ID   SYL_CYTH3               Reviewed;         921 AA.
AC   Q11VK7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, 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=CHU_1287;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(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}.
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DR   EMBL; CP000383; ABG58559.1; -; Genomic_DNA.
DR   RefSeq; WP_011584674.1; NZ_FPJX01000009.1.
DR   AlphaFoldDB; Q11VK7; -.
DR   SMR; Q11VK7; -.
DR   STRING; 269798.CHU_1287; -.
DR   PRIDE; Q11VK7; -.
DR   EnsemblBacteria; ABG58559; ABG58559; CHU_1287.
DR   KEGG; chu:CHU_1287; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001822; 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; 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; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..921
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074831"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           695..699
FT                   /note="'KMSKS' region"
FT   BINDING         698
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   921 AA;  104655 MW;  FEE623E5B6E57BFB CRC64;
     MADYHFGEVE NKWQSKWNAE KTFKALENSS KPKYFVLDMF PYPSGSGLHV GHPLGYIASD
     IMARYKRIKG YNVLHPMGFD SFGLPAEQYA VQTGQHPAIT TEQNIARYIE QLNKIGFSFD
     WDREIRTSDP AYYKWTQWIF IQLFNHWYNK ASDKAEPITN LVKQFETAGN AGINAACDED
     AVTFTAADWK SYSEKQQSDT LLKYRLTYLS ETMVNWCPGL GTVLANEEVK DGLSERGGFP
     VERKKMKQWS MRITAYADRL LKGLDTIDWP EAMKEMQRYW IGKSLGAMLT FKVVDKDMEL
     TVFTTRIDTT FGVTYVSIAP EHEWIGALTS PEQKAAVEEY VTKAKNRSER DRMSDVKTVS
     GCFTGSYVTN PFNNEKIPVW IADYVLAGYG TGVVMAVPSS DERDYKFASF YKLPIISVQE
     GAHTDITKED FDPKAGTMIN SGFLNGLTVK QAIPEAIKFI EEKKIGFAKI NFKMRDSIFG
     RQRYWGEPIP VSYKNDIPYV LNESELPLAL PAIDEYKPTE TGEPPLARNK AFADKGYELS
     TMPGWAGSSW YFMRYMDPQN KTAVAAADKI NYWGQVDLYM GGAEHATGHL LYSRFWNKFL
     FDMGITPNDE PFAKLINQGM IQGVSKFAYR INGTNKFVSA GLKKEYDTTP IHVDVSIVHN
     DVLDTEAFKK WRPDFASAEF ILENNTYVCG SEVEKMSKSK FNVVNPDDIV NKYGADTLRM
     YEMFLGPLEQ SKPWNTNGIE GVYKFLNRFW RLFHDTAGNF AVSDAQPTAE ELKVLHKTLK
     RVEEDIERFS FNTPVSTFMI CVNELGSLKC NKRTILEPLT IALSPLAPHI AEELWSLLGH
     TTSVSTATYP AWDEKFLVES NHEYPISING KMRAKLNLPV DMPAAEVEQQ VLANEVVQKW
     LEGKAPKKII VIPNKIVNVV M