SYL_MYCS2
ID SYL_MYCS2 Reviewed; 953 AA.
AC A0R7H5; I7FPE6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN OrderedLocusNames=MSMEG_6917, MSMEI_6729;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK71384.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP43155.1; -; Genomic_DNA.
DR RefSeq; WP_011731626.1; NZ_SIJM01000001.1.
DR RefSeq; YP_891113.1; NC_008596.1.
DR AlphaFoldDB; A0R7H5; -.
DR SMR; A0R7H5; -.
DR STRING; 246196.MSMEI_6729; -.
DR EnsemblBacteria; ABK71384; ABK71384; MSMEG_6917.
DR EnsemblBacteria; AFP43155; AFP43155; MSMEI_6729.
DR GeneID; 66738167; -.
DR KEGG; msg:MSMEI_6729; -.
DR KEGG; msm:MSMEG_6917; -.
DR PATRIC; fig|246196.19.peg.6734; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..953
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334775"
FT MOTIF 71..82
FT /note="'HIGH' region"
FT MOTIF 725..729
FT /note="'KMSKS' region"
FT BINDING 728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 953 AA; 106556 MW; FE42D3FF49C6681C CRC64;
MTEPATTPTT PDEQIPRHRY NADLAGQIER AWQETWSDRG TFNVANPVGS LAPTDGSDVP
ADKMFVQDMF PYPSGDGLHV GHPLGYIATD VYARYYRMLG RNVLHALGFD AFGLPAEQYA
VQTGTHPRTR TEANIVNFRR QLGRLGLGHD TRRSFSTTDV DYYKWTQWIF LQIYNAWFDR
DQNKARRISE LVEEFESGKR TLDDGRNWAD LSKGERADVI DGYRLVYRAD SMVNWCPGLG
TVLANEEVTS EGRSDRGNFP VFRKRLRQWM MRITAYSDRL LEDLDVLDWP EKVKTMQRNW
IGRSTGASVL FATAADDIEV FTTRPDTLFG ATYLVLAPEH DLVDTLVTDA WPDGTDERWT
YGAATPREAV AAYRTDIAAK SDLERQENKT KTGVFLGAYA TNPADGKQVP IFIADYVLAG
YGTGAIMAVP GGDQRDWDFA KEFGLPIIEV VTGGDISEAA YAGDGTMVNS GFLDGMDVAS
AKEAIIARLE ADGRGKRRVE YKLRDWLFAR QRYWGEPFPI VYDADGRAHP LPESALPVEL
PDVPDYSPVL FDPDDADSEP SPPLNKATEW VHVELDLGDG LQSYTRDTNV MPQWAGSSWY
ELRYTDPHNP DEMCAKENEA YWMGPRPDEH GPEDPGGVDL YVGGVEHAVL HLLYSRFWHK
VLYDLGYVSS REPYRRLVNQ GYIQAFAYTD SRGTYVPAAE VIERDGKFFW PGPDGEIEVN
QEFGKIGKSL KNSVSPDEIC DNYGADTLRV YEMSMGPLEA SRPWATKDVV GAHRFLQRVW
RVVIDETSGN VRVVEHEALS DETLRLLHRT IEGVREDYAA LRNNTAAAKL IEYTNHLTKE
GVAARAAIEP LVLMVAPLAP HLAEELWKRL GHDTSLAHGP FPEADPQYLV EDTIEFPVQV
NGKVRGKIVV AADADKAALE AAALADEKVQ AFLAGATPKK VIVVPGRLVN LVV
