EF1A1_ARATH
ID EF1A1_ARATH Reviewed; 449 AA.
AC P0DH99; P13905;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha 1;
DE AltName: Full=eEF-1A1;
GN Name=A1; OrderedLocusNames=At1g07940; ORFNames=T6D22.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2615757; DOI=10.1007/bf00261164;
RA Axelos M., Bardet C., Liboz T., Le van Thai A., Curie C., Lescure B.;
RT "The gene family encoding the Arabidopsis thaliana translation elongation
RT factor EF-1 alpha: molecular cloning, characterization and expression.";
RL Mol. Gen. Genet. 219:106-112(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-438 AND LYS-441, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19292762; DOI=10.1111/j.1365-313x.2009.03862.x;
RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.;
RT "Tandem affinity purification and mass spectrometric analysis of
RT ubiquitylated proteins in Arabidopsis.";
RL Plant J. 59:344-358(2009).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: There are four genes for EF-1-alpha in Arabidopsis
CC thaliana. The sequence of genes 1, 2, and 3 are identical.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; X16430; CAA34453.1; -; Genomic_DNA.
DR EMBL; U63815; AAB07882.1; -; Genomic_DNA.
DR EMBL; AC026875; AAF79847.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28215.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28216.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58322.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58323.1; -; Genomic_DNA.
DR EMBL; AY039583; AAK62638.1; -; mRNA.
DR EMBL; BT000595; AAN18164.1; -; mRNA.
DR PIR; S06724; S06724.
DR RefSeq; NP_001030993.1; NM_001035916.3.
DR RefSeq; NP_001119464.1; NM_001125992.1.
DR RefSeq; NP_001318848.1; NM_001345413.1.
DR RefSeq; NP_001320767.1; NM_001331743.1.
DR RefSeq; NP_001320768.1; NM_001331742.1.
DR RefSeq; NP_200847.1; NM_125432.4.
DR RefSeq; NP_563799.1; NM_100666.4.
DR RefSeq; NP_563800.1; NM_100667.4.
DR RefSeq; NP_563801.1; NM_100668.3.
DR AlphaFoldDB; P0DH99; -.
DR SMR; P0DH99; -.
DR BioGRID; 21405; 3.
DR BioGRID; 22548; 10.
DR BioGRID; 22549; 3.
DR BioGRID; 22550; 2.
DR STRING; 3702.AT1G07920.1; -.
DR iPTMnet; P0DH99; -.
DR MetOSite; P0DH99; -.
DR PaxDb; P0DH99; -.
DR PRIDE; P0DH99; -.
DR EnsemblPlants; AT1G07920.1; AT1G07920.1; AT1G07920.
DR EnsemblPlants; AT1G07930.1; AT1G07930.1; AT1G07930.
DR EnsemblPlants; AT1G07940.1; AT1G07940.1; AT1G07940.
DR EnsemblPlants; AT1G07940.2; AT1G07940.2; AT1G07940.
DR EnsemblPlants; AT1G07940.3; AT1G07940.3; AT1G07940.
DR EnsemblPlants; AT1G07940.4; AT1G07940.4; AT1G07940.
DR EnsemblPlants; AT5G60390.1; AT5G60390.1; AT5G60390.
DR EnsemblPlants; AT5G60390.2; AT5G60390.2; AT5G60390.
DR EnsemblPlants; AT5G60390.3; AT5G60390.3; AT5G60390.
DR GeneID; 836161; -.
DR GeneID; 837307; -.
DR GeneID; 837308; -.
DR GeneID; 837309; -.
DR Gramene; AT1G07920.1; AT1G07920.1; AT1G07920.
DR Gramene; AT1G07930.1; AT1G07930.1; AT1G07930.
DR Gramene; AT1G07940.1; AT1G07940.1; AT1G07940.
DR Gramene; AT1G07940.2; AT1G07940.2; AT1G07940.
DR Gramene; AT1G07940.3; AT1G07940.3; AT1G07940.
DR Gramene; AT1G07940.4; AT1G07940.4; AT1G07940.
DR Gramene; AT5G60390.1; AT5G60390.1; AT5G60390.
DR Gramene; AT5G60390.2; AT5G60390.2; AT5G60390.
DR Gramene; AT5G60390.3; AT5G60390.3; AT5G60390.
DR KEGG; ath:AT1G07920; -.
DR KEGG; ath:AT1G07930; -.
DR KEGG; ath:AT1G07940; -.
DR KEGG; ath:AT5G60390; -.
DR Araport; AT1G07940; -.
DR TAIR; locus:2205115; AT1G07940.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P0DH99; -.
DR OMA; DIMVRKL; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P0DH99; -.
DR BRENDA; 3.6.5.3; 399.
DR PRO; PR:P0DH99; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0DH99; baseline and differential.
DR Genevisible; P0DH99; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; GTP-binding; Isopeptide bond; Methylation;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090932"
FT DOMAIN 5..230
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 261
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 306
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 396
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
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
