ID B6C7N3_9HYME Unreviewed; 357 AA.
AC B6C7N3;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Elongation factor 1 alpha {ECO:0000313|EMBL:ABU89934.1};
DE Flags: Fragment;
OS Rediviva saetigera.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Melittinae; Rediviva.
OX NCBI_TaxID=326117 {ECO:0000313|EMBL:ABU89934.1};
RN [1] {ECO:0000313|EMBL:ABU89934.1}
RP NUCLEOTIDE SEQUENCE.
RA Michez D., Patiny S., Danforth B.N.;
RT "Phylogeny of the bee family Melittidae (Hymenoptera: Anthophila) based on
RT combined molecular and morphological data.";
RL Syst. Entomol. 34:574-597(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; EF594322; ABU89934.1; -; Genomic_DNA.
DR AlphaFoldDB; B6C7N3; -.
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:ABU89934.1};
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:ABU89934.1}.
FT DOMAIN 1..177
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU89934.1"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:ABU89934.1"
SQ SEQUENCE 357 AA; 38873 MW; BC7A2DB4BC3EB681 CRC64;
ERERGITIDI ALWKFETSKY YVTIIDAPGH RDFIKNMITG TSQADCAVLI VAAGTGEFEA
GISKNGQTRE HALLAFTLGV KQLIVGVNKM DSTEPPYSEP RFEEIKKEVS SYIKKIGYNP
AAVAFVPISG WHGDNMLEAS SKMPWFKGWN VERKEGKAEG KCLIEALDAI LPPTRPTDKA
LRLPLQDVYK IAGIGTVPVG RVETGLLKPG MVVTFAPAGL TTEVKSVEMH HEALQEAVPG
DNVGFNVKNV SVKELRRGYV AGDSKNNPPK GAADFTAQVI VLNHPGQISN GYTPVLDCHT
AHIACKFFEI KEKCDRRTGK TTEENPKAIK SGDAAIVVLV PSKPMCVEAF QEFPPLG
//
