SYL_DEIRA
ID SYL_DEIRA Reviewed; 823 AA.
AC Q9RSF0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 143.
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=DR_2174;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF11720.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF11720.1; ALT_INIT; Genomic_DNA.
DR PIR; D75307; D75307.
DR RefSeq; NP_295897.1; NC_001263.1.
DR RefSeq; WP_027479923.1; NC_001263.1.
DR AlphaFoldDB; Q9RSF0; -.
DR SMR; Q9RSF0; -.
DR STRING; 243230.DR_2174; -.
DR PRIDE; Q9RSF0; -.
DR EnsemblBacteria; AAF11720; AAF11720; DR_2174.
DR KEGG; dra:DR_2174; -.
DR PATRIC; fig|243230.17.peg.2398; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR InParanoid; Q9RSF0; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; 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..823
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152009"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 823 AA; 92613 MW; 2E6445F39005A110 CRC64;
MTQEATKPNI QEPRAERYNP HAIEQKWQGQ WQESGLYKFD ENAPGEKFYA LTMFPYPSGN
LHIGHWYANV APDARARWLR MRGYNVLFPM AFDAFGLPAE NAAIKNNTNP ATWTYANIER
MTGQFSRMGT MIDWSRKFAT CDPEYYRWNQ WFFIEFWKRG LAYKKGGLVN WCPKDQTVLA
NEQVVNGHCE RCGTAVERRN LSQWYLKITD YAEELLDFSA TDMPEKVRAM QTNWIGKSVG
AEVTFDTPAG PETVFTTRPD TLMGATFMVL APEHAKVKEL TTDEQRAEVE AYVAAAGRKT
DVERQQEGEK TGVFTGSYAT HPISGHQLPI WVADYVLVTY GTGSIMAVPA HDERDFAFAK
KFDLPIREVI RAEGSEGMGD QPSEPYSGEG QIVNSGEFDG MPGGKASIAA IIARLEERGV
AKAKTTYRLR DWLFARQRYW GTPIPFVHCE KCGMQPVPED QLPVKLPENV AFTPTGQSPL
KLDEEWKTTT CPCCGGPAER ETDTMDTFVD SSWYMYRYLS PNYDGGPFDP SKAGLLPVDL
YTGGIEHAIL HLLYSRFWTK VMRDMGLTTQ SEPFARLRNQ GMVLGEDGEK MSKSRGNVVD
PDDLVREYGA DTVRAFLMFI APWELGGPWD PQGINGPSKW LSRVWNVFFE EKVSGPEEKM
QGADVRFAVH SALKKVNDDF ERMSFNTIIS TLMELTNALV KAKRSPVFGT PVWEEALDIF
NRMLAPVVPH IAEEIWHERG QKGSVHTAQW PQVDEAAAVR DTVTIGVQVS GKVRGEVSIS
KTASQEEALS AARAIAEVQK HLEGKTVVKE IYVPGRIINI VAK
