SYLM_ARATH
ID SYLM_ARATH Reviewed; 973 AA.
AC Q9XEA0;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Leucine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.4 {ECO:0000305};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000305};
DE Short=LeuRS {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2369 {ECO:0000303|PubMed:16297076};
DE Flags: Precursor;
GN Name=EMB2369 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At4g04350 {ECO:0000312|Araport:AT4G04350};
GN ORFNames=T19B17.7 {ECO:0000312|EMBL:AAD36946.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a two step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000250|UniProtKB:Q9P2J5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16251277}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8RXK8}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC embryo at the globular stage. {ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AF069441; AAD36946.1; -; Genomic_DNA.
DR EMBL; AL161500; CAB77903.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82383.1; -; Genomic_DNA.
DR EMBL; AY079159; AAL84999.1; -; mRNA.
DR EMBL; BT002249; AAN72260.1; -; mRNA.
DR PIR; A85055; A85055.
DR RefSeq; NP_192344.1; NM_116673.7.
DR AlphaFoldDB; Q9XEA0; -.
DR SMR; Q9XEA0; -.
DR IntAct; Q9XEA0; 1.
DR STRING; 3702.AT4G04350.1; -.
DR PaxDb; Q9XEA0; -.
DR PRIDE; Q9XEA0; -.
DR ProteomicsDB; 232981; -.
DR EnsemblPlants; AT4G04350.1; AT4G04350.1; AT4G04350.
DR GeneID; 825755; -.
DR Gramene; AT4G04350.1; AT4G04350.1; AT4G04350.
DR KEGG; ath:AT4G04350; -.
DR Araport; AT4G04350; -.
DR TAIR; locus:2134887; AT4G04350.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_0_0_1; -.
DR InParanoid; Q9XEA0; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 375759at2759; -.
DR PhylomeDB; Q9XEA0; -.
DR PRO; PR:Q9XEA0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEA0; baseline and differential.
DR Genevisible; Q9XEA0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..973
FT /note="Leucine--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433548"
FT MOTIF 126..135
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 730..734
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 973 AA; 111033 MW; 286C9807D33D93F2 CRC64;
MSSHHQILQI RSDPFVLSHC CRHTRLTSSL TLQSPLKQPF SCLPFRWRRS YRGGVRSSTT
ETHGSKKEAL VSETATTSIE LKRVYPFHEI EPKWQRYWED NRIFRTPDDV DTSKPKFYVL
DMFPYPSGAG LHVGHPLGYT ATDILARLRR MQGYNVLHPM GWDAFGLPAE QYAIETGTHP
KTTTLKNIDR FRLQLKSLGF SYDWDRELST TEPDYYKWTQ WIFLQLYKKG LAYQAEVPVN
WCPALGTVLA NEEVVDGVSE RGGHPVIRKP MRQWMLKITA YADRLLEDLD ELEWPESIKE
MQRNWIGRSE GAELNFSILD GEGRETDKEI TVYTTRPDTL FGATYMVVAP EHQLLSYFVT
AEQKQQVEEY KDFASRKSDL ERTELQKDKT GVFTGCYAKN PANGDAIPIW VADYVLASYG
TGAIMAVPAH DTRDNEFALK YNIPIKWVVR NEANSSDDAK QVYPGLGIIE NSSTLETGLD
INQLSSKEAA LKVIEWAERT GNGKKKVNYK LRDWLFARQR YWGEPIPILI LDESGETIAI
SESELPLTLP ELNDFTPTGT GEPPLSKAVS WVNTVDPSTG KPAKRETSTM PQWAGSCWYY
LRFMDPKNPE ALVDKEKEKY WSPVDVYVGG AEHAVLHLLY SRFWHKVLYD IGVVSTKEPF
KCVINQGIIL GEVQYTAWKD QEGNYVSADT EERLNEHQQV TIPEEKVIKS GDHFVLKEDP
SIRLIPRVYK MSKSRGNVVN PDDVVLEYGA DSLRLYEMFM GPFRDSKTWN TSGIEGVHRF
LARTWRLVIG LPQSDGSFKD GTLVTDDEPT LEQLRTLHKC IAKVTEEIES TRFNTGISGM
MEFVNAAYKW NNQPRGIIEP FVLLLSPYAP HMAEELWSRL GHPNSLAYES FPKANPDYLK
NTTIVLPVQI NGKTRGTIEV EEGCSEDDAF VLASQDDKLR KYLDGQSIKK RIYVPGKILN
VILDRTNVKV TTK
