ID C6YYJ9_9HYME Unreviewed; 360 AA.
AC C6YYJ9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Elongation factor 1 alpha {ECO:0000313|EMBL:ABW75552.1};
DE Flags: Fragment;
OS Panurgus banksianus proximus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Andrenidae; Panurginae; Panurgini; Panurgus.
OX NCBI_TaxID=465458 {ECO:0000313|EMBL:ABW75552.1};
RN [1] {ECO:0000313|EMBL:ABW75552.1}
RP NUCLEOTIDE SEQUENCE.
RA Patiny S.M.L., Michez D., Ascher J.S., Larkin L.L., Danforth B.N.;
RT "Phylogeny of Panurginae.";
RL Submitted (MAY-2007) 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|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; EF599197; ABW75552.1; -; Genomic_DNA.
DR AlphaFoldDB; C6YYJ9; -.
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:ABW75552.1};
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:ABW75552.1}.
FT DOMAIN 1..179
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABW75552.1"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:ABW75552.1"
SQ SEQUENCE 360 AA; 39205 MW; 55F5A0BFCCA828E2 CRC64;
KAERERGITI DIALWKFETS RYYVTIIDAP GHRDFIKNMI TGTSQADCAV LIVAAGTGEF
EAGISKNGQT REHALLAFTL GVKQLIVGVN KMDSTEPPYS ENRFEEIKKE VSSYIKKIGY
NPAAVAFVPI SGWNGDNMLE VSAKMPWFKG WMVDRKEGKA EGKTLIEALD AILPPTRPTD
KALRLPLQDV YKIGGIGTVP VGRVETGVLK PGMVVTFAPA GLTTEVKSVE MHHEALQEAV
PGDNVGFNVK NVSVKELRRG YVAGDSKNNP PRGAADFTAQ VIVLNHPGQI SNGYTPVLDC
HTAHIACKFA EIKEKCDRRT GKTTEENPKS IKSGDAAIVT LVPSKPMCVE AFQEFPPLGR
//