ID   SYL_FLAPJ               Reviewed;         962 AA.
AC   A6H244;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=FP2363;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44418.1; -; Genomic_DNA.
DR   RefSeq; WP_011964452.1; NC_009613.3.
DR   RefSeq; YP_001297219.1; NC_009613.3.
DR   AlphaFoldDB; A6H244; -.
DR   SMR; A6H244; -.
DR   STRING; 402612.FP2363; -.
DR   PRIDE; A6H244; -.
DR   EnsemblBacteria; CAL44418; CAL44418; FP2363.
DR   GeneID; 66553471; -.
DR   KEGG; fps:FP2363; -.
DR   PATRIC; fig|402612.5.peg.2420; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000006394; 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; -; 3.
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; 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; 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..962
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009339"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           737..741
FT                   /note="'KMSKS' region"
FT   BINDING         740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   962 AA;  109354 MW;  517F77D040A253F0 CRC64;
     MKYNPNEIDA KWQKNWANNQ TFAASNTSIK PKYYILDMFP YPSGAGLHVG HPLGYIASDI
     VARFKRHKGF NVLHPQGYDS FGLPAEQYAI QTGQHPDKTT KENIARYREQ LDKIGFSFDW
     SREIRTSNAN YYKHTQWIFI QLFNSWYNKS NDKAEDITTL ISLFQKEGNT NINAVCDDNI
     APFSAQDWTG FSSSKQQKIL LQYRLTYLAE TEVNWCPGLG TVLANDEIIN GVSERGGHPV
     IRKKMTQWSM RISAYAERLL QGLNDIDWSE SIKESQRNWI GKSVGAMVSF KVKNQKSQVT
     SEATLSDLRP STLDYIEVFT TRPDTIFGVT FMTLAPEHPL VQEITTPEQK AAIEAYIEKT
     AKRSERERMA DVKTISGVFT GAYAEHPFTK EQIPVWIGDY VLAGYGTGAV MAVPCGDERD
     YAFANFFKGQ NGMPEIKNIF DNVDIATEAY GSKDNVIIAN SDFLNGLNYK QATKKAIAEL
     ETLNQGKGKT NYRLRDAVFS RQRYWGEPFP VYYVNGLPQM IDAKHLPIAL PEVEKYLPTE
     DGLPPLGNSA KWAWNTITNE VDFNENINNT TIYPLELNTM PGWAGSSWYW MRYMDPHNDN
     EFASPEAIKY WESVDLYIGG SEHATGHLLY ARFWNKFLKD KGYAPTEEPF KKLINQGMIL
     GNSAFVYRSE DSKKLYSKGL ISDKTTQAIH VDLAIINETT NELDIEAFKK HPLYSDYANA
     EFILENGKYI VGREVEKMSK SKYNVVNPDD ICNEYGADTL RLYEMFLGPL EQSKPWNTAG
     ITGVFGFLKK LWRLYFDDNG LIVTNNEPSK ESLKSLHKTI KKVTEDIENF SFNTSVSQFM
     ICVNELGTQN CHERAILEPL AIILSPYAPH IAEELWSQLG NSESISTVAF PICHEKYLVE
     SDKEYPVSFN GKMKFTINLP LDLTPAQIEE IIMKDERTIK QLDGNTPKKV IIIPGKVINL
     VG