ID A0A0G1IKF5_9BACT Unreviewed; 957 AA.
AC A0A0G1IKF5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
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=UW53_C0006G0023 {ECO:0000313|EMBL:KKT59876.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWA1_44_25.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618645 {ECO:0000313|EMBL:KKT59876.1, ECO:0000313|Proteomes:UP000034087};
RN [1] {ECO:0000313|EMBL:KKT59876.1, ECO:0000313|Proteomes:UP000034087}
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:KKT59876.1}.
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DR EMBL; LCIR01000006; KKT59876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1IKF5; -.
DR PATRIC; fig|1618645.3.peg.515; -.
DR Proteomes; UP000034087; 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 CDD; cd02883; Nudix_Hydrolase; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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-RELATED; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00293; NUDIX; 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; SSF55811; Nudix; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 378..519
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 725..729
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 957 AA; 110079 MW; 5F6364235124539B CRC64;
MPYDHKKIEK KWQKEWEKSK IYETNDQPKA DWPRARNFYV LVEFPYPSGN LHTGHWYAFS
VPDIFARKKR MEGKNVLFPI GFDAFGLPAE NAAIKRGLNP KKWTYGNIDY MRKQIKSMGA
SFDWSREVIT SDPEYYKWTQ WIFLQFFKKG LAYQAETSVN WCPKDKTVLA NEQIVGGCCE
RCGAEVEQKQ MKQWMLKITN YADRLLFGLD KLNWKEEIKE AQRNWIGKSE GAEIEFRIKN
LEFKIKVFTT RPDTLFGATY MVLAPEHPLI SNLKPLISNL KEVERYIDVA KKKTQLQRQK
AEKEKTGVEL KGIKAVNPAN KEEIPIWVAD YVFMGYGTGA IMAVPAHDQR DFEFAKKFGL
QTRTVVEPVT GELRENEEFR KSIVAVVEDS KTGKFLSINW GPKLGGNLFV GGGIDGAENY
EAAACREIQE ETGYKNLKLV SVSEKIHHHY VAFSKNVNRN INATGLHFQL LNNEKTPPRL
ENTEKEKFSL EWLSKTEVLD KVKDQLHSLV FRRLILGEAY AGSGIMVNSG KFDGMDSEKA
KKTITEFVGG EIKTQYRLRD WVVSRQRYWG APIPIIYCLK DGALAAPEKD LPVLLPEIKD
YKPRSDGKSP LAKAEKWLKV KCPKCGSVAE RETDTLDTFV DSSWYFLRYC DPKNEKEFAQ
KRKMENWMPV DLYSGGAEHT TMHLLYSRFW YEAMFDSGLI PKELGDEPYK DRRNRGIILG
PDGQKMSKSK GNVIDPDEYV AKFGADTVRM YLAFIGPYNE AGSYPWNPQG ILGIRRFLDR
VWKFASPRGK TLGVFRDSTP SVEERGDFAR ALNKTIKKVG EDIEEFHFNT AVSALMVLLN
EMEKVGASSE NFSVFLKLLA PFAPHLAEEL WSRLGNKASI HFEPWPKYDP KLVEENTFEL
IIQINGKVRD KFEVPVNISQ SEAERLTLAR EKVKLALENR KPRKIIFVPR RLVNIVV
//