SYLC_ARATH
ID SYLC_ARATH Reviewed; 1091 AA.
AC F4I116; Q56WB9;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Leucine--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.4 {ECO:0000305};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000305};
DE Short=LeuRS {ECO:0000305};
GN OrderedLocusNames=At1g09620 {ECO:0000312|Araport:AT1G09620};
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 [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 [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] OF 480-1091.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
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).
RN [6]
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).
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: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AC000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC003970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28469.1; -; Genomic_DNA.
DR EMBL; AK222125; BAD95115.1; -; mRNA.
DR RefSeq; NP_172433.2; NM_100834.5.
DR AlphaFoldDB; F4I116; -.
DR SMR; F4I116; -.
DR IntAct; F4I116; 1.
DR STRING; 3702.AT1G09620.1; -.
DR PaxDb; F4I116; -.
DR PRIDE; F4I116; -.
DR ProMEX; F4I116; -.
DR ProteomicsDB; 234104; -.
DR EnsemblPlants; AT1G09620.1; AT1G09620.1; AT1G09620.
DR GeneID; 837489; -.
DR Gramene; AT1G09620.1; AT1G09620.1; AT1G09620.
DR KEGG; ath:AT1G09620; -.
DR Araport; AT1G09620; -.
DR TAIR; locus:2012240; AT1G09620.
DR eggNOG; KOG0437; Eukaryota.
DR HOGENOM; CLU_004174_1_1_1; -.
DR InParanoid; F4I116; -.
DR OMA; MLIGEFV; -.
DR OrthoDB; 75155at2759; -.
DR PRO; PR:F4I116; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I116; baseline and differential.
DR Genevisible; F4I116; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA: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:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PTHR45794; PTHR45794; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..1091
FT /note="Leucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000433547"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 715..719
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 591
FT /note="Q -> L (in Ref. 3; BAD95115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 123451 MW; 7875BD1F436674CC CRC64;
MASESKSYAR RDRLLEIEAT VRKWWEDEDV FRAESCENLP KPGEKFFSTF PFPYMNGYLH
IGHAFSLSKV DFASAYHRLR GANVLLPFGF HCTGMPIKAS ADKLRREIEQ FGNPPVFTAE
DTTKVPEVQE ESSDTIALPI PGQFKGKKSK VAAKAGGQVY QWEIMRSFGL TDSEIANFRE
PSEWLYYFPP LAVEDLRAYG LGCDWRRSFV TTDVNPFFDA FVRWQMRKLK SMGKIVKDRR
YTIFSPLDGQ PCADHDRATG EGVQPQEYTL IKMEVVKPFP LKLGPLEGKR VFLAAATLRP
ETMYGQTNAW VLPDGKYGAY EISETEVFIL TERAALNLAY QNFSKNPQEP SCLVELTGYD
LIGLPLRSPL SVNEIIYALP MLTILTNKGT GIVTSVPSDA PDDYMALQDL IKKPALQDKY
GVKTEWLPTE IIPIINIPEF GDKAAEKVCL DLKIKSQNDK EKLAEAKRLT YLKGFTEGTM
LIGEFFGRKV QEIKPIIKTK LIETGEAIIY SEPEKPVMSR SGDECVVALT DQWYITYGES
EWRKIAEECL SKMNLYSDET RHGFEHTLSW LNQWACSRSF GLGTRIPWDE QFLVESLSDS
SLYMAYYTVA HIFHDGDMYK GSKSLIRPQQ MNDEVWEYLF CDGPYPKSSD IPSAVLSEMK
QEFDYWYPLD LRVSGKDLIQ NHLTFFIYNH TALMANRNWP RGIRCNGHIM LNSEKMSKST
GNFRTLRQSI EEFSATGTRF CLADAGDGVD DANFAFETAN AAILRLTKEL TWMEEVLDVE
SSLRTGPPST YADKVFENDM NIALRLTERA YKDCLFREAL KNGFYDLQAA RDEYRLSCGT
GGMHHDLLLK FMDVQTRLIV PICPHFADYV WRKVLNKEGC VLTAGWPPSN EPDLVLKSAN
KYLQDSIVLM RKLLQKQLSG SKKGAKKGAQ VTAVPEGKLK GLVYVNEQFD GWRAHCLRIL
QSRFDQQTCS FPPDTEMLAE LSATLLQEGK NLKAIQKVCM PFLKFKKDEA ISIGTQALNL
RLPFGEIEVL QSNKDLIRRQ LGLEEVEIYS ASDPDDVSIA GPHASLLTQN PPSPGSPTAI
FVTSTSVCPP S
