SYL_LEPIC
ID SYL_LEPIC Reviewed; 863 AA.
AC Q72UY6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=LIC_10517;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS69138.1; -; Genomic_DNA.
DR RefSeq; WP_001199946.1; NC_005823.1.
DR AlphaFoldDB; Q72UY6; -.
DR SMR; Q72UY6; -.
DR PaxDb; Q72UY6; -.
DR EnsemblBacteria; AAS69138; AAS69138; LIC_10517.
DR GeneID; 61143872; -.
DR KEGG; lic:LIC_10517; -.
DR HOGENOM; CLU_004427_0_0_12; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000007037; Chromosome I.
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; 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.
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..863
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152035"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 635..639
FT /note="'KMSKS' region"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 99567 MW; E38A638C81C6E644 CRC64;
MQYPFQEVES FWQKFWEEHK SFQTNIRSSK PKFYCLDMFP YPSGAGLHVG HPEGYTATDI
LSRFKRMKGF EVLHPMGWDA FGLPAERYAM QTGIHPAITT KDNIDNFRRQ IQMIGLSYDW
SRELSTTDPD YYKFTQWIFI QLYQSWFNPE LKKAESINEL IRRFSNQGSN GLDYRQFNSE
EWKNFSPVEK EKILSDFRLV YQAEIPVNWC EALGTVLANE EVEEWVGKGY EVVRKPMRQY
MMRITAYADR LLEDLELVEW PPSTLEMQKN WIGKSEGLEI TFPFLKPLQS GLEGIRIFTT
RPDTIFGVTY MVVAPEHPIV SEITTPEQKQ KVEEYQKTSS LKSDLDRMEL NKEKTGVFTG
TFVFNPADPS QKIPVWISDY VLYGYGTGAI MAVPAHDQRD FEFARTFGLK IIPVIEGEIS
EAAFDSKTST CINSSSSEIS INGLDYTSAS SKIISWAESK KIGRKKIQFK LRDWLFARQR
YWGEPIPLVH YPSGVTKPIP ESELPLVLPN LEEFKPSGTG ESPLALAKDW LQYKDPSTGE
IGTRETNTMP QWAGSCWYYL RYIDPKNGRF LCDPELEKKW MPVNLYVGGS EHAVLHLLYS
RFWHKFLFDI GAVSTKEPFD KLIHQGLILG EDKRKMSKSL GNVVNPDDVI KEYGADSLRL
FEMFMGPLEM VKPWSTRGVE GVFRFLNRIW RLFHSGSQES FRLDDVEPTP EELKILHKTI
QKVNEDIPNF SFNTAIAQLM IFVNEFTPSD RRPKKVLESF ILLLAPFAPH IAEELWKRSG
KMESLSYEKF PEADPQYLVE SEILIVVQVN GKLRDEFKAP KDVSQSDAIS MAKNLDKIKG
ILEGKTIRKE IYVPGKLVNL VIG
