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Database: UniProt
Entry: A0A0T6B4E2_9SCAR
LinkDB: A0A0T6B4E2_9SCAR
Original site: A0A0T6B4E2_9SCAR 
ID   A0A0T6B4E2_9SCAR        Unreviewed;       457 AA.
AC   A0A0T6B4E2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325};
DE   Flags: Fragment;
GN   ORFNames=AMK59_3591 {ECO:0000313|EMBL:KRT82232.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT82232.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT82232.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT82232.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT82232.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) 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   -!- 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:KRT82232.1}.
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DR   EMBL; LJIG01009862; KRT82232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6B4E2; -.
DR   OrthoDB; 167272at2759; -.
DR   Proteomes; UP000051574; 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; cd03706; mtEFTU_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; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT   DOMAIN          56..251
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         457
FT                   /evidence="ECO:0000313|EMBL:KRT82232.1"
SQ   SEQUENCE   457 AA;  50942 MW;  D31CF46E7AC6A7BF CRC64;
     MAMFISARTL VPVLRKTLFN CESVRCYHQK KIVQYIIPFT QQKRYYAEKK VFDRNKPHCN
     VGTIGHVDHG KTTLTAAITK VLSDKKLAAA KKYDDIDNAP EEKARGITIN VAHIEYQTEN
     RHYGHTDCPG HADYIKNMIT GTAQMDGAIL VVAATDGVMP QTREHLLLAK QIGVKYVVIF
     INKVDAADKE MAELVEMEIR ELMTEMGFDG ENVPVITGSA LCALEGTKSE IGTEAILKLL
     DEVDKYIPTP VRELDKPFLL PVEHVYAIPG RGTVVTGRLE RGVLKKGADC EFVGFNKVLK
     STVTGVEMFH QILEEAQAGD QLGALVRGLK RDDIKRGMIM CKPGTMKAHD QIEAQAYILS
     KEEGGRSKPF TSFIQLQMFS KTWDCAVQVT IPDKEMVMPG EDSKLLLKMI RPMVLEEGQR
     FTLRDGNLTL GTGVVTKILS NMNENERVAI TEGKKAR
//
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