SYL_CHLL2
ID SYL_CHLL2 Reviewed; 805 AA.
AC B3EH05;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Clim_0598;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001097; ACD89685.1; -; Genomic_DNA.
DR RefSeq; WP_012465566.1; NC_010803.1.
DR AlphaFoldDB; B3EH05; -.
DR SMR; B3EH05; -.
DR STRING; 290315.Clim_0598; -.
DR EnsemblBacteria; ACD89685; ACD89685; Clim_0598.
DR KEGG; cli:Clim_0598; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008841; 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; 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; 2.
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..805
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091302"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 91997 MW; D4F3FE28F9E92DF3 CRC64;
MRYEFSAIEK KWQAIWQENG TFKTGESTEK PKYYVLDMFP YPSGSGLHVG HLEGYTASDI
IARFKRSRGF NVLHPMGWDA FGLPAEQYAI KTGTHPKITT ENNIRSFRET LQAMGFSYDW
SKEINTTDPA YFKWTQWIFL RLYEMGLAYM SDVDVNWCEE LKTVLANEEV DEKIADGYTV
VRKPLRQWVL KITAYAERLL ADLDELEWPE NVKQMQRNWI GRSEGVEIDF ELRCHGKNLR
VYTTRPDTLF GATYLVVSPE HPLAEKLATA DNLKEVKAYI SRAKLKTELE RTGLQKDKTG
VFTGSYAINP ATGNPLPVWI SDFVLISYGT GAIMSVPAHD SRDWEFAKKF DLPIIEVIKS
PHDVNDAVFE GKESVPVNSS NSEITIDGLP FREAFDTMAS WLEKKGAGKR TINYKLRDWI
FSRQRYWGEP IPIKHYEDGT LRTETILPLT LPDVEAYQPS ETGESPLATI HDWLYGSDEF
GSFRRETNTM PQWAGSCWYY LRFIDPENSG RLIDPEREKY WMNVDLYIGG AEHAVLHLLY
ARFWHKVLFD LNVVSTVEPF RKLFNQGMIL GEDNEKMSKS RGNVIPADHV LKTYGADAVR
LYEMFLGPLE QVKPWNTNGI EGISRFLGKV WRLVYPEQEG NKAELTDETM PEELLRRLHK
TIRKVTEDTE ALKFNTAIAE MMVLVNELQR NGCRNRTAVE SMILLLAPYA PHIAEELWQA
TGHTGSISNE PFPNYVAGLA TDSVVQIAVQ VNGKLRGTFS TPAGTPQNSL IETARNVESV
MKFLEGKAIM REIVVPDKLV NFAVK
