SYL_RENSM
ID SYL_RENSM Reviewed; 862 AA.
AC A9WS85;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=RSal33209_1940;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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=ABY23673.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000910; ABY23673.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A9WS85; -.
DR SMR; A9WS85; -.
DR STRING; 288705.RSal33209_1940; -.
DR PRIDE; A9WS85; -.
DR EnsemblBacteria; ABY23673; ABY23673; RSal33209_1940.
DR KEGG; rsa:RSal33209_1940; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR Proteomes; UP000002007; 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; 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; 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.
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..862
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334801"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..89
FT /note="'HIGH' region"
FT MOTIF 627..631
FT /note="'KMSKS' region"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 862 AA; 95215 MW; F244F35CF99EC356 CRC64;
MVQSRGFSLS SVRNGTEGNT MSQHTSQPAA DVPVDVADEN RYDIAAIEAK WLPRWEEANI
FAPLDDGSKE RRYVCDMFPY PSGDLHMGHA EAFVMGDVVG RYWKLKGFDV LHPVGWDSFG
LPAENAAIKR NAHPAEWTYA NIETQAASFK RYAIGVDWSR RLQTSDPEYY RWTQWLFLRF
YERGLAYRKN SPVNWCPKDL TVLANEQVIN GACERCGTPV TKKNLNQWYF KITDYADRLL
DDMAQLEGHW PERVLAMQRN WIGRSQGAHV DFVIDGMSDA ETGEAKKVTV FTTRPDTLYG
ATFFAVAVDA ALADELVTEE QRAELSAYQE RVKHLSDIER QESDREKTGV FLGRYAINPI
DGEMLPIWAA DYVLADYGTG AIMAVPAHDQ RDLDFARAFD LPVRQVLDTG AENPAETGTA
AIGDGVLVNS GELDGLAKAE AIPAAISLLS KIGTGEATTN YRLRDWLLSR QRFWGAPVPI
IHCAECGEVP VPDDQLPVRL PENLRGEQLA PKGTSPLASV ADWVNVDCPK CGGAATRDTD
TIDTFVDSSW YYLRYTSPEY TDGPFDPAAA TRWMGVDQYV GGVEHAILHL LYSRFFVKVL
NDLGLLEAKE PFKALLNQGQ VLNGGKAMSK SLGNGVDLSQ QLDRFGVDAV RLTMVFASPP
EDDVDWADVS PSGSAKFLAR AWRLAQDVTS EIGVDPATGD RALRSVTHRT LSEAADLIDA
HKFNVVVAKT MELVNITRKS IDSGCGPADP AVREAVEAVA VILSLFAPYT AEDIWAELGH
QDFVARASWP TVDDSLLVQS TITAVVQVQG KVRDRLEVPT DITEDQLREL ALASEIVQKT
LDGRGIRTVI VRAPKLVNIV PA
