ID A0A0G1FMM1_9BACT Unreviewed; 931 AA.
AC A0A0G1FMM1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=UV63_C0042G0008 {ECO:0000313|EMBL:KKS88118.1};
OS Microgenomates group bacterium GW2011_GWC1_43_11.
OC Bacteria.
OX NCBI_TaxID=1618520 {ECO:0000313|EMBL:KKS88118.1, ECO:0000313|Proteomes:UP000034204};
RN [1] {ECO:0000313|EMBL:KKS88118.1, ECO:0000313|Proteomes:UP000034204}
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 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:KKS88118.1}.
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DR EMBL; LCFF01000042; KKS88118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FMM1; -.
DR STRING; 1618520.UV63_C0042G0008; -.
DR PATRIC; fig|1618520.3.peg.974; -.
DR Proteomes; UP000034204; 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; 3.
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; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 2.
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; 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 53..195
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 234..426
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 441..497
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 644..728
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 780..899
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 700..704
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 931 AA; 105679 MW; 49DAF935E5C839CD CRC64;
MGVFIIGSMD DPRKFRYDHQ TIEAQWQGVW AQTSLDVADV ESAKRPFYNL MMFPYPSAEG
LHIGNMYAFI GSDIYGRFQR MRGYDVFEPI GLDGFGIHSE NYALKIGRHP MDHARITQKH
FYDQLHRIGA MFDFTRTLET YDSTYYRWTQ WLFVQMFKAG LAYRAKAQVN FCPSCKTVLA
DEQVIESKCE RCGNAVEKRA LEQWFFKITA YAEKLLGNIP KLKWSEKVKI AQTNWIGKKE
GINIIYQVAD EKGKPLGKEI VCFTTTPVNF ATTFIVIAPE HPLITDMLRV IDKEQALKIT
NYVEQAKKKS QQDRIAEGRK KTGVFSGLYV INHVTGEKIP VWITDFVIMS VGTGAVQGCP
GHDLRDFDFA MQFHIPIKRV VVGPDGDTSE ITRREQVIEH GPGKMVNSGF LDGMGFADAM
QKTMDYFVEK GWGKRAVTFH LRDWLISRQR YWGPPIPMIY CASCGKEGKT WDITEDAMAR
EARNSKHEAR NKSKNQISND QNYFGFRISD FGFPASMAGW YPVPEDQLPV LLPRIEDYKP
SADGIAPLSK HKEFFDTVCP YCGKPAVRET DVSDTFLDSS WYFLRYPSLH SHFSAVANEK
FDPSSVASSN TPSARVAESS EAGQNFVRFP QNADVVPFIP EITKKWLPVN MYTGGAEHSV
LHLLYSRYIT MVLHDLGYVD FDEPFTNFFA HGLIIKEGAK MSKSKGNIVN PDDYIAKYGS
DAVRLYLMFI GPFSMGGDFR DTGMEGMARW VGRVWRIIQN SLIPLPAPPP SLPRKSPESI
IHLLEKTIAK LTDDMEKRRY NTAIASLMEL TNAIMDAGGA LGQEELQKYI LLLAPFAPYL
SEEAWNLLNG RTLYTDPSDS VHRQSWPSCD PTILEEEEIS FIIQVNGKLR DMLSVHPSDA
KNQTLVEEKH LSGKTVINTI FIPGKLINFV L
//
