SYL_MYCPU
ID SYL_MYCPU Reviewed; 807 AA.
AC Q98RB6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=MYPU_0930;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL445563; CAC13266.1; -; Genomic_DNA.
DR PIR; E90523; E90523.
DR RefSeq; WP_010924897.1; NC_002771.1.
DR AlphaFoldDB; Q98RB6; -.
DR SMR; Q98RB6; -.
DR STRING; 272635.MYPU_0930; -.
DR EnsemblBacteria; CAC13266; CAC13266; CAC13266.
DR KEGG; mpu:MYPU_0930; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_14; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; MPUL272635:G1GT6-91-MON; -.
DR Proteomes; UP000000528; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..807
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152051"
FT MOTIF 38..49
FT /note="'HIGH' region"
FT MOTIF 579..583
FT /note="'KMSKS' region"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 807 AA; 93884 MW; C888CC0524A9A3A1 CRC64;
MYNHKEIEKK WQKIWDQSKA FKTGNKSDKK YYVLDMFPYP SGSGLHVGHP EGYTATDIIA
RFKRLKGFDV LHPMGWDAFG LPAEQYAIST GNNPNEFTQK NIATFKKQIK SLGLSYDFDK
EVNTTDPKFY EQTQWIFKEL YKKGLAVLAD IDVNWCEELG TVLANEEVLI DKDGNKVSER
GSFPVVKKKM RQWVLKITNY ADKLLEGLED LDWENSLKLL QKNWIGKSTG TKVKFALELL
DESIEVFTTR IETIFGATFL TISPEHPLVE KIVTSENKEK VKDFIKEFEK LDDRQKADKN
EKNGIFTGSY AINPFNQKKI PIWIGDFVLL SYGTGAIMSV PAHDKRDYEF ANKYGLEIKQ
VIVSKENVEL PYLESGHLIN SSEFNGLSSK EAIEKLNQYV EKNNLGQVET FYKLRDWIFS
RQRYWGEPFP VAFDDENNVY LIDGLVELPF MENIKPSKNG QSPLFNNKKW LYFEKDGKKL
TRETNTMPQW AGSNWYYLAY ILKNADGSYE KLDSEEAKKR FKKWLPVDLY IGGQEHAVLH
LLYSRFWHRF LYDIGVVPTK EPFQKVVNQG MILGTDGQKM SKSRGNIINP SEIVDELGAD
TLRVYEMFMG PLTDDKDWQV ESIKGIRKWL ERVYRLFEMF FDGQKTIEKS NEDHLILSQY
NKLIKEIENE VELLKFNTAI SKLMVFVNLL YKVEKIPSWE ILKNFALILS LFAPHIAEEL
LEKMNQKQVK DQIWPTYDPT YLESNLTKYV IQINGKVRAI VDFELDKTQE EVLAKAMQIE
KIKTLLENKN IIKVIFVANK VLNLIVK
