ID A0A288Z8C7_9STRA Unreviewed; 337 AA. AC A0A288Z8C7; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 29-SEP-2021, entry version 11. DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325}; DE Flags: Fragment; OS Phytophthora macrochlamydospora. OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae; OC Phytophthora. OX NCBI_TaxID=67591 {ECO:0000313|EMBL:ASU42833.1}; RN [1] {ECO:0000313|EMBL:ASU42833.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=33D5 {ECO:0000313|EMBL:ASU42833.1}; RA Yang X., Tyler B.M., Hong C.; RT "An expanded multi-locus phylogeny for the genus Phytophthora with new RT insights into its evolutionary history."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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|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; KX252518; ASU42833.1; -; Genomic_DNA. 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 Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. 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; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00483; EF-1_alpha; 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|RuleBase:RU000325, KW ECO:0000313|EMBL:ASU42833.1}; GTP-binding {ECO:0000256|RuleBase:RU000325}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000325}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 1..170 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ASU42833.1" FT NON_TER 337 FT /evidence="ECO:0000313|EMBL:ASU42833.1" SQ SEQUENCE 337 AA; 37081 MW; 4674E6E9639856B0 CRC64; DNLKAERERG ITIDIALWKF ESPKYFFTVI DAPGHRDFIK NMITGTSQAD CAILVVASGV GEFEAGISKE GQTREHALLA FTLGVKQMIV AINKMDDSSV MYSQSRYEEI KNEVTTYLKK VGYKPAKIPF VPISGWEGDN MIERSTNMPW YKGPFLLEAL DNLNAPKRPV DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVATFGP VGLSTEVKSV EMHHESLPEA VPGDNVGFNV KNVSVKELRR GFVASDSKND PAKGTQDFTA QVIVLNHPGQ IGNGYSPVLD CHTAHVACKF KEITEKMDRR SGKVLETAPK FVKTGDACMV IRSRRSP //