UniProt: D7KHX1

Database: UniProt
Entry: D7KHX1_ARALL

LinkDB:  D7KHX1_ARALL 
Original site:  D7KHX1_ARALL

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Ontology (3)   
   GO (3)   
Gene (4)   
   KEGG GENES (2)   
   NCBI-Gene (2)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (25)   

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ID   D7KHX1_ARALL            Unreviewed;       449 AA.
AC   D7KHX1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN   ORFNames=ARALYDRAFT_470837 {ECO:0000313|EMBL:EFH65933.1},
GN   ARALYDRAFT_496177 {ECO:0000313|EMBL:EFH40943.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|EMBL:EFH65933.1}
RP   NUCLEOTIDE SEQUENCE.
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA   Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA   van de Peer Y., Weigel D., Grigoriev I.V.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFH65933.1}
RP   NUCLEOTIDE SEQUENCE.
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Bakker E., Bergelson J., Cheng J.Fang., Clark R.M., Fawcett J., Gaut B.,
RA   Grigoriev I., Gundlach H., Guo Y., Haberer G., Hollister J., Hu T.T.,
RA   Mayer K.F.X., Nasrallah J., Nordborg M., Otillar R., Pattyn P., Schmutz J.,
RA   Spannagl M., van de Peer Y., Wang X., Weigel D., Yang L.;
RT   "The basis of rapid genome size change in Arabidopsis.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EFH40943.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bakker E., Bergelson J., Cheng J.F., Clark R.M., Fawcett J., Gaut B.,
RA   Grigoriev I., Gundlach H., Guo Y., Haberer G., Hollister J., Hu T.T.,
RA   Mayer K.F.X., Nasrallah J., Nordborg M., Otillar R., Pattyn P., Schmutz J.,
RA   Spannagl M., van de Peer Y., Wang X., Weigel D., Yang L.;
RT   "The basis of rapid genome size change in Arabidopsis.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   -!- 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; GL348720; EFH40943.1; -; Genomic_DNA.
DR   EMBL; GL348713; EFH65933.1; -; Genomic_DNA.
DR   RefSeq; XP_002864684.1; XM_002864638.1.
DR   RefSeq; XP_002889674.1; XM_002889628.1.
DR   AlphaFoldDB; D7KHX1; -.
DR   SMR; D7KHX1; -.
DR   STRING; 81972.D7KHX1; -.
DR   EnsemblPlants; fgenesh2_kg.1__791__AT1G07930.1; fgenesh2_kg.1__791__AT1G07930.1; fgenesh2_kg.1__791__AT1G07930.1.
DR   EnsemblPlants; fgenesh2_kg.8__1993__AT5G60390.1; fgenesh2_kg.8__1993__AT5G60390.1; fgenesh2_kg.8__1993__AT5G60390.1.
DR   GeneID; 9300760; -.
DR   GeneID; 9325738; -.
DR   Gramene; fgenesh2_kg.1__791__AT1G07930.1; fgenesh2_kg.1__791__AT1G07930.1; fgenesh2_kg.1__791__AT1G07930.1.
DR   Gramene; fgenesh2_kg.8__1993__AT5G60390.1; fgenesh2_kg.8__1993__AT5G60390.1; fgenesh2_kg.8__1993__AT5G60390.1.
DR   KEGG; aly:9300760; -.
DR   KEGG; aly:9325738; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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:SF301; ELONGATION FACTOR 1-ALPHA 1-RELATED; 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   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:EFH65933.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:EFH65933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          5..230
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   449 AA;  49502 MW;  12FFA6C537DFCEE9 CRC64;
     MGKEKFHINI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
     DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
     GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKARYDEI IKEVSSYLKK
     VGYNPDKIPF VPISGFEGDN MIERSTNLDW YKGPTLLEAL DQINEPKRPS DKPLRLPLQD
     VYKIGGIGTV PVGRVETGMI KPGMVVTFAP TGLTTEVKSV EMHHESLLEA LPGDNVGFNV
     KNVAVKDLKR GYVASNSKDD PAKGAANFTS QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF
     SEILTKIDRR SGKEIEKEPK FLKNGDAGMV KMTPTKPMVV ETFSEYPPLG RFAVRDMRQT
     VAVGVIKSVD KKDPTGAKVT KAAVKKGAK
//

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