ID A0A1F6EMV7_9BACT Unreviewed; 958 AA.
AC A0A1F6EMV7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=A3A34_04145 {ECO:0000313|EMBL:OGG74978.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_50_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798507 {ECO:0000313|EMBL:OGG74978.1, ECO:0000313|Proteomes:UP000178587};
RN [1] {ECO:0000313|EMBL:OGG74978.1, ECO:0000313|Proteomes:UP000178587}
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 -!- 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:OGG74978.1}.
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DR EMBL; MFLU01000010; OGG74978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6EMV7; -.
DR STRING; 1798507.A3A34_04145; -.
DR Proteomes; UP000178587; 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; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
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; 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; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS51462; NUDIX; 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 382..519
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT BINDING 738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 958 AA; 110021 MW; 186633F3035D096A CRC64;
MKRYDHKSIE RKWQLQWAKK KVYRSTEKKG KKKCYVLDMF PYPSGEGLHV GHPKGYIASD
IYSRFQRMRG RSVLHPMGWD AFGLPAENYA LQNKVHPRVA VKKNIARFKE QLSHIGFDYD
WDREINTTDP EYYKWTQWIF LQLFKKGLAY QSDEPINWCP SCKTGLANED LEGNACERCG
TVVEQKRLPQ WVLRITDYAD RLLADLDTLP WPEYIKELQR NWIGKSEGAL IKFQILKSKF
QIEVFTTRPD TLFGATYLTL APEHTLVQSI YASQTCVNSD EVEDYIKAAA KKSDLERQEH
KEKTGVLLEG IRAVNPATKE EIPIFVADYV LAGVGTGAIM AVPAHDERDF EFAKKYNISI
RDVIMPHLPD PTNPHQPNKE VVHRRATINI VYDPKTDRYL TLRWKKQPWI TYVTGGVENG
EDVVESARRE IAEETGYTDV RFVRKLGGDA QAEFYAAHKG VNRVARNSLL LFELASDARE
KIDPKEAEKH EVVWIPARDL TKTRFQHSEA QIITERIFSG MDAYMGEGIL IDSGEFSGTD
SAEARKKITA RFGTPKTTYK LRDWIFSRQR YWGEPIPMIH CEKCGVVPVS EKYLPVILPE
VKSYAPSGTG ESPLANITKW VNTKCPTCGG KGRRETNTMP QWAGSSWYHI AYCISENLKS
QVPNSKQSLS TKLQNKIQKW LPVDVYVGGV EHATRHLIYA RFWHKFLHDI GIVSTMEPFI
QLHTVGLVLA EDGRKMSKRF KNTIDPDDVV KLYGADTLRL YEMFMGPFEN TIAWKTESLI
GVRRFLERIW RRGQLPASSF KLPENPNLQT SLHRTIKKIT EDIAAFKFNT AISQLMIFMN
AAEKEKTIGK KQWEIFLKLL APFVPHVAEE LWSQCGGKGS IHLQKWPEYD EKFLKDETVT
IAVQIDGKVR GEVTIATRAD KVEHERAARE VVATRLQGRE VVKVIVVPNR LVNFVLRT
//
