ID D6BUU4_9HYME Unreviewed; 358 AA.
AC D6BUU4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1a-F1 {ECO:0000313|EMBL:ADD13373.1};
OS Nebothriomyrmex majeri.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dolichoderinae; Nebothriomyrmex.
OX NCBI_TaxID=613204 {ECO:0000313|EMBL:ADD13373.1};
RN [1] {ECO:0000313|EMBL:ADD13373.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20525640; DOI=10.1093/sysbio/syq012;
RA Ward P.S., Brady S.G., Fisher B.L., Schultz T.R.;
RT "Phylogeny and biogeography of dolichoderine ants: effects of data
RT partitioning and relict taxa on historical inference.";
RL Syst. Biol. 59:342-362(2010).
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 -!- 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 ECO:0000256|RuleBase:RU000325}.
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DR EMBL; FJ940070; ADD13373.1; -; Genomic_DNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_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; 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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 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; 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|RuleBase:RU000325,
KW ECO:0000313|EMBL:ADD13373.1};
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|RuleBase:RU000325,
KW ECO:0000313|EMBL:ADD13373.1}.
FT DOMAIN 1..192
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD13373.1"
FT NON_TER 358
FT /evidence="ECO:0000313|EMBL:ADD13373.1"
SQ SEQUENCE 358 AA; 39204 MW; 856B4D87CF4A619F CRC64;
KGSFKYAWVL DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD
CAVLIVAAGI GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDMTDP PYSETRFEEI
KKEVSSYIKK IGYNTAXVAF VPISGWHGDN MLESSPKTPW YKGWKVERKD GNADGKTLIE
ALDVILPPSR PTDKALRLPL QDVYKIGGIG TVPVGRVETG ILKPGMLVTF APAALTTEVK
SVEMHHEALT EALPGDNVGF NVKNISVKEL RRGYVAGDSK NQPPRGAADF TAQVIVLNHP
GQISNGYTPV LDCHTAHIAC KFAEIKEKCD RRTGKTTEEN PKSIKSGDAA IVMLQPTK
//
