SYL_CHRSD
ID SYL_CHRSD Reviewed; 856 AA.
AC Q1QV15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=Csal_2344;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE59693.1; -; Genomic_DNA.
DR RefSeq; WP_011507639.1; NC_007963.1.
DR AlphaFoldDB; Q1QV15; -.
DR SMR; Q1QV15; -.
DR STRING; 290398.Csal_2344; -.
DR PRIDE; Q1QV15; -.
DR EnsemblBacteria; ABE59693; ABE59693; Csal_2344.
DR KEGG; csa:Csal_2344; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000239; 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; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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..856
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009324"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 615..619
FT /note="'KMSKS' region"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 856 AA; 95491 MW; 37952B02BD302926 CRC64;
MDAQYTPHAI ESAAQTFWDK NQCFKAVEDA TREKFYCLSM FPYPSGKLHM GHVRNYTIGD
VVSRFQRMQG KNVLQPMGWD AFGMPAENAA IKNRVPPGAW TYDNIDAMRR QLKALGFAYD
WNREFATCDV DYYRWEQWFF TKLVEKGLVY KKMSTVNWDP VDQTVLANEQ VIEGRGWRSG
ALVERKEIPL WFLKITDYAD ELLADLDKVD WPEQVKTMQR NWIGKSTGVE LSFAVADSSE
QLEVYTTRPD TLYGVTYVAV AAGHPLARQA AQDNPALGDF LEECQQGGNS EAELATMEKK
GMDTGHKAIH PLTGREVPIF VANFVLMEYG TGAVMAVPAH DQRDWEFATK YGIPIEPVIA
DAEGNTPDLS QGAHTEHGKL INSGEFDGLE FDAAFDAIAA RLEANGQGTV KTNFRLRDWG
VARQRYWGAP IPVKYGPEGQ TVPLTDDELP VALPMEVEVD ASGSPLKKMP AFYDLGEGWT
RETDTFDTFM ESSWYYARFA SADNMEAMLD ERADYWLPVD LYIGGIEHAI LHLLYARFFH
KLMRDFGLVA SDEPFQRLLT QGMVIAETFY RANDDGSKDW FNPADVDVQR DDKGRPVSAI
LREDGQPVEM GGIEKMSKSK NNGVDPQAMI DRFGADTVRL FMMFAAPPEQ SLEWSDSGVE
GAHRFLKRLW KLVADHLDAG TPAALDADAL NDDQKTLRRK THETIAKASD DIGRRTTFNT
AIAAVMELVN AIGRFEDTSP QGLAVTREAL EACVLVLAPI VPHACHALWD ALGHDTPVID
AAWPQADEAA MVKDSVELAV QVNGKLRARL DVPAAADKAA IEAQALEAEN VRRHTEGKTI
RKVIVVPGKL VNIVAN