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Protein

Glutamate--tRNA ligase, cytoplasmic

Gene

At5g26707

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).By similarity

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931ATPBy similarity
Binding sitei227 – 2271ATPBy similarity
Binding sitei411 – 4111GlutamateBy similarity
Binding sitei414 – 4141ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi448 – 4525ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G26710-MONOMER.
BRENDAi6.1.1.17. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase, cytoplasmicCurated (EC:6.1.1.17Curated)
Alternative name(s):
GluRSAt1 Publication
Glutamyl-tRNA synthetaseCurated
Short name:
GluRSCurated
Gene namesi
Ordered Locus Names:At5g26707Imported, At5g26710Imported
ORF Names:F21E10.12Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G26710.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 719719Glutamate--tRNA ligase, cytoplasmicPRO_0000433543Add
BLAST

Proteomic databases

PaxDbiO82462.
PRIDEiO82462.

Expressioni

Gene expression databases

GenevisibleiO82462. AT.

Interactioni

Subunit structurei

Interacts with GLN2, COL4 AND RPP13L4/ZAR1.1 Publication

Protein-protein interaction databases

DIPiDIP-48341N.
STRINGi3702.AT5G26710.1.

Structurei

3D structure databases

ProteinModelPortaliO82462.
SMRiO82462. Positions 147-707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 2193Glutamate bindingBy similarity
Regioni393 – 3975Glutamate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi220 – 23011"HIGH" regionCuratedAdd
BLAST
Motifi448 – 4525"KMSKS" regionCurated

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1147. Eukaryota.
COG0008. LUCA.
HOGENOMiHOG000259234.
InParanoidiO82462.
KOiK01885.
OMAiTEYRTNA.
PhylomeDBiO82462.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O82462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGMKLSFPP ESPPLSVIVA LSLSASPVTI DSSAAATTVP SFVFSDGRKL
60 70 80 90 100
NGATVLLRYV GRSAKKLPDF YGNNAFDSSQ IDEWVDYASV FSSGSEFENA
110 120 130 140 150
CGRVDKYLES STFLVGHSLS IADVAIWSAL AGTGQRWESL RKSKKYQSLV
160 170 180 190 200
RWFNSILDEY SEVLNKVLAT YVKKGSGKPV AAPKSKDSQQ AVKGDGQDKG
210 220 230 240 250
KPEVDLPEAE IGKVKLRFAP EPSGYLHIGH AKAALLNKYF AERYQGEVIV
260 270 280 290 300
RFDDTNPAKE SNEFVDNLVK DIGTLGIKYE KVTYTSDYFP ELMDMAEKLM
310 320 330 340 350
REGKAYVDDT PREQMQKERM DGIDSKCRNH SVEENLKLWK EMIAGSERGL
360 370 380 390 400
QCCVRGKFNM QDPNKAMRDP VYYRCNPMSH HRIGDKYKIY PTYDFACPFV
410 420 430 440 450
DSLEGITHAL RSSEYHDRNA QYFKVLEDMG LRQVQLYEFS RLNLVFTLLS
460 470 480 490 500
KRKLLWFVQT GLVDGWDDPR FPTVQGIVRR GLKIEALIQF ILEQGASKNL
510 520 530 540 550
NLMEWDKLWS INKRIIDPVC PRHTAVVAER RVLFTLTDGP DEPFVRMIPK
560 570 580 590 600
HKKFEGAGEK ATTFTKSIWL EEADASAISV GEEVTLMDWG NAIVKEITKD
610 620 630 640 650
EEGRVTALSG VLNLQGSVKT TKLKLTWLPD TNELVNLTLT EFDYLITKKK
660 670 680 690 700
LEDDDEVADF VNPNTKKETL ALGDSNMRNL KCGDVIQLER KGYFRCDVPF
710
VKSSKPIVLF SIPDGRAAK
Length:719
Mass (Da):81,065
Last modified:November 1, 1998 - v1
Checksum:i0778C243219DA24C
GO

Sequence cautioni

The sequence AAC13597.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067773 mRNA. Translation: AAC36469.1.
AF058914 Genomic DNA. Translation: AAC13597.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93573.1.
AY099592 mRNA. Translation: AAM20443.1.
BT000248 mRNA. Translation: AAN15567.1.
AK226448 mRNA. Translation: BAE98590.1.
PIRiT01200.
T52043.
RefSeqiNP_850874.1. NM_180543.2.
UniGeneiAt.49067.
At.71213.

Genome annotation databases

EnsemblPlantsiAT5G26710.1; AT5G26710.1; AT5G26710.
GeneIDi832718.
GrameneiAT5G26710.1; AT5G26710.1; AT5G26710.
KEGGiath:AT5G26710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067773 mRNA. Translation: AAC36469.1.
AF058914 Genomic DNA. Translation: AAC13597.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93573.1.
AY099592 mRNA. Translation: AAM20443.1.
BT000248 mRNA. Translation: AAN15567.1.
AK226448 mRNA. Translation: BAE98590.1.
PIRiT01200.
T52043.
RefSeqiNP_850874.1. NM_180543.2.
UniGeneiAt.49067.
At.71213.

3D structure databases

ProteinModelPortaliO82462.
SMRiO82462. Positions 147-707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48341N.
STRINGi3702.AT5G26710.1.

Proteomic databases

PaxDbiO82462.
PRIDEiO82462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G26710.1; AT5G26710.1; AT5G26710.
GeneIDi832718.
GrameneiAT5G26710.1; AT5G26710.1; AT5G26710.
KEGGiath:AT5G26710.

Organism-specific databases

TAIRiAT5G26710.

Phylogenomic databases

eggNOGiKOG1147. Eukaryota.
COG0008. LUCA.
HOGENOMiHOG000259234.
InParanoidiO82462.
KOiK01885.
OMAiTEYRTNA.
PhylomeDBiO82462.

Enzyme and pathway databases

BioCyciARA:AT5G26710-MONOMER.
BRENDAi6.1.1.17. 399.

Miscellaneous databases

PROiO82462.

Gene expression databases

GenevisibleiO82462. AT.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA for glutamyl-tRNA synthetase from Arabidopsis thaliana."
    Day I.S., Golovkin M., Reddy A.S.
    Biochim. Biophys. Acta 1399:219-224(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo development in Arabidopsis."
    Berg M., Rogers R., Muralla R., Meinke D.
    Plant J. 44:866-878(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana."
    Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D., Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.
    Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "AtPIN: Arabidopsis thaliana protein interaction network."
    Brandao M.M., Dantas L.L., Silva-Filho M.C.
    BMC Bioinformatics 10:454-454(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLN2; COL4 AND RPP13L4/ZAR1.

Entry informationi

Entry nameiSYEC_ARATH
AccessioniPrimary (citable) accession number: O82462
Secondary accession number(s): O65253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.