ID Q9Y0U2_9MUSC Unreviewed; 354 AA.
AC Q9Y0U2;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:AAD41506.1};
DE Flags: Fragment;
OS Therevidae gen. sp. 6.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC Therevidae.
OX NCBI_TaxID=97364 {ECO:0000313|EMBL:AAD41506.1};
RN [1] {ECO:0000313|EMBL:AAD41506.1}
RP NUCLEOTIDE SEQUENCE.
RA Winterton S.L., Yang L.L., Wiegmann B.M., Yeates D.K.;
RT "Phylogenetic revision of Agapophytinae subf.n. (Diptera: Therevidae) based
RT on molecular and morphological evidence.";
RL Syst. Entomol. 26:173-211(2001).
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}.
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}.
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DR EMBL; AF150976; AAD41506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y0U2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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:SF236; ELONGATION FACTOR 1-ALPHA 1; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:AAD41506.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000313|EMBL:AAD41506.1}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAD41506.1"
FT NON_TER 354
FT /evidence="ECO:0000313|EMBL:AAD41506.1"
SQ SEQUENCE 354 AA; 38361 MW; 91C0BDFABA760F52 CRC64;
RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ ADCAVLIVAA GTGEFEAGIS
SNGQTREHAL LAFTLGVKQL IVGVNKMDSS EPPYSESRYE EIKKEVSSYI KRVGYNPAAV
AFVPISGWHG DNMLEPSSNM PWFKGWKVER KEGNAEGKTL IDALDAILPP SRPTDKPLRL
PLQDVYKIGG IGTVPVGRVE TGVLKPGTVV VFAPANITTE VKSVEMHHEA LSEAVPGDNV
GFNVKNVSVK ELRRGYVAGD SKNNPPKGAA DFTAQVIVLN HPGQISNGYT PVLDCHTAHI
ACKFAEIKQK VDRRTGKATE ENPKSIKSGD AAIVNLIPSK PLCVESFQEF PPLV
//
