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SYL_SORC5
ID   SYL_SORC5               Reviewed;         854 AA.
AC   A9EYY7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=sce7417;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(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; AM746676; CAN97586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9EYY7; -.
DR   SMR; A9EYY7; -.
DR   STRING; 448385.sce7417; -.
DR   PRIDE; A9EYY7; -.
DR   EnsemblBacteria; CAN97586; CAN97586; sce7417.
DR   KEGG; scl:sce7417; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; DIDWADV; -.
DR   BioCyc; SCEL448385:SCE_RS37990-MON; -.
DR   Proteomes; UP000002139; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..854
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334822"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           69..80
FT                   /note="'HIGH' region"
FT   MOTIF           633..637
FT                   /note="'KMSKS' region"
FT   BINDING         636
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   854 AA;  95563 MW;  0D0B4545E599E4D8 CRC64;
     MARRDMAAET MDPRASTEPS PNEPREPARY DHAAVEPRWQ RAWEEGETFR AVRSADPARG
     KRYVLDMFPY PSGSGLHVGH PEGYTATDIM SRYFRMRGID VLHVMGWDAF GLPAEQHALE
     TGTHPADTTA RNIATFKRQL KMLGFSYDWS RELSTTDPRY VRWTQWIFLQ LFKKGLAYQD
     EVSVNWCPAL GTVLANEEVI DGKSERGSHP VYRTPLRQWM LRITAYADRL AEDLRLLDWP
     EGTVAMQRSW IGRSEGALIT FEVKGWGKGA LSVFTTRPDT LMGVTYVVLA PEHPLTTWLT
     SAESGASEPR REAVRAYVAA AAGKSDRERL AAAAREKTGV DTGLVAVHPI TGVEVPIWVA
     DYVLGGYGTG AVMAVPGHDE RDFSFARTYG LPIVEVVSPD GSLHDQLEAA YVDPGVAVRS
     GEFDGLATEE CKRAVIARLE ALGRGKREVN YKLRDWVFSR QRYWGEPIPI YFPVELADPQ
     GDPRKGAAHT IRYDQPIAVD EASLPIELPP LADFRPGDDP AGPLARAVDW RFFQRDGKWY
     ARETNTMPQW AGSCWYYLRF LDPQNDAEPF SEAAYDAWMP VDLYVGGAEH GVLHLLYARF
     WHKVLYDLGH VKHPEPFAKL VHQGMILGED NEKMSKSRGN VINPDDIVRA HGADVLRMYE
     MFMGPLEAVK PWQSGQIQGV VRFRDRVFAT CTRPLSDAMD DATSRQLHRT IKKVTGDIEG
     MAFNTAISAM MVFVNHLSSL PSPPREAVLR LILLVSPFAP HLAEELWRLT GHERSLSYEP
     WPTYDEAFCV DDVLEIPVQV NGKVRGRVML AKAASEEEAR AAALGLETVA ALAAGKQLKK
     FIYVAGKIVN IVVG
 
 
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