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Protein

Leucine--tRNA ligase, chloroplastic/mitochondrial

Gene

EMB2369

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

Functioni

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.By similarity

Catalytic activityi

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei733 – 7331ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in seed dormancy Source: TAIR
  • leucyl-tRNA aminoacylation Source: GO_Central
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:AT4G04350-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine--tRNA ligase, chloroplastic/mitochondrialCurated (EC:6.1.1.4Curated)
Alternative name(s):
Leucyl-tRNA synthetaseCurated
Short name:
LeuRSCurated
Protein EMBRYO DEFECTIVE 23691 Publication
Gene namesi
Name:EMB23691 Publication
Ordered Locus Names:At4g04350Imported
ORF Names:T19B17.7Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G04350.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

Pathology & Biotechi

Disruption phenotypei

Embryo defective. Developmental arrest of the embryo at the globular stage.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 973Leucine--tRNA ligase, chloroplastic/mitochondrialCuratedPRO_0000433548
Transit peptidei1 – ?Chloroplast and mitochondrionCurated

Proteomic databases

PaxDbiQ9XEA0.
PRIDEiQ9XEA0.

Expressioni

Gene expression databases

GenevisibleiQ9XEA0. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G04350.1.

Structurei

3D structure databases

ProteinModelPortaliQ9XEA0.
SMRiQ9XEA0. Positions 84-963.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi126 – 13510"HIGH" regionCurated
Motifi730 – 7345"KMSKS" regionCurated

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0435. Eukaryota.
COG0495. LUCA.
HOGENOMiHOG000200748.
InParanoidiQ9XEA0.
KOiK01869.
OMAiLHMGHAE.
PhylomeDBiQ9XEA0.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 5 hits.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 2 hits.
PF13603. tRNA-synt_1_2. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XEA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSHHQILQI RSDPFVLSHC CRHTRLTSSL TLQSPLKQPF SCLPFRWRRS
60 70 80 90 100
YRGGVRSSTT ETHGSKKEAL VSETATTSIE LKRVYPFHEI EPKWQRYWED
110 120 130 140 150
NRIFRTPDDV DTSKPKFYVL DMFPYPSGAG LHVGHPLGYT ATDILARLRR
160 170 180 190 200
MQGYNVLHPM GWDAFGLPAE QYAIETGTHP KTTTLKNIDR FRLQLKSLGF
210 220 230 240 250
SYDWDRELST TEPDYYKWTQ WIFLQLYKKG LAYQAEVPVN WCPALGTVLA
260 270 280 290 300
NEEVVDGVSE RGGHPVIRKP MRQWMLKITA YADRLLEDLD ELEWPESIKE
310 320 330 340 350
MQRNWIGRSE GAELNFSILD GEGRETDKEI TVYTTRPDTL FGATYMVVAP
360 370 380 390 400
EHQLLSYFVT AEQKQQVEEY KDFASRKSDL ERTELQKDKT GVFTGCYAKN
410 420 430 440 450
PANGDAIPIW VADYVLASYG TGAIMAVPAH DTRDNEFALK YNIPIKWVVR
460 470 480 490 500
NEANSSDDAK QVYPGLGIIE NSSTLETGLD INQLSSKEAA LKVIEWAERT
510 520 530 540 550
GNGKKKVNYK LRDWLFARQR YWGEPIPILI LDESGETIAI SESELPLTLP
560 570 580 590 600
ELNDFTPTGT GEPPLSKAVS WVNTVDPSTG KPAKRETSTM PQWAGSCWYY
610 620 630 640 650
LRFMDPKNPE ALVDKEKEKY WSPVDVYVGG AEHAVLHLLY SRFWHKVLYD
660 670 680 690 700
IGVVSTKEPF KCVINQGIIL GEVQYTAWKD QEGNYVSADT EERLNEHQQV
710 720 730 740 750
TIPEEKVIKS GDHFVLKEDP SIRLIPRVYK MSKSRGNVVN PDDVVLEYGA
760 770 780 790 800
DSLRLYEMFM GPFRDSKTWN TSGIEGVHRF LARTWRLVIG LPQSDGSFKD
810 820 830 840 850
GTLVTDDEPT LEQLRTLHKC IAKVTEEIES TRFNTGISGM MEFVNAAYKW
860 870 880 890 900
NNQPRGIIEP FVLLLSPYAP HMAEELWSRL GHPNSLAYES FPKANPDYLK
910 920 930 940 950
NTTIVLPVQI NGKTRGTIEV EEGCSEDDAF VLASQDDKLR KYLDGQSIKK
960 970
RIYVPGKILN VILDRTNVKV TTK
Length:973
Mass (Da):111,033
Last modified:November 1, 1999 - v1
Checksum:i286C9807D33D93F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069441 Genomic DNA. Translation: AAD36946.1.
AL161500 Genomic DNA. Translation: CAB77903.1.
CP002687 Genomic DNA. Translation: AEE82383.1.
AY079159 mRNA. Translation: AAL84999.1.
BT002249 mRNA. Translation: AAN72260.1.
PIRiA85055.
RefSeqiNP_192344.1. NM_116673.7.
UniGeneiAt.27749.
At.74904.

Genome annotation databases

EnsemblPlantsiAT4G04350.1; AT4G04350.1; AT4G04350.
GeneIDi825755.
GrameneiAT4G04350.1; AT4G04350.1; AT4G04350.
KEGGiath:AT4G04350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069441 Genomic DNA. Translation: AAD36946.1.
AL161500 Genomic DNA. Translation: CAB77903.1.
CP002687 Genomic DNA. Translation: AEE82383.1.
AY079159 mRNA. Translation: AAL84999.1.
BT002249 mRNA. Translation: AAN72260.1.
PIRiA85055.
RefSeqiNP_192344.1. NM_116673.7.
UniGeneiAt.27749.
At.74904.

3D structure databases

ProteinModelPortaliQ9XEA0.
SMRiQ9XEA0. Positions 84-963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G04350.1.

Proteomic databases

PaxDbiQ9XEA0.
PRIDEiQ9XEA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G04350.1; AT4G04350.1; AT4G04350.
GeneIDi825755.
GrameneiAT4G04350.1; AT4G04350.1; AT4G04350.
KEGGiath:AT4G04350.

Organism-specific databases

TAIRiAT4G04350.

Phylogenomic databases

eggNOGiKOG0435. Eukaryota.
COG0495. LUCA.
HOGENOMiHOG000200748.
InParanoidiQ9XEA0.
KOiK01869.
OMAiLHMGHAE.
PhylomeDBiQ9XEA0.

Enzyme and pathway databases

BioCyciARA:AT4G04350-MONOMER.

Miscellaneous databases

PROiQ9XEA0.

Gene expression databases

GenevisibleiQ9XEA0. AT.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 5 hits.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 2 hits.
PF13603. tRNA-synt_1_2. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "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: DISRUPTION PHENOTYPE.
  5. "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.

Entry informationi

Entry nameiSYLM_ARATH
AccessioniPrimary (citable) accession number: Q9XEA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2015
Last sequence update: November 1, 1999
Last modified: February 17, 2016
This is version 122 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.