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Database: UniProt
Entry: B6CNA0_9NEOP
LinkDB: B6CNA0_9NEOP
Original site: B6CNA0_9NEOP 
ID   B6CNA0_9NEOP            Unreviewed;       351 AA.
AC   B6CNA0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:ACD75970.1};
DE   Flags: Fragment;
GN   Name=EF1a {ECO:0000313|EMBL:ACD75970.1};
OS   Dolichopsyllus stylosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Siphonaptera; Leptopsyllidae; Dolichopsyllus.
OX   NCBI_TaxID=507045 {ECO:0000313|EMBL:ACD75970.1};
RN   [1] {ECO:0000313|EMBL:ACD75970.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F113 {ECO:0000313|EMBL:ACD75970.1};
RA   Whiting M.F., Whiting A.S., Hastriter M.W., Dittmar K.;
RT   "A molecular phylogeny of fleas (Insecta: Siphonaptera): origins and host
RT   associations.";
RL   Cladistics 24:677-707(2008).
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; EU336295; ACD75970.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6CNA0; -.
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; 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:SF236; ELONGATION FACTOR 1-ALPHA 1; 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:ACD75970.1};
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:ACD75970.1}.
FT   DOMAIN          1..166
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD75970.1"
FT   NON_TER         351
FT                   /evidence="ECO:0000313|EMBL:ACD75970.1"
SQ   SEQUENCE   351 AA;  38123 MW;  B9E8A55CD889B8ED CRC64;
     LWKFETAKYY VTIIDAPGHR DFIKNMITGT SQADCAVLIV AAGVGEFEAG ISKNGQTREH
     ALLAFTLGVK QLIVGVNKMD STEPPYSENR FEEIKKEVSS YIKKIGYNPA AVAFVPISGW
     HGDNMLEVSS KMGWFKGWNI ERKEGKADGK CLIEALDAIL PPARPTDKPL RLPLQDVYKI
     GGIGTVPVGR VETGVLKPGT VVVFAPANLT TEVKSVEMHH EALQEAVPGD NVGFNVKNVS
     VKELRRGYVA GDSKASPPRG AADFTAQVIV LNHPGQISNG YTPVLDCHTA HIACKFAEIK
     EKVDRRTGKS TEENPKAIKS GDAAIVNLVP SKPMCVESFQ EFPPLGRFAV R
//
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