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Database: UniProt
Entry: J3JXE8_DENPD
LinkDB: J3JXE8_DENPD
Original site: J3JXE8_DENPD 
ID   J3JXE8_DENPD            Unreviewed;       461 AA.
AC   J3JXE8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   ORFNames=D910_10484 {ECO:0000313|EMBL:ERL93187.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:AEE62879.1};
RN   [1] {ECO:0000313|EMBL:AEE62879.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Larvae {ECO:0000313|EMBL:AEE62879.1};
RX   PubMed=22516182; DOI=10.1016/j.ibmb.2012.03.010;
RA   Keeling C.I., Henderson H., Li M., Yuen M., Clark E.L., Fraser J.D.,
RA   Huber D.P., Liao N.Y., Roderick Docking T., Birol I., Chan S.K.,
RA   Taylor G.A., Palmquist D., Jones S.J., Bohlmann J.;
RT   "Transcriptome and full-length cDNA resources for the mountain pine beetle,
RT   Dendroctonus ponderosae Hopkins, a major insect pest of pine forests.";
RL   Insect Biochem. Mol. Biol. 42:525-536(2012).
RN   [2] {ECO:0000313|EMBL:ERL93187.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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, ECO:0000256|RuleBase:RU000325}.
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       ECO:0000256|RuleBase:RU000325}.
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DR   EMBL; BT127917; AEE62879.1; -; mRNA.
DR   EMBL; KB632348; ERL93187.1; -; Genomic_DNA.
DR   RefSeq; XP_019759532.1; XM_019903973.1.
DR   AlphaFoldDB; J3JXE8; -.
DR   STRING; 77166.J3JXE8; -.
DR   HOGENOM; CLU_240970_0_0_1; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000030742; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Elongation factor {ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT   DOMAIN          5..242
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   461 AA;  50580 MW;  0C9A3000B103389E CRC64;
     MGREKTHINI VVIGHVDSGK STSTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGT
     GEFEAGISKN GQTREHALLA VTLGVKQLIV GVNKMDSTEP PYSEVRFEEI KHEVCSYIKK
     IGFNPNGVPF VPISGWHGDN MLEPSEKMPW FKGWSIERKE GKADGKTLIE ALDAILPPSR
     PTEKALRLPL QDVYKIGGIG TVPVGRVETG ILKPGMVVTF APVGLTTEVK SVEMHHEALQ
     EAVPGDNVGF NVKNVSVKEL RRGFVAGDSK NNPPRGAADF TAQVIVLNHP GQISNGYTPV
     LDCHTAHIAC KFAEIKEKCD RRSGKVTEEN PKFIKTGDAA FVNLVPSKPM CVESFQEFPP
     LGRFAVRDMR QTVAVGVIKQ VNFKDTAGKV TKAAEKAQKK K
//
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