ID A0A1F8B7B7_9BACT Unreviewed; 890 AA.
AC A0A1F8B7B7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2892_00885 {ECO:0000313|EMBL:OGM59830.1};
OS Candidatus Woesebacteria bacterium RIFCSPLOWO2_01_FULL_39_10b.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802517 {ECO:0000313|EMBL:OGM59830.1, ECO:0000313|Proteomes:UP000176404};
RN [1] {ECO:0000313|EMBL:OGM59830.1, ECO:0000313|Proteomes:UP000176404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:RU363035}.
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:OGM59830.1}.
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DR EMBL; MGHD01000013; OGM59830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8B7B7; -.
DR STRING; 1802517.A2892_00885; -.
DR Proteomes; UP000176404; 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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 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: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 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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 241..428
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 590..678
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 731..850
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 650..654
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 890 AA; 102600 MW; 59BD71C5BAEC1012 CRC64;
MRFKHKKIER KWLGKWLKDG IYYPSKMVGK RKKFYNLWMF PYPSAEGLHA GHAFASTGSD
VYGRFMRMKG YEVFQPIGYD SFGIHSENFA IKVGKHPKEF ICKTTKNYEN QLKSLGHAYD
WTRTVTTSDI DYYRWTQWLF VQMFKAGLAY RKKSEVNFCP SCKTVLADEQ VMTPAQAGKI
PVGFKSMEEV SEGTYICERC ASIVEKKDLE QWRFRITDYA DKLLDGLDRI DWPEKIKIAQ
RNWIGKKDGI TITYPVKESD LTISCWTSRP DTNFGATFVA ISPEYKDVLR LTTKENRGKV
TEYIKKAKSK SEDEKIEQGK EKTGVFTGLF AINHLTGKEM PIWVTDFVLF DVGTGAVVGV
PGHDRRDFEF AEKYDLKIIR VVVGSDGDIS PIIQVEQVQE EEGMMINSGF LNGMDTHKAT
RKIIDYMESE GQGVRTTSYH LRNWIISRQR YWGPPIPMIY CKACAKESMS WFTFKDDTSK
REALRKDQSD WVHAGWYPVD EAKLPVNLPD IKDYIPKGEG RGPLADHPEF YQVACPECGL
PARRETDVSD TFLDSSWYFL RYPSVGAKRV GLRQDNLQPT THKLQLPWDE KITKKWLPVD
LYFGGAEHAV LHLMYARFVT MVLNDLNYLE FDEPFPRFFA HGLMIKDGAK MSKSRGNVVN
PDEYIEKYGA DTLRLYLMFM GPMDGYPDFR DTGIEGMRKF VERVWDLFQN SQFITHPSTA
LRTSNSQLSI KMHQTIKKVT EDIEKFHYNT AISSIMEYVN ALRAQTQKSL PAQAKKLITD
NLKALALMLA PFAPHLAEEV WVNVLGQKFS VHKASWPEYD PELIVEETVE IPVQVNGKLR
ATLTVDRVQS TYKKKVVELA KEDRKIAKWL AGRKIKREVF VPGKLVNFVV
//
