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Database: UniProt
Entry: SYL_EXIS2
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ID   SYL_EXIS2               Reviewed;         801 AA.
AC   B1YKH4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Exig_2275;
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-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; CP001022; ACB61727.1; -; Genomic_DNA.
DR   RefSeq; WP_012371144.1; NC_010556.1.
DR   AlphaFoldDB; B1YKH4; -.
DR   SMR; B1YKH4; -.
DR   STRING; 262543.Exig_2275; -.
DR   KEGG; esi:Exig_2275; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001681; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..801
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091318"
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   801 AA;  91651 MW;  C99750E7764ED912 CRC64;
     MPYNHREIEP KWQARWEQDN AFVTTEDPEK EGFYALDMFP YPSGAGLHVG HPEGYTATDI
     LARMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPREFT AQNIETFKRQ LKDLGFSYDW
     DREINTTDPK YYKWTQWIFT KLYEQGLAFV DEVAVNWCPA LGTVLANEEV IDGLSERGNH
     PVVRVPMRQW VLKITEYADR LLEDLDELDW PESVKEMQRN WIGKSEGAEI DFTIDGHKKQ
     VTVFTTRPDT VFGATYLVLA PEHPFVTDIT TEDHEEAVKA YIASVQTKSD LERTDLAKEK
     TGVFTGAFAV NPISGERLPI WIADYVLATY GTGAIMAVPA HDERDHEFAK QFDLPIIEVV
     KGGNVDEVAY TGEGEHVNSQ MLDGLSKQEA IETIIAELET NQVGRKKITF RLRDWLFSRQ
     RYWGEPIPVV HMEDGTMKTL DKSELPLELP MIPEIKPSGT GESPLALAED WLDYTDPVTG
     LKGRRETNTM PQWGGSCWYY LRFIDPHNEE AIADPEKLKY WLPVDIYIGG AEHAVLHLLY
     ARFWHKVLYD IGVVPTKEPF QKLYNQGMIL GENNEKMSKS RGNVINPDEI VKSHGADTLR
     LYEMFMGPLD ASVSWSENGL DGARRFLDRV WRLFERTADI QDVTTVDADF ERVYHQTVKK
     VTEDFTNIQF NTGISQLMVF VNEANKQPVL PRHFLRGFIQ LLTPVAPHLG EELWEQLGFE
     DTLTYAAWPT FDETKLVSDT MEFVIQVNGK VRSKLVISME ATKEEIEALA FADEKTQEWI
     GDKTVRKVIV VPKKLINIVA N
//
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