SYL_CERSK
ID SYL_CERSK Reviewed; 847 AA.
AC B9KMH8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=RSKD131_2209;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(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; CP001150; ACM02069.1; -; Genomic_DNA.
DR RefSeq; WP_015921266.1; NC_011963.1.
DR AlphaFoldDB; B9KMH8; -.
DR SMR; B9KMH8; -.
DR EnsemblBacteria; ACM02069; ACM02069; RSKD131_2209.
DR GeneID; 67447594; -.
DR KEGG; rsk:RSKD131_2209; -.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001597; Chromosome 1.
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; 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; 2.
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..847
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199221"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 847 AA; 94035 MW; 342919F87D884627 CRC64;
MSRYDPAATE SRWQAAWDAA GVFTARHDPA RPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
VARQKAAAGF SVLHPMGWDA FGMPAENAAM ERGGHPKDWT YGNIADMRAQ MKPLGLSIDW
SREFATCDPE YYGQQQAMFI DMMEAGLVYR KNAVVNWDPV DMTVLANEQV IDGKGWRSGA
PVVRRELTQW FFRISDYAGE LLEALDTLKD WPEKVRLMQA NWIGQSRGLQ FAFSTAGAPE
GFDRLEVYTT RPDTLMGASF AAISPDHPLA RHLERHDAEV AEFVAECRRV GTSEEALEKA
EKKGFDTGLR VRHPFDTAWE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FATKYGLPIR
PVFLPEGTEE TALAEAFVPM KSERVHYIRG FAGAEVQSGE EGVAAAIDFC ESQGVGRGVT
NYRLRDWGIS RQRYWGCPIP VIHCETCGVV PEAKENLPVR LPDDVSFDVP GNPLDRHPTW
RDCTCPKCGA KARRETDTMD TFVDSSWYYA RFTAPRAATP TDAEEADYWM NVDQYIGGIE
HAILHLLYSR FFARAMQKTG HLPAKAIEPF NALFTQGMVT HEIYLTRDAA GRPVYHLPED
VTDGKLADGT PVEIIPSAKM SKSKKNVVDP MNIIRQFGAD TARWFVMSDS PPERDVEWTA
SGAEAASKHL HRVWRLADEI SRADGEANAE DGALDKATAR AIAEVTQGVE GFAFNKAIAK
LYEFTNTLSR SGAGAEAKKR AMRTMAQLMS PMVPHLAEEV WAMLGGEGLV AQAAWPKADP
ALLIDDTVTL PIQVNGKRRG EITVPKEMAA SEVEKLVLAD EAVQRALGGA APKKLIVVPG
RIVNVVI
