ID A0A0G0D8K9_9BACT Unreviewed; 845 AA.
AC A0A0G0D8K9;
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=UR95_C0001G0141 {ECO:0000313|EMBL:KKP90614.1};
OS Parcubacteria group bacterium GW2011_GWC1_36_108.
OC Bacteria.
OX NCBI_TaxID=1618894 {ECO:0000313|EMBL:KKP90614.1, ECO:0000313|Proteomes:UP000034191};
RN [1] {ECO:0000313|EMBL:KKP90614.1, ECO:0000313|Proteomes:UP000034191}
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:KKP90614.1}.
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DR EMBL; LBRD01000001; KKP90614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0D8K9; -.
DR STRING; 1618894.UR95_C0001G0141; -.
DR PATRIC; fig|1618894.3.peg.150; -.
DR Proteomes; UP000034191; 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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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}; 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 12..208
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 220..369
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 457..661
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..806
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 845 AA; 97302 MW; 8D7B98691F10E69B CRC64;
MEKYIPSDIE KKWQKYWEDN GTYKNYSREK KFYALDMFPY PSGVGLHVGH PKGYIATDVV
SRFKMLNGYS VLHPMGWDAF GLPAENYAIK NKTNPNIFTA KSIANYKKQL EMFGFTYDWD
REINTTDPQY YKWTQWIFLK LFEKGLAYES NAPINWCPSC KTGLSNEDLE DGKCERCGSE
VEQKPMRQWV LKMTDYADRL LYDLDSSELD WEDMIVDQQK NWIGRSEGVQ FEMKIKDSDE
KIEVYTTRID TAFGITYAVV APEHPIIEKL KDKISNYAEV AQYVADANKK TNLERTELQK
EKTGKKLEGI NVINPFTNEA VPLFVADYVI GGYGTGAVMA VPAHDERDFE FANKKELQIK
YTIIPEYGRN RKPLLGKPDG QTYEGIEMLK AQILNDTNDE CIRSILASQI ISKRAYTVDG
ILINSGSYSI LTSKQAREKM ADWLEKEKIG KRKVNYKMRD WVYSRQRYWG EPIPIVHCEK
CGAVAVPEQQ LPVMLPDVEN YEPTGTGESP LAAITDWVNT ICPKCGGPGK RETNTMPQWG
GSSWYYLRYI DPKNDKELVN KELEKEWMPV DLYVGGAEHA TRHLLYARFW HKFLYDIGVV
STIEPFKKLL HVGLIMAEDG RKMSKRWNNV VNPDEIIGEF GADAMRLYEM FMGPFTQSIA
WSTSGVSGVR RFLDKVWNLQ EKTTIDNIAS DKKITSLLHK TIKKVTEDIE NFRFNTAISA
MMILVNAMEK EPSISVSHYE TLLTLLSSFA PHITEELWEK IGHKESIFLQ DWPKVDEKYL
QDEEIEMVVQ VNGKVRERLM VANDVTEDEA KETALESDKV KVFTDGKEIK KIIFVPGKLI
NIVVI
//
