ID   SYL_CHRFK               Reviewed;         962 AA.
AC   A0M5T1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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};
GN   OrderedLocusNames=GFO_3032;
OS   Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS   (Gramella forsetii).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17595 / CGMCC 1.15422 / KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67976.1; -; Genomic_DNA.
DR   RefSeq; WP_011710877.1; NC_008571.1.
DR   AlphaFoldDB; A0M5T1; -.
DR   SMR; A0M5T1; -.
DR   STRING; 411154.GFO_3032; -.
DR   KEGG; gfo:GFO_3032; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000755; 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   Gene3D; 3.40.50.620; HUPs; 3.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_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.
FT   CHAIN           1..962
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009347"
FT   REGION          548..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           737..741
FT                   /note="'KMSKS' region"
FT   COMPBIAS        548..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   962 AA;  110237 MW;  F535EE086A219AC2 CRC64;
     MSYHFNKIEE KWQKYWADNQ TFKASNDSEK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
     YARFKRHKGF NVLHPQGYDS FGLPAEQYAI QTGQHPAVTT ENNIARYREQ LDKIGFSFDW
     SREVRTSEPD YYKWTQWIFI QLFESWYDQE AEKSRAITEL EEIFTSEGNS RINAASDDDV
     EKFSADDWNA CSEDEKEQIL LKYRLTYLAE AEVNWCPQLG TVLANDEIVN GVSERGGYPV
     VRKKMTQWSM RISAFSERLL QDLNKIDWTE SLKESQRNWI GKSVGAHVDF KIENSKFKIG
     VFTTRPDTIF GVSFMTLAPE HELVEKITTE DRKEEVQAYI EASAKRSERE RMADVKTISG
     AFTGAYAEHP FTKKPVPIWI GDYVLAGYGT GAVMAVPCGD QRDHDFARHF DLLIPNIFEN
     VDVSQEAYAG KEGTVIANSD FLSGLEYKEA LNKVILELEK TGQGYGKTNY RLRDAVFSRQ
     RYWGEPFPVY YVNGLPKMID EKYLPLKLPE VEKYLPTETG EPPLGNATDW AWDSKNNKVV
     SNKVLKQSRK LSGQHDEPNS NVTPSAVEGS DDNGIYPLEL NTMPGWAGSS WYLFRYMGAG
     NPDRFVSEEA QKYWENVDLY IGGSEHATGH LLYSRFWTKF LYDRGWLTVE EPFKKLINQG
     MILGTSAFVY RLEGENVFVS KNQINGNNVQ PIHADVSLVN SSDELDIEGF KKWRPEFADA
     KFLTEDGKYI VGREVEKMSK SKYNVVNPDE ICQDYGADTL RMYEMFLGPL EQAKPWNTAG
     ITGVHNFLKK LWKLYYDGEE FFVSDEKASA DSLKTFHKTI KKVTEDIEEF SFNTSVSTFM
     ICVNELTAQK CNSREILEPL AVLIAPYAPH IAEELWEKLG NSESVTTAKY PEFEEKYLVE
     SMKNYPVSFN GKMRFTMELS LDMSKEEIEK TVMADERTQK QLDGRTPKKV IVVPGKIVNI
     VG
//