ID   SYL_FUSNN               Reviewed;         859 AA.
AC   Q8RIQ3;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=FN1517;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC   KCTC 2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009951; AAL93643.1; -; Genomic_DNA.
DR   RefSeq; NP_602344.1; NC_003454.1.
DR   RefSeq; WP_011015646.1; NZ_CP028101.1.
DR   AlphaFoldDB; Q8RIQ3; -.
DR   SMR; Q8RIQ3; -.
DR   STRING; 190304.FN1517; -.
DR   PaxDb; 190304-FN1517; -.
DR   EnsemblBacteria; AAL93643; AAL93643; FN1517.
DR   GeneID; 79782458; -.
DR   KEGG; fnu:FN1517; -.
DR   PATRIC; fig|190304.8.peg.20; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   InParanoid; Q8RIQ3; -.
DR   BioCyc; FNUC190304:G1FZS-21-MONOMER; -.
DR   Proteomes; UP000002521; Chromosome.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 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; 2.
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..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152018"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   859 AA;  99129 MW;  1F081E6B36C46E0C CRC64;
     MRDYEFKEIE KKWQERWSKD NIFKTENQVE GKENYYVLSM LPYPSGKLHV GHARNYTIGD
     VISRYKRMKG YNVLQPMGWD SFGLPAENAA IQNGTHPAIW TKSNIENMRR QLKLMGFSYD
     WEREIASYTP EYYKWNQWLF KRMYEKGLIY KKKSLVNWCP DCQTVLANEQ VEDGMCWRHS
     KTHVIQKELE QWFFKITDYA DELLEGHEEI KDGWPEKVLT MQKNWIGKSF GTELKLKVVE
     TGEDLPIFTT RIDTIYGVSY AVVAPEHPIV EKILKDNPSI KDKVTEMKNT DIIERGAEGR
     EKNGIDSGWH IENPVNKEIV PLWIADYVLM NYGTGAVMGV PAHDERDFVF AGKYNLPVKQ
     VITSKKSDEK VQLPYIEEGV MINSGEFNGL SSKDALVKIA EYVEEKGYGK RTYKYRLKDW
     GISRQRYWGT PIPALYCEKC GEVLEKDENL PVLLPDDIEF SGNGNPLETS NKFKEATCPC
     CGGKARRDTD TMDTFVDSSW YFLRYCDPKN LNLPFSKEIV DKWTPVDQYI GGVEHAVMHL
     LYARFFHKVL RDLGLLSSNE PFKRLLTQGM VLGPSYYSEK ENKYLLQKAA IIKGDKAYSQ
     SGEELQVKVE KMSKSKNNGV DPEEMLDKYG ADTTRLFIMF AAPPEKELEW NENGLAGAYR
     FLTRVWRLVF ENSELVKNAN DEIDYNKLSK EDKTLLIKLN QTIKKVTDAI ENNYHFNTAI
     AANMELINEV QTYVSSSMNS EQAAKILGYT LKKIIIMLSP FVPHFCDEIW EELGEKGYLF
     NEKWPEYDEK MLSSDETTIA VQVNGKVRGS FEIAKDSEQA LVEKTALKLP NVAKHLEGMN
     VVKIIVIPNK IVNIVVKPQ
//