ID B4UVH3_9HYME Unreviewed; 365 AA.
AC B4UVH3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:ABK00296.1};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:ABK00296.1};
OS Xenochilicola mamigna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Colletidae; Xeromelissinae; Xenochilicola.
OX NCBI_TaxID=395831 {ECO:0000313|EMBL:ABK00296.1};
RN [1] {ECO:0000313|EMBL:ABK00296.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida E.A.B., Magnacca K.N., Danforth B.N.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABK00296.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18992829; DOI=10.1016/j.ympev.2008.09.028;
RA Almeida E.A., Danforth B.N.;
RT "Phylogeny of colletid bees (Hymenoptera: Colletidae) inferred from four
RT nuclear genes.";
RL Mol. Phylogenet. Evol. 50:290-309(2009).
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; DQ884660; ABK00296.1; -; Genomic_DNA.
DR AlphaFoldDB; B4UVH3; -.
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:ABK00296.1};
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:ABK00296.1}.
FT DOMAIN 1..180
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABK00296.1"
FT NON_TER 365
FT /evidence="ECO:0000313|EMBL:ABK00296.1"
SQ SEQUENCE 365 AA; 39758 MW; 0FD20488CDB67B78 CRC64;
LKAERERGIT IDIALWKFET SKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE
FEAGISKNGQ TREHALLAFT LGVKQLIVGV NKMDSTEPPY SEARFEEIKK EVSSYIKKIG
YNPAAVAFVP ISGWHGDNML EVSSKMPWFK GWTVERKEGK AEGKCLIEAL DAILPPTRPT
DKALRLPLQD VYKIGGIGTV PVGRVETGVL KPGMIVTFAP TALTTEVKSV EMHHEALQEA
VPGDNVGFNV KNVSVKDLRR GYVAGDSKNN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD
CHTAHIACKF AEIKEKCDRR TGKTTEENPK AIKSGDAAIV VLIPSKPMCV EAFQEFPPLG
RFAVR
//
