ID A0A0G0K9B8_9BACT Unreviewed; 829 AA.
AC A0A0G0K9B8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=US98_C0044G0004 {ECO:0000313|EMBL:KKQ76243.1};
OS Parcubacteria group bacterium GW2011_GWC1_38_6.
OC Bacteria.
OX NCBI_TaxID=1618898 {ECO:0000313|EMBL:KKQ76243.1, ECO:0000313|Proteomes:UP000034446};
RN [1] {ECO:0000313|EMBL:KKQ76243.1, ECO:0000313|Proteomes:UP000034446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ76243.1}.
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DR EMBL; LBVB01000044; KKQ76243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0K9B8; -.
DR PATRIC; fig|1618898.3.peg.481; -.
DR Proteomes; UP000034446; Unassembled WGS sequence.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 38..181
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..415
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 430..640
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 678..787
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 279..306
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 605..609
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 829 AA; 95570 MW; 4550351E7226F3AB CRC64;
MKYNPEAIEK KYQEVWDKNQ AFKAENYSKK PKFYTLVEFP YASGSGLHVG HCRSYIALDV
ISRKKRMKGF NVLFPMGWDA FGLPTENYAI KTGTHPVVVT KENTDNFKKQ LQSLGFSFDW
SREINTSDPS YYKWTQWIFI QLFKKGLAYK AKIPINWCPS CKIGLANEEV IAGNCERCGT
KVIQKEREQW LLKITKYADR LLEDLEKVDY PERVKVAQKE WIGKGDGWNI KFQIKDSKDQ
IEVFTTRIDT LFGTTFLALS PEHPIIEKLK DQILNLKVVD KYRNDLKNKK QNKDQKENAK
SGIELRGVVA INPANDKEIP VFVADYISMQ YGKGAIMAVP CHDQRDFEFA RSHNLAFMEV
IEPYQAHRTL PQKAPWITTG GQFELPYEGE GFLINSGRFD GLPSHGARIR IGEWLTKKTG
KIAEKVTCYK LRDWIFSRQR YWGEPIPMVY CKKCASLPAG QGWVPLKESD LPLELPDIKE
YKPTDEGDSP LAKIKKWTNL ACPKCGSAAR RETDVMPNWA GSNWYYMRYC DPSNDKKFAD
PKLLEYWLPV DWYNGGMEHA TLHLLYSRFI YKFLWDIGAV PKSLGPEPYK KRTSHGIILG
EGSVKMSKSK GNVIDPVKIA KEFGTDTLRV YQMFMGPYEQ MIPWDVKGVK GARRFLEKVW
DIAEKNIEYL KDKTALSIEK ALHRTIKKIT GDIDNLKFNT AVSFLMEFCN SWKDSGSYLN
KKDLGSFLKI LYPFAPHISE ALWEKAGFEG LCIAQSWPKY DKTLAQPEKI VLILQVNGKM
RDKLEIDGEI TEVELKELVL SKENIKKWIK GKEVKKVVFV PQKLMNIVV
//
