ID A0A0G0ZET3_9BACT Unreviewed; 856 AA.
AC A0A0G0ZET3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=UV09_C0008G0030 {ECO:0000313|EMBL:KKS47164.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_42_18.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618442 {ECO:0000313|EMBL:KKS47164.1, ECO:0000313|Proteomes:UP000034320};
RN [1] {ECO:0000313|EMBL:KKS47164.1, ECO:0000313|Proteomes:UP000034320}
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:KKS47164.1}.
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DR EMBL; LCDD01000008; KKS47164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0ZET3; -.
DR PATRIC; fig|1618442.3.peg.424; -.
DR Proteomes; UP000034320; 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; 3.40.50.620; 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 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.
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 20..224
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 230..428
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 442..645
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 706..816
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 615..619
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 856 AA; 98140 MW; 1BE57D286B1D29FD CRC64;
MKATTDKYKQ TFKPGDFEKK WQSVWERDGI YQPDLKKAKK PFYNLMMFPY PSAEGLHVGN
MYAFTGSDIY GRFKRMQGFD VLEPIGLDGF GIHSENYALK IGKHPKDQAK VSQQNFYRQL
RSIGNSFAWK NTVETYDPDY YKWTQWIFTQ MFKHGLAYRK KSLVNFCPSC KTVLSDEQVI
DGRCERCKTE VEKKEMQQWF FKITSYAEKL YQNTFKESFR WSGKVKTGQR NWIGRKEGIN
ITYPVVSDSG PAKETITCFT TRPDTNFGAT FVVVGPEHPF VASLLNSIPI ESGQNSKLNE
IKNYVEKTKG KSEMERIAEG REKTGIFSGY YAINQLNGYK MPIYVTDFVL GHVGTGAVVG
VPGHDLRDFE FAKKFKLQVI RVVVGSDGDK SGIIREEQVQ EEEGMMINSE FLNGKDIHES
TRLMMDYLEK KGWGKRVTSY RLRDWCISRQ RYWGAPIPMI YCEKCNWQPV SDKDLPVLLP
DLSDWKPEGT GKGPLAKAAS FVKTKCPKCG GDAERETDVC DTFLDSSWYF LRYPSTRSGQ
VPWDPEITKK WLPVEQYTGG AEHTVLHLLY SRFIWMCFYD WGYFDFSTKG RPAFGWEEPF
ENFYAHGLII AEGAKMSKSK GNIVNPDTYI NKYGADTLRT YLMFLGPYDA GGDFRDSGIA
GMFRFLGRVW RLVTNTWDGG SKTENEKNTS QVARRDSWDG GGLRRIMHKT IKEVTEDITS
LKYNTAIAHI MEYVNAMIEN SAVSRENIKI LLLLLAPFAP HLTEELWQNL KIGDSSIHTH
PWPSYNPQYL KEDTVTVVVQ VNGKLRDSLQ VAAGEAKKQE PVEKEAMNSA KVKKYLAGRK
VKKTIFVPGR LINFVV
//
