SYL_EHRRW
ID SYL_EHRRW Reviewed; 830 AA.
AC Q5HBM8; Q5FE96;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=Erum3010, ERWE_CDS_03070;
OS Ehrlichia ruminantium (strain Welgevonden).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=254945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA Allsopp B.A.;
RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT tandem repeats of actively variable copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(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; CR767821; CAH58018.1; -; Genomic_DNA.
DR EMBL; CR925678; CAI26801.1; -; Genomic_DNA.
DR RefSeq; WP_011154983.1; NC_006832.1.
DR AlphaFoldDB; Q5HBM8; -.
DR SMR; Q5HBM8; -.
DR STRING; 254945.Erum3010; -.
DR EnsemblBacteria; CAI26801; CAI26801; ERWE_CDS_03070.
DR KEGG; eru:Erum3010; -.
DR KEGG; erw:ERWE_CDS_03070; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR BioCyc; ERUM254945:ERUM_RS01650_1-MON; -.
DR Proteomes; UP000001021; 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 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; 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; 2.
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.
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..830
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334755"
FT MOTIF 34..44
FT /note="'HIGH' region"
FT MOTIF 592..596
FT /note="'KMSKS' region"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 830 AA; 95353 MW; 255DC2566DEC9A19 CRC64;
MHYNFKEVER DVQEKWDFTV NVKDVQCYVL EMFPYPSGNI HMGHLRNYTI GDVIARYKRA
CGLHVFHPIG WDAFGLPAEN AALSYNISPQ VWTRKNIDNM RSQLKSIGLS YNWDKEFATC
DAEYYKYEQE FFLDFLKYGL AYRKESLVNW DPVDQTVLAN EQVIDGRGWR SGAIIEKRKL
SQWFLKITDF AAELLDDLKS LNQWPEKVKL MQERWIGKSE GVIIDFQIVG INEVLQVFTT
SPHTLFGASF IAVSFDHPIL KYVNDVQLIQ LIDNFDRKDL IDESSINTVE KFGINSGLVA
RHPLLDVDLP IYVANFVLMN YGTGAVFCCP AHDQRDFDFA KKYSLPIRQV IFPEQNVDLE
QEAYVGSGIM GCSGFLDGMT VDDAKKSMIE KLISLGICKK QVYYRLHDWG ISRQRYWGCP
IPIIYCKKCG IVPVDKKDLP ITLPEDIDFT KSGNPLDNHP TWKYTKCPSC GADAKRETDT
FDTFFESSWY FAAFCGIGKG IDKDVCNKLL PVDYYIGGIE HAVLHLLYSR FFCRALTRCG
YFDVKEPFSS LITQGMVCHS TYLDKYGNYL FPEDGKKMIQ EGKYVTVGRA EKMSKSKKNV
VHLDDIIDKY GADSARLFIL SDTPPERDIE WLDENIEGVS RYLNKLWKMI VDYDQLEQNF
VCDNISSDTL EYRINVHKIL NDITNDLEFY RFNCAVAKFR ELSNVISEMI RLSINHHVVS
EAIYILIRVV EPFIPHIAEK LWQIVGGQGM LCNQLWPKVD PQLLIKKNVN IVVQVNGKFI
KAVSVPNDID DDTLKSIALE VAQRRIGNSS VKNIYIIPGR VINIVITKSS
