ID Q23TC1_TETTS Unreviewed; 600 AA. AC Q23TC1; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 02-SEP-2026, entry version 96. DE SubName: Full=Elongation factor Tu protein {ECO:0000313|EMBL:EAR99785.1}; GN ORFNames=TTHERM_00666610 {ECO:0000313|EMBL:EAR99785.1}; 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:EAR99785.1, 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 -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000256|ARBA:ARBA00049117}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000256|ARBA:ARBA00049117}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. 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 --------------------------------------------------------------------------- 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; GG662636; EAR99785.1; -; Genomic_DNA. DR RefSeq; XP_001020030.1; XM_001020030.1. DR AlphaFoldDB; Q23TC1; -. DR STRING; 312017.Q23TC1; -. DR GeneID; 7842500; -. DR KEGG; tet:TTHERM_00666610; -. DR eggNOG; KOG0458; Eukaryota. DR HOGENOM; CLU_007265_3_5_1; -. DR InParanoid; Q23TC1; -. DR OMA; VVQITCH; -. DR OrthoDB; 342024at2759; -. DR Proteomes; UP000009168; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR CDD; cd01883; EF1_alpha; 1. DR CDD; cd04093; HBS1_C_III; 1. DR FunFam; 2.40.30.10:FF:000070; Translation elongation factor EF-1 subunit; 1. DR FunFam; 3.40.50.300:FF:000204; Translation elongation factor Tu; 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; IPR054696; GTP-eEF1A_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR050100; TRAFAC_GTPase_members. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF22594; GTP-eEF1A_C; 1. DR Pfam; PF00009; GTP_EFTU; 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; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Elongation factor {ECO:0000313|EMBL:EAR99785.1}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PROSITE- KW ProRule:PRU01059}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU01059}; Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}; KW Reference proteome {ECO:0000313|Proteomes:UP000009168}. FT DOMAIN 176..401 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 76..140 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 185..192 FT /note="G1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 241..245 FT /note="G2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 262..265 FT /note="G3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 324..327 FT /note="G4" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 363..365 FT /note="G5" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT COMPBIAS 76..89 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 98..136 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 600 AA; 68122 MW; D0840B69E3378D9E CRC64; MSRNTKMKQI AAEGIDDHYH SEDDEQFNSE DEEIIEDIIF HYKNQFTKKE VVRILDKHNW VEDDVYDALD DLKKKREQKQ NKVTEEKKQP TGGNVLVKKQ QNQNQQGKSN NDQAAQLTKQ ASSSVTAAST SGATTAPSDK SKAGEYIKIE RDVVKFNQAY PSVEYDIEAD KKEENVKNMN LVIVGHVDSG KSTLVGHLCH LKKVIDQKLA HKNEKESKNI GKESFKFAWV NDEFEAERQR GITIDIGYKV IQTKNKNITF LDAPGHKDFV PNMIQGVTQA DYALLVIEGS LQAFERGFEF GGQTKEHAFL VKQLGVQRLI VLINKMDTVN WDRNRFEYIK LELTRFLTSI GYSEDNLIFV PISAFYAENI VEKSKLPEAG WYEGKCLMEL LDTLPVPTRP VNTPLRLNIY NSFYQKNKGL IIQGKVEGGV IFEKSKALIM PQGLVVTVKE INRENVKVKY AKVGENIDVH IVHKEDCEIR SGDVLCSIEH PIPISRIFEV ELSAFELSYP ILKGAQIVMY INTAKCPGYI KKITAILDKA NGQITKKNPK CIRNNECAIV EVCIEKENCM ELFSNFKSFG RVVLREKMNT IGVGSITKIL //