SYL_RICTY
ID SYL_RICTY Reviewed; 828 AA.
AC Q68WV8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=RT0407;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(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; AE017197; AAU03884.1; -; Genomic_DNA.
DR RefSeq; WP_011190868.1; NC_006142.1.
DR AlphaFoldDB; Q68WV8; -.
DR SMR; Q68WV8; -.
DR STRING; 257363.RT0407; -.
DR EnsemblBacteria; AAU03884; AAU03884; RT0407.
DR KEGG; rty:RT0407; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000604; 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; 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; 3.
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..828
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152076"
FT MOTIF 36..46
FT /note="'HIGH' region"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 828 AA; 96495 MW; 5981B26469952B26 CRC64;
MHKIEQKWQK IWKEEKAFQV SNDSSKPKYY VLEMLPYPSG KIHIGHIRNY SIGDVIARFM
TMQGFNVLHP MGWDAFGLPA ENAAIQNNSR PQDWTYSNIE YMKKQLQSMG FSYDWTREIN
SCDPQYYKHE QKFFLELYDR DLVYQKESLV NWDPVDNTVL ANEQVVNGRG WRSGAIIEKR
YLNQWFLKIT NYAEELLNEI QNLKDWPEAV RVMQEEWIGK STGVNFHFKI KYHENSTIEV
FSTKPETIFG ASFIGIAFNH PIIEQLIFKT DEIANFITKC SYITKSSELE KSEKEGVFTG
LYVIHPFDAN IILPVIITNF VLMDYGTGAI FGCPAHDKRD HELAMKMNLP IKKVIGTDNT
QEEVLINSDW LNGLTSSEAK QKVISKFETL GIGKRSVNYR LKDWGISRQR FWGCPIPIIY
CETCGIVPVP YKDLPVTLPD DVSFDNNYNP LEHHPSWKHV NCPKCDNHAI RETDTFDTFF
ESSWYFTRYC NNNAVEMTDS KACNYWLPVD KYIGGIEHAV MHLLYARFFT KLMNEHHYVS
IREPFKGLFT QGMVLHATYK DENNNWLYPA EVVKNGNEFF HKETNTRVVQ GRIEKMSKSK
KNIIDLETIQ EQYSADAIRL FVLSDSPPEK DLQWSASGIE GCSRFIHKLD NMFEVISSLK
DDMNNEINTE LNRLIHFTIK HVADDIKTFS LNRAIARMRT LTNAIYCEIS KDKIDVRTIK
YGFNVLIQLL NPFIPHITEE IWQKLGNKER LYKSVFAEFD DSMLEFSTYI MAVQVNGKLR
DTYEFNTDIS EDEVKQITVN LPKIQKFLAG KEPNKIILVP RKIVNIII
