SYL_CHLT3
ID SYL_CHLT3 Reviewed; 805 AA.
AC B3QRU2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Ctha_1432;
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX NCBI_TaxID=517418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78;
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., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-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; CP001100; ACF13895.1; -; Genomic_DNA.
DR RefSeq; WP_012499979.1; NC_011026.1.
DR AlphaFoldDB; B3QRU2; -.
DR SMR; B3QRU2; -.
DR STRING; 517418.Ctha_1432; -.
DR PRIDE; B3QRU2; -.
DR EnsemblBacteria; ACF13895; ACF13895; Ctha_1432.
DR KEGG; cts:Ctha_1432; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001208; 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 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; 1.
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_1000091306"
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; 91951 MW; BF8D0259AE8672C4 CRC64;
MKYDFTEIEK KWQAYWEQHQ TFKATEEPNK PKYYVLDMFP YPSGSGLHVG HLEGYTASDI
TARYKRLKGF SVLHPMGWDA FGLPAEQYAI KTGTHPRLTT ETNVANFKST LQRMGFSYDW
SREINTTDPG YVKWTQWIFL KLYEKGLAYV DDVPVNWCEE LKVVLANEEV DEKVNDGYTV
VRRPLRQWML KITAYAERLL TDLDEVDWPE SVKEMQRNWI GKSVGAELDF YLAGTDEKFR
IFTTRPDTVF GATYMVLSPE HPLLDKITTD EHKSAVAAYR EEAERKSDLE RTGLQKEKTG
VFTGSYALNP ATGKEIPIWT SDFVLMGYGT GAIMSVPAHD ERDWEFAKKF GIPIVEVIKS
PHSVQEAVFA GKDSVCTNSE NAEISINGLA YEEAFEKITD WFEKKGLGQR KVNYKLRDWL
FSRQRYWGEP IPIKHYEDGA ERAETELPLN LPEVSAYQPS GTGESPLANI AEWLYGEDEH
GKFRRETNTM PQWAGSCWYY LRFIDPDNPN EAVSPEKEKY WMNVDLYIGG AEHAVLHLLY
ARFWHKVLYD VGVVSTKEPF RKLFNQGMIL GEDNEKMSKS RGNVITADSV MSGYGADAVR
LYEMFLGPLE QVKPWSTNGI EGISRFLGKV WRLVYPNEAD GTVQVTDDAP SETVLRRMHK
TIKKVGEDTE TLKFNTAISE MMIYVNELQK EKCRSRTAIE NLLLMLSPFA PHICEELWQA
LGHEESITFA KFPEYDATLA KDDVVTIAVQ VNGKLRGTFD AAAGLSKDDM IAEAMKVESV
IKFTEGKEIV KQIAVPNKLV NLVVK
