SYL_EHRRG
ID SYL_EHRRG Reviewed; 830 AA.
AC Q5FHG5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=ERGA_CDS_03010;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
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; CR925677; CAI27753.1; -; Genomic_DNA.
DR RefSeq; WP_011255458.1; NC_006831.1.
DR AlphaFoldDB; Q5FHG5; -.
DR SMR; Q5FHG5; -.
DR EnsemblBacteria; CAI27753; CAI27753; ERGA_CDS_03010.
DR KEGG; erg:ERGA_CDS_03010; -.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; ERUM302409:ERGA_RS01550-MON; -.
DR Proteomes; UP000000533; 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_0000334754"
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; 95394 MW; 39F0E588B3039040 CRC64;
MHYDFKEVER 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 LIDSFDRKDL IDDSSINTVE KFGINSGLVA
KHPLLDMDLP IYVANFVLMN YGTGAVFCCP AHDQRDFDFA KKYSLPIRQV IFPEQNVDLE
REAYVGSGIM 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 VDYDQIEQNF
VFNDISNDAV EYRMNVHKIL NDITNDLEFY RFNCAVAKFR ELSNVISEMI RLSINHHVVS
EAIYILIRVV EPFIPHIAEK LWQIVGGQGM LCNQLWPKVD SQLLIKKNVN IVVQVNGKFI
KAVSVPNDID DDTLKSIALE VAQRRIGNSS VKNIYIIPAR VINIVITKSS
