SYL_MYCUA
ID SYL_MYCUA Reviewed; 976 AA.
AC A0PKG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=MUL_0056;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL02831.1; -; Genomic_DNA.
DR RefSeq; WP_011738456.1; NC_008611.1.
DR AlphaFoldDB; A0PKG2; -.
DR SMR; A0PKG2; -.
DR STRING; 362242.MUL_0056; -.
DR PRIDE; A0PKG2; -.
DR EnsemblBacteria; ABL02831; ABL02831; MUL_0056.
DR KEGG; mul:MUL_0056; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000765; 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; -; 3.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..976
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009376"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..97
FT /note="'HIGH' region"
FT MOTIF 745..749
FT /note="'KMSKS' region"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 976 AA; 107185 MW; 42E0040F495963EA CRC64;
MTESPTTTPG STSGAPSGVP SGVNDAESDA PRHRYTAELA AGVERTWQQN WARLGTFNVP
NPVGSLAPSD GSPVPEDKLF VQDMFPYPSG EGLHVGHPLG YIATDVFARY HRMKGRNVLH
ALGFDAFGLP AEQYAVQTGT HPRTRTEANV VNFRRQLGRL GLGHDSRRSF STTDVEFYKW
TQWIFLQIYN AWFDAAANKA RPISELVAEF DSGARSLVDG RDWSTLSAGE RADVIDDHRL
VYRADSMVNW CPGLGTVLAN EEVTSDGRSD RGNFPVFRKR LRQWMMRITA YSDRLLDDLD
VLDWPDQVKT MQRNWIGRST GASALFTATR SNGETVGLEV FTTRPDTLFG ATYLVLAPEH
DLVDDLVGAG WPAGVDPLWT GGGATPAEAV AAYRRAIAVK SDLERQESKE KTGVFLGSHA
INPATGQPVP IFIADYVLAG YGTGAIMAVP GHDQRDWDFA RALGLPVVEV IAGGDISQAA
YTGDGVLVNS GFLDGMSVGE AKQAITARLE SDGYGQARIE FKLRDWLFAR QRYWGEPFPI
VYDADGRPHA LDESALPVEL PDVPDYSPVL FDPDDANSEP SPPLGKATEW LHVELDLGDG
LKPYSRDTNV MPQWAGSSWY ELRYTDPHNA DRFCAKENET YWMGPRPAEH GPDDPGGVDL
YVGGAEHAVL HLLYARFWHK VLYDLGHVSS REPYRKLINQ GYIQAFAYTD ARGSYVPAEE
VIERDGGFVY PGADGEIEVF QEFGKIGKSL KNSISPDEIC DDYGADTLRV YEMSMGPIEA
SRPWATKDVI GAHRFLQRVW RLVIDENTGE ILVADTPAEL DTDTLRALHR AIAGVAEDYA
ALRNNTAVAK LIEYTNFLTK RHRDAVPRAV IEPLVLMVAP LAPHLAEELW QRLGHTTSLA
HGPFPAADPA YLIDDTVEYP VQVNGKVRGR VVVAADADDD AVKAAALADQ KVQAFLAGAS
PRKVIVVAGR LVNLVV
