ID I7MGI2_TETTS Unreviewed; 447 AA. AC I7MGI2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 2. DT 27-MAR-2024, entry version 57. DE RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325}; GN ORFNames=TTHERM_00151810 {ECO:0000313|EMBL:EAS01468.2}; OS Tetrahymena thermophila (strain SB210). OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS01468.2, ECO:0000313|Proteomes:UP000009168}; RN [1] {ECO:0000313|Proteomes:UP000009168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168}; RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286; RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R., RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L., RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M., RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L., RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y., RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z., RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A., RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A., RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A., RA Hamilton E.P., Orias E.; RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a RT model eukaryote."; RL PLoS Biol. 4:1620-1642(2006). 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; GG662603; EAS01468.2; -; Genomic_DNA. DR RefSeq; XP_001021714.2; XM_001021714.3. DR AlphaFoldDB; I7MGI2; -. DR STRING; 312017.I7MGI2; -. DR GeneID; 7835984; -. DR KEGG; tet:TTHERM_00151810; -. DR InParanoid; I7MGI2; -. DR OrthoDB; 167272at2759; -. DR Proteomes; UP000009168; Unassembled WGS sequence. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. 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; IEA:UniProtKB-UniRule. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. 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:UP000009168}. FT DOMAIN 31..227 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" SQ SEQUENCE 447 AA; 49103 MW; 4DAEB33C1CE5BDA1 CRC64; MFKNILKLGS NTQKTLSAIP CYGFAKFQRN KPHLNVGTIG HIDHGKTTLT AAITKICADK KLAEFMAYDS IDKAPEEKAR GITINTATVE YETETRHYGH VDCPGHIDYV KNMITGAAKM DAGILVCSAT DGVMPQTREH ILLCRQVGVK TIIVFVNKCD MAKDPEIQEL VEMEVRELLS KYEYNGDEAP VIFGSALCAL NGTDPEIGIN KINTLLDTMD KQIALPERTV DKPFMMSVEG TYQIPGRGTV VTGTVDTGKV KTGEDIEIVG YSNKVLKTTI TGIETFRKQL DYAEAGDNVG LLLRGVTRDD VRRGQVLSKP GTQESHKKIE ANLYILTEQE GGRKKPFPDG YRPQLYLRTA DVAAQISIHG ANKLGMPGDN ITANLDLHFP LPVAPGKLTI ILFNNQCQQQ NNFQIKGLRF ALREGGKTIA AGVISKVIPE EKEAPKK //