SYL_STRCO
ID SYL_STRCO Reviewed; 966 AA.
AC Q9RDL5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SCO2571;
GN ORFNames=SCC123.09c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939113; CAB66249.1; -; Genomic_DNA.
DR RefSeq; NP_626809.1; NC_003888.3.
DR RefSeq; WP_003976232.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9RDL5; -.
DR SMR; Q9RDL5; -.
DR STRING; 100226.SCO2571; -.
DR PRIDE; Q9RDL5; -.
DR GeneID; 1098005; -.
DR KEGG; sco:SCO2571; -.
DR PATRIC; fig|100226.15.peg.2616; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR InParanoid; Q9RDL5; -.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q9RDL5; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..966
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152093"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..82
FT /note="'HIGH' region"
FT MOTIF 734..738
FT /note="'KMSKS' region"
FT BINDING 737
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 966 AA; 107128 MW; 87C81658A6C12B87 CRC64;
MSETNPAATA PVSADAAPHR YTAAMAAEIE ARWQDFWDAE GTYAAPNPKG DLAGDPELVA
KPKKFIMDMF PYPSGAGLHV GHPLGYIATD VFARFQRMTG HNVLHTLGFD AFGLPAEQYA
VQTGTHPRVS TEANMKNMQS QLRRLGLGHD RRRSFATIDP EYYKWTQWIF LQIFNSWYDD
EAKKARPIAE LVAQFASGER EVPGHAGRAW SSLSEAERAD VLGEYRLAYA SDAPVNWCPG
LGTVLANEEV TADGRSERGN FPVFKSKLRQ WNMRITAYAD RLLDDLDQLD WPEAIKLQQR
NWIGRSEGAR VDFPVDGERI TVFTTRPDTL FGATYMVLAP EHPLVEKFTP AVWPEGTRDA
WTGGHATPTE AVAAYRAQAA SKSDVERQAE AKDKTGVFIG AYATNPVNGE QVPVFVADYV
LMGYGTGAIM AVPAHDSRDF EFARAFELPV RCVVEPTDGR GTDTSTWDEA FASYDAKIVN
SSGTDVSLDG LGVVEAKERV TEWLERAGAG AGTVNFRLRD WLFSRQRYWG EPFPIVYDED
GIAHPLPDSM LPLELPEVED YSPRTFDPDD ADTKPETPLS RNEDWVHVTL DLGDGRGPRK
YRRETNTMPN WAGSCWYELR YLDPHNGERL VDPEIEQYWM GPREGLPHGG VDLYVGGAEH
AVLHLLYARF WSKVLFDLGH VSSAEPFHKL FNQGMIQAYV YRDSRGIAVP AAEVEERDGA
YYYQGEKVSR LLGKMGKSLK NAVTPDEICA EYGADTLRLY EMAMGPLDVS RPWDTRAVVG
QFRLLQRLWR NVVDEDTGEL SVADVAESDI DAGTLRALHK AVDGVRQDLE GMRFNTAIAK
VTELNNHLTK AGGPVPRSVA ERLVLLVAPL APHVAEELWR KLGHESSVVH EDFPVADPAY
VVDETVTCVV QIKGKVKARL EVAPSISEDD LEKAALADEK VVAALGGAGI RKVIVRAPKL
VNIVPA
