL377604; EFJ20057.1; -; Genomic_DNA. DR RefSeq; XP_002979100.1; XM_002979054.1. DR AlphaFoldDB; D8S6G0; -. DR STRING; 88036.D8S6G0; -. DR EnsemblPlants; EFJ20057; EFJ20057; SELMODRAFT_153081. DR GeneID; 9659605; -. DR Gramene; EFJ20057; EFJ20057; SELMODRAFT_153081. DR KEGG; smo:SELMODRAFT_153081; -. DR eggNOG; KOG0460; Eukaryota. DR HOGENOM; CLU_007265_0_0_1; -. DR InParanoid; D8S6G0; -. DR OMA; FHNNYRP; -. DR OrthoDB; 167272at2759; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central. DR GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03707; EFTU_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR033720; EFTU_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. 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; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, KW ECO:0000256|RuleBase:RU000325}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000325}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. FT DOMAIN 8..204 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" SQ SEQUENCE 397 AA; 43303 MW; 9A92BCA05E72DE6B CRC64; MATFTRTKPH MNIGTIGHVD HGKTTLTAAI TKVLASEGRA KAIAFEDIDK APEERKRGIT ISAAHVEYET ANRHYGHVDC PGHADYVKNM ITGAAQMDGG ILVVSAPDGP MPQTKEHILL ARQVGVPSLV CFLNKVDAVE DEELLELVEM ELRELLSFYK FPGDDIPIIR GSALQALQGT NDETGKNSIL KLMEAVDTYI PEPKRVLDKP FLLAVEDVFS IQGRGTVATG RIEQGVIKVG EEVEIVGLKE SGPQKSVVTG VEMFKKILDQ GQAGDNVGLL LRGLKREDIS RGQVICKPGT IKTYKKFEAE IYVLSKDEGG RHTPFFSNYR PQFYLRTADV TGTITLPENV KMVMPGDNVS LKFELRVPAP IEAGQRFALR EGGRTVGAGV ISKVIPG //