SYL_COXB2
ID SYL_COXB2 Reviewed; 820 AA.
AC B6J1B2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CbuG_1438;
OS Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434923;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuG_Q212;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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; CP001019; ACJ18740.1; -; Genomic_DNA.
DR RefSeq; WP_012570259.1; NC_011527.1.
DR AlphaFoldDB; B6J1B2; -.
DR SMR; B6J1B2; -.
DR KEGG; cbg:CbuG_1438; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
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 Gene3D; 3.90.740.10; -; 1.
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; 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; 2.
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.
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..820
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091310"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 820 AA; 94273 MW; 06B683979B235DCF CRC64;
MNESYQPTLI EQLAQEYWEE NETFEVKEDL SREKFYCLSM LPYPSGDLHM GHVRNYTIGD
VIARYQIHKG RNVLQPMGWD AFGLPAENAA IQRELPPAEW TRKNIKKMRK QLKQLGFAYD
WSREITTCDS TYYRWEQWLF LQLYKKGLAY KKNAIVNWDP VDQTVLANEQ IVDGRGWRSG
AVVERREISQ WFLKITDYSE ELLKDLDELK EWPEQVITMQ RNWIGQSQGV IINFNLEKGP
DKLQVYTTRP DTLMGVTYLA IAPEHPLAKE RAKKSKKIAA FLKKCKQTRV AEADIATQEK
EGIDSGLFAV HPLSKEKLPI WIANFVLMEY ASGVVMAVPA HDERDHEFAL KYDLPLKPVI
EPADGHDWDY NQAAYTNPGK LINSGSFNDI DSKTAFNLIA DYLKNNGAGS RQTHYRLRDW
GISRQRYWGT PIPIIYCKTC GTVPVPENQL PVLLPEDIIP TGHGSPLKET ASFYKTRCPV
CNKPATRETD TMDTFVESSW YYARYSCPDQ DKVMLDDRAK YWTPVDQYIG GIEHAVMHLL
YARFMHKILR DLGLLNSNEP FIRLLTQGMV LKDGAKMSKS KGNVVTPQSL IKKYGADTVR
LFIIFAAPPE QDLEWSDSGV EGAYRFLKKL WGFSYRIKDA LLAINQQKER SNYQWEAPEH
RQTRQQIHEC LQQANIDMER LQFNTVVSAV MKILNILIKL TTDNDAEAHL IREGTGILLR
LLSPITPHIS HHLWQSLGFG GDILDTPWPR PDPKALQTTE LELIVQINGK LRGRIQVPTE
ASKEIIESTA LNQENVQRHL ADKKIKKVIV VPKKLINIVV
