ID A0A0G1MJB6_9BACT Unreviewed; 967 AA.
AC A0A0G1MJB6;
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=UW79_C0031G0007 {ECO:0000313|EMBL:KKT80927.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWA2_44_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619025 {ECO:0000313|EMBL:KKT80927.1, ECO:0000313|Proteomes:UP000034032};
RN [1] {ECO:0000313|EMBL:KKT80927.1, ECO:0000313|Proteomes:UP000034032}
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 -!- 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:KKT80927.1}.
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DR EMBL; LCJR01000031; KKT80927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1MJB6; -.
DR PATRIC; fig|1619025.3.peg.974; -.
DR Proteomes; UP000034032; 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; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR010662; Hydrolase_RBBP9/YdeN.
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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF06821; Ser_hydrolase; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
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}; 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 13..216
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 416..538
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 566..760
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 811..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 729..733
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 967 AA; 111216 MW; B3549F6967AA3778 CRC64;
MLKYNPSEIE KKWQRYWETK KFYDTKDSVE GKKNYMLLTE FAYPSGNLHI GHWYAFSLPD
IRARYLRMKG YNVMYPTGFD AFGLPAENAA IKNNIHPEVW TKKNITYMTK QLKSMGATFD
WSRMVSTMDP DYYQWTQWMF LKFYEKGLAY RALTSVNWCP KDKTVLANEQ AEGGKCDRCG
TEVMQKELSQ WMFKITQFAD DLVDGLKDLD WQETAKLGQI NWIGRSEGAE ISFPLTKKHK
VLIIHGYTGS PDENKYPWIK NKLEELGYEV DIPRLPNTNN PDQNEQVNYV LKNYKIDENT
ILFGHSLGAV VALKVLEKVG KPIAKLVLGA MAMDPGATDS RLKNDPRPNW RNFSWDFDFE
KIKKLTYEVV VLSDLKERKR IFFMKYLSEK LSARLIEGHS VKEHFTGPTE PMILNNLINS
IKVFTTRPDT IFGATFLVVS PEMAQKWINT HGDLAPPEVK KYVQDSLKKT ELQRQENREK
TGVDTRAKAI NPATGKEIPI WVADYVLGHY GTGAIMAVPS HDERDRAFAE KFSLPISDAP
LRDKSEIMKL LKDKGVGMPH KTYRLHDWIL SRQRYWGVPI PMINCKTCGY QPVPEKELPI
KLPPLKDFKP ADDGRSPLAK AEKWLKVKCP KCGNDAERET DTMDTFVDSS WYFMRYTDPK
NKKEFASKKN MANWLPVPMY SGGAEHTTMH LLYSRFIAKA LHSLGYVDFN EPFLSRMNRG
IILGPDNQKM SKSRGNVIDP DVEVKKYGAD AVRMYLAFMG PYEQGGPWSP GGINGVYRFL
NRIWYLVSGI SYNKDKNGGN SNEYRDLDIA IHKAIKNIGD DIEKLAFNTC VSELMKLLNA
FEQAARDGYK IQNTKYKILL LLLAPFAPHL AEELWQTVLK NKKSIHLESW PEYNQEMLSE
EKIKLVVQVN GRLRDTLDVK RGISENEAKE LALKSENVKK HIEGGVKKVI YVKDRIINLV
VGIDLTK
//
