ID B4UUY6_9HYME Unreviewed; 360 AA.
AC B4UUY6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:ABJ16087.1};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:ABJ16087.1};
OS Chilicola sp. 6 EABA-2006.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Colletidae; Xeromelissinae; Chilicola.
OX NCBI_TaxID=395715 {ECO:0000313|EMBL:ABJ16087.1};
RN [1] {ECO:0000313|EMBL:ABJ16087.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida E.A.B., Danforth B.N.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABJ16087.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ872753; ABJ16087.1; -; Genomic_DNA.
DR AlphaFoldDB; B4UUY6; -.
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:ABJ16087.1};
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:ABJ16087.1}.
FT DOMAIN 1..180
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABJ16087.1"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:ABJ16087.1"
SQ SEQUENCE 360 AA; 39098 MW; A8808CF2B8B21C05 CRC64;
LKAERERGIT IDIALWKFET SKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE
FEAGISKNGQ TREHALLAFT LGVKQLIVGV NKMDSTEPPY SEARFEEIKK EVSSYIKKIG
YNPAAVAFVP ISGWHGDNML EVSSKMPWFK GWAVERKEGK AEGKCLIEAL DAILPPTRPT
DKALRLPLQD VYKIGGIGTV PVGRVETGVL KPGMIVTFAP TALTTEVKSV EMHHEALQEA
VPGDNVGFNV KNVSVKDLRR GYVAGDSKNN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD
CHTAHIACKF AEIKEKCDRR TGKTTEENPK AIKSGDAAIV VLIPSKPMCV EAFQEFPPLG
//
