ID   SYL_SACD2               Reviewed;         819 AA.
AC   Q21FG6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Sde_3308;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(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}.
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DR   EMBL; CP000282; ABD82563.1; -; Genomic_DNA.
DR   RefSeq; WP_011469779.1; NC_007912.1.
DR   AlphaFoldDB; Q21FG6; -.
DR   SMR; Q21FG6; -.
DR   STRING; 203122.Sde_3308; -.
DR   PRIDE; Q21FG6; -.
DR   EnsemblBacteria; ABD82563; ABD82563; Sde_3308.
DR   KEGG; sde:Sde_3308; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001947; 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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009421"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           577..581
FT                   /note="'KMSKS' region"
FT   BINDING         580
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  92026 MW;  513F6286CAE6CF0C CRC64;
     MNEYYQPSEI EAQAQKYWEE NKSFNVTEDP TKEKFYCLAM FPYPSGRLHM GHVRNYTISD
     VISRFHRMQG KNVLHPMGWD AFGLPAENAA IKNNTAPAKW TYSNTDYMRK QLTELGFGFD
     WSREVTTCKP DYYKWEQWFF TRLYEKGLAY KKVASVNWCP NDQTVLANEQ VVDGQCWRCD
     TAVERKEIPQ WFIRITDYAE ELLADLDKLP NWPEQVKTMQ RNWIGKSQGV EMRFDLANPI
     AGTTGFDVYT TRPDTLMGVT YVSLAAEHPI AKALAETNPA LAAFIQECKV QSVAEADMAN
     MEKKGIDTGI KAKHPITGDE VSVWVANYVL MDYGSGAVMA VPAHDQRDWE FAKKYDLEIK
     QVIAPEDGSD IDLTKEAFVD KGVLVNSGEY DGLNFNAAFE AISQTLQAAN KGKVTTNFRL
     RDWGVSRQRY WGSPIPIFNL PDGGVIPVPA DRLPVLLPED VQMDGVQSPI KADKEWCKAE
     LNGQAVEHET DTFDTFMESS WYYARYTSPN ADSMLDPDKA NYWLPVDQYV GGIEHAILHL
     LYARFFHKLM RDEGLVECDE PFERLLCQGM VLKDGTKMSK SKGNTVDPED LIKTYGADTV
     RLFSMFAAPP EQSLEWTDSG VEGAFRFLKK LWKAVASHLE AGSAGEIDAN SLDEQQKALR
     RKTHETISKV SDDYGRRQTF NTAIAAVMEL LNEITRSADR STPNGLAVER EALEAATLLL
     APIVPHACHA LWQAFGNEVA VLDAPWPTVD EAALVKDTIT IVAQVNGKVR AKLDAPANAD
     KDALEKIALA DESVLKHIDG KMIRKVIVVP GKLVNIVAN