SYL_UREP2
ID SYL_UREP2 Reviewed; 806 AA.
AC B1AJ10;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=UPA3_0387;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
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; CP000942; ACA33294.1; -; Genomic_DNA.
DR RefSeq; WP_010891746.1; NC_010503.1.
DR AlphaFoldDB; B1AJ10; -.
DR SMR; B1AJ10; -.
DR EnsemblBacteria; ACA33294; ACA33294; UPA3_0387.
DR GeneID; 29672253; -.
DR KEGG; upa:UPA3_0387; -.
DR HOGENOM; CLU_004427_0_0_14; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002162; Chromosome.
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 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..806
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000074849"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 806 AA; 93299 MW; B5F61AFE314A41A9 CRC64;
MYNHNKIEKK WQKYWLDNKT FKFVDNPNNP KKFYVLDMFP YPSGKGLHVG HPKGYTATDV
ISRFKRLNGY DVLHPIGWDA FGLPAEQYAL ETNNHPHTFT QQNIKIFRKQ LQMIGFDFDY
DKEVDTTDPQ FYQWTQWIFV QLYKHNLAEI QDIDVNWCEN LGTVLSNEEV VLNDKNERVS
ERGGHPVVRK PMKQWVLKIV DYADKLLDGL NEVEFSESLK SLQRNWIGKS IGTSVQFKIK
DSLLTLDVFT TRIDTIYGVQ YLVVAPEHPI LKSITSEQQI NVVQSYIEQT KKISDLDRIA
DTNKTGVFSG AYAINPINQE IIPIWVSDYV LMNFATGAVM GVPAHDERDY AFAKKYALPI
KSVIDTKQKL PYAGDGLHIN SAMINGLNIK QSQNVLNDYL IKNHLGKKVA NYKLRNWIFS
RQRYWGEPFP VLFDENNQIK IIEDLPVLLP NLNEFKPSKT GESPLANAQE WLYVEIDGKK
YRRETNTMPQ WAGSSWYFLA YILKNEDGSY TPLNSEEAKK RFAKWLPVDV YIGGQEHAVL
HLLYSRFWHR FLYDIGVVPT KEPFYKVINQ GMILGENNEK MSKSKGNVIN PDDIIASHGA
DTLRIYEMFM GPLTASLPWN PDGLDAMRKW LDRVYRLYHN LSELEVVEDL NKLNEEIIIA
YHTLIKNYTK AINEQAFNIA ISEMMVFVNV LYKNKVINYE LLDNFLILLS CYAPHLAEEL
YSLNHSESVC LQKMPIYDEQ KIIAQNITIP IQINGKLKHT INVLRDTNAE ELVNLALACE
QVKQEIGDQP IKKQIVVVNK IINFVI