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Database: UniProt
Entry: A0A0G1IKF5_9BACT
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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
//
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