SYL_PSELT
ID SYL_PSELT Reviewed; 815 AA.
AC A8F8B7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Tlet_1847;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000812; ABV34401.1; -; Genomic_DNA.
DR RefSeq; WP_012003877.1; NC_009828.1.
DR AlphaFoldDB; A8F8B7; -.
DR SMR; A8F8B7; -.
DR STRING; 416591.Tlet_1847; -.
DR EnsemblBacteria; ABV34401; ABV34401; Tlet_1847.
DR KEGG; tle:Tlet_1847; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002016; 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; 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; Reference proteome.
FT CHAIN 1..815
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000071114"
FT MOTIF 41..51
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 815 AA; 94816 MW; FE81700E65574478 CRC64;
MPRYEPQEIE SKWQKFWEKE GLFKTPQHSD LPKYYMLVMF PYPSGTLHVG HVKNYVIGDA
VARYKRMRAY NVLHPFGYDA FGLPAENAAI ERKIHPKDWT LNNINIIRRQ IKKLGISYDW
NREVITCLES YYKWTEWIFL KLYEAGLAYK KKAAVNWCPK CMTSLANEQV KDGRCERCDT
PVTIKHLEQW FFKITDYAER LLKDLDKLTG WPEHVKTMQR NWIGESKGAK ISFKVEESEM
NIEVFTTRPD TLWGVTFMVL APESDLVNHI TLPELKGELE KFLNYVGQQD RHKRGSADVE
KEGFFTGRYA INPVSGERIP IYVANYVLME YGTGAVMGVP AHDQRDYEFA VKYNLPIKEV
IKPSEDIPKN RAYDGPGIMV NSGPLNGTVV PEGIERVIQW LEERGIAKRS VQYKLRDWLI
SRQRYWGAPI PIVYCEKCGM VPVPEKSLPV QLPYDVEFLP TGQSPLMLND EFRKTSCPKC
GGPALRDADT MDTFVDSSWY FLRYVNPDRD DVPFVKEDVD HWLPVDQYVG GVEHAVLHLL
YSRFITKVLY DLGYLSFDEP FENLFTQGMI YKDGAKMSKS KGNVVSPDEM IDRYGADTLR
MYILFMGPPE RDAEWNDAGI EGVYRFIRRA WSLMDQIISL PDNQNQVFAE EEKHLRRKLH
ISLRKVTQDM EGGFKFNTVV SSLMELVNDA YDYIDNLPQH RWNIKLLKEL AKNFVLMISP
FAPHFAEELW QRMGYSSSVM KEKWPEYDPD ALVVEEVEIA IQVNGKLRDK VKIPVDATED
QIKEIALKSE KVRKYISDEP KKIIYVPKRL LNIIF