ID Q7RBK9_PLAYO Unreviewed; 477 AA. AC Q7RBK9; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325}; GN ORFNames=PY06134 {ECO:0000313|EMBL:EAA18291.1}; OS Plasmodium yoelii yoelii. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA18291.1, ECO:0000313|Proteomes:UP000008553}; RN [1] {ECO:0000313|EMBL:EAA18291.1, ECO:0000313|Proteomes:UP000008553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17XNL {ECO:0000313|EMBL:EAA18291.1, RC ECO:0000313|Proteomes:UP000008553}; RX PubMed=12368865; DOI=10.1038/nature01099; RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C., RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M., RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E., RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M., RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E., RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., RA Carucci D.J.; RT "Genome sequence and comparative analysis of the model rodent malaria RT parasite Plasmodium yoelii yoelii."; RL Nature 419:512-519(2002). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAA18291.1}. 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; AABL01002045; EAA18291.1; -; Genomic_DNA. DR AlphaFoldDB; Q7RBK9; -. DR STRING; 73239.Q7RBK9; -. DR PaxDb; 73239-Q7RBK9; -. DR EnsemblProtists; EAA18291; EAA18291; EAA18291. DR VEuPathDB; PlasmoDB:Py17XNL_001303353; -. DR InParanoid; Q7RBK9; -. DR OMA; FHNNYRP; -. DR Proteomes; UP000008553; Unassembled WGS sequence. 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 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 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:UP000008553}. FT DOMAIN 91..287 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" SQ SEQUENCE 477 AA; 53768 MW; 6D6155040BB83E74 CRC64; MMKTRSRILN SLTKNGVGNQ LMGFENYINN CNNVMNKRNI NSLIQINENE GKGINIKYYI KKNVNLYNQN KINIFKINKK NFAIGIFERK KPHMNIGTIG HVDHGKTTLT AAITKVCSKY DRGTFKSYED IDKTPEEQKR GITINATHVE YETEKRHYSH IDCPGHLDYI KNMITGTSQM DGSILVVSAY DGLMPQTKEH VLLSRQIGIN KIIVYLNKID MCEDQELVDL VELEVRELLS FHKYDGDNIP FIKGSALKAL NDDPSEYGVP SILKLLDACD NYIDEPKRKI DLPFLMSIDD VLQISGKGTV ATGRVEQGTI KINESVDILG IKEKSIKTVI TGIEMFRKTL DTAQAGDQIG VMLKNVKKND ISRGMVVTKI PNMKTYKKFE SDIYVLKNEE GGRKNPFSSY YRPQVYIRTA DVNCAVILNE DTQIANPGDN IKCTIELMYP LAISSGLRFS LREGGKTVAS GIITKVL //