ID SYL_YERPY Reviewed; 860 AA.
AC B1JGA5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=YPK_3015;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP000950; ACA69288.1; -; Genomic_DNA.
DR RefSeq; WP_012304390.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JGA5; -.
DR SMR; B1JGA5; -.
DR KEGG; ypy:YPK_3015; -.
DR PATRIC; fig|502800.11.peg.3736; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..860
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091384"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 860 AA; 97065 MW; C4DF4CEE7E87C5EE CRC64;
MQEQYRPEDI ETQVQLHWQE KQTFKVTEDA SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIEYMKN QLKLLGFGYD
WDREIATCKP DYYRWEQWFF TKLYEKGMVY KKTSAVNWCP HDLTVLANEQ VIDGCCWRCD
TKVERKEIPQ WFIKITDYAE QLLNDLDTLE SWPEQVKTMQ RNWIGRSEGV DIIFDVVDSE
EKLSVYTTRP DTFMGVTYVA VAAGHPLSLQ AAATNPALAD FVAECRNTKV AEAEMATMEK
KGMATGLYAI HPLTGEKLPI WAANFVLMDY GTGAVMAVPG HDARDWEFAT KYNLPIKPVI
LAADGSEPDL SQEAMTEKGT LFNSGEFDGL NHEDGFNAIA DKLVALGVGQ RKVNYRLRDW
GVSRQRYWGA PIPMVTLEDG TVVPTPEDQL PVILPEDVVM DGISSPIKAD PEWAKTTVNG
IPGLRETDTF DTFMESSWYY ARYTCPQYDD GMLDPAAANY WLPVDQYVGG IEHAIMHLMY
FRFFHKLLRD AGLVDSDEPA KRLLCQGMVL ADAFYYTGNN GERIWVSPVD AIVERDDKGR
IVKAVDAEGH ELVYAGMSKM SKSKNNGIDP QVMVEKYGAD TVRLFMMFAS PAEMTLEWQE
SGVEGANRFL KRVWRLAFDH TAKGAVKPLD IASLTEEQKS LRRDLHKTIA KVTDDVGRRQ
TFNTAIAAVM ELMNKLGRAP QETEQDRALM QEALLAVVRM LYPFTPHVCF SLWQALGGEG
DIDTAPWPIA DEQAMVEDSK LVVVQVNGKV RGRITVPADA TEQQVRERAG QEHLVAKYLD
GVTVRKVIYV PGKLLNLVVG
//
