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Database: UniProt
Entry: Q964Y0_9HYME
LinkDB: Q964Y0_9HYME
Original site: Q964Y0_9HYME 
ID   Q964Y0_9HYME            Unreviewed;       361 AA.
AC   Q964Y0;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:AAK66617.1};
DE   Flags: Fragment;
OS   Lasioglossum truncatum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Halictidae; Halictinae; Halictini; Lasioglossum; Evylaeus.
OX   NCBI_TaxID=88522 {ECO:0000313|EMBL:AAK66617.1};
RN   [1] {ECO:0000313|EMBL:AAK66617.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12116931; DOI=10.1080/10635150151125914;
RA   Danforth B.N., Ji S.;
RT   "Australian Lasioglossum + Homalictus form a monophyletic group: resolving
RT   the "Australian enigma".";
RL   Syst. Biol. 50:268-283(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; AF264836; AAK66617.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q964Y0; -.
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; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; 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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:AAK66617.1};
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:AAK66617.1}.
FT   DOMAIN          1..177
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK66617.1"
FT   NON_TER         361
FT                   /evidence="ECO:0000313|EMBL:AAK66617.1"
SQ   SEQUENCE   361 AA;  39215 MW;  7C3A0FD5E09B8FF7 CRC64;
     ERERGITIDI ALWKFETSKY YVTIIDAPGH RDFIKNMITG TSQADCAVLI VAAGTGEFEA
     GISKNGQTRE HALLAFTLGV KQLIVGVNKM DSTEPPYSEA RFEEIKKEVS SYIKKIGYNP
     AAVAFVPISG WHGDNMLEAS SKMPWFKGWA VERKEGKAEG KCLIEALDAI LPPSRPTDKA
     LRLPLQDVYK IGGIGTVPVG RVETGLLKPG MVVTFAPAGL TTEVKSVEMH HEALTEAVPG
     DNVGFNVKNV SVKELRRGYV AGDSKNNPPK GAADFTAQVI VLNHPGQISN GYTPVLDCHT
     AHIACKFHKI IEKCDRRTGK TTEMEPKAIK SGDAAIVTLV PSKPMCVEAF QEFPPLGRFA
     V
//
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