ID A0A212DYT4_9BACT Unreviewed; 845 AA.
AC A0A212DYT4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=US76_03860 {ECO:0000313|EMBL:OWK27478.1};
OS Parcubacteria group bacterium GW2011_GWA2_38_13b.
OC Bacteria.
OX NCBI_TaxID=1618780 {ECO:0000313|EMBL:OWK27478.1, ECO:0000313|Proteomes:UP000034916};
RN [1] {ECO:0000313|EMBL:OWK27478.1, ECO:0000313|Proteomes:UP000034916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW2011_GWA2_38_13b {ECO:0000313|EMBL:OWK27478.1};
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).
RN [2] {ECO:0000313|EMBL:OWK27478.1, ECO:0000313|Proteomes:UP000034916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW2011_GWA2_38_13b {ECO:0000313|EMBL:OWK27478.1};
RX PubMed=28067254; DOI=10.1038/srep40101;
RA Castelle C.J., Brown C.T., Thomas B.C., Williams K.H., Banfield J.F.;
RT "Unusual respiratory capacity and nitrogen metabolism in a Parcubacterium
RT (OD1) of the Candidate Phyla Radiation.";
RL Sci. Rep. 7:40101-40101(2017).
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:OWK27478.1}.
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DR EMBL; LBUF02000001; OWK27478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212DYT4; -.
DR STRING; 1618780.US76_C0009G0013; -.
DR Proteomes; UP000034916; 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; 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; 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 16..222
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 224..423
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 429..644
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 689..802
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 616..620
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 845 AA; 98131 MW; 1E8142CBFAEE51C5 CRC64;
MPNREKNEKV LKIEKKWQKR WGEAHLYEPD LDEAKKPFYN LMMFPYPSAE GLHVGNVYAY
TGSDIYGRFQ RLKGNDVFEP MGFDAFGIHS ENYARKIGKA PKETIEKNVK NFHKQLDRLG
MMFDWSREIN TTHPEYYKWN QWLFLQLFKK GLAYKKEAPV NWCSSCETVV ADAMAIDNKC
ERCGTEITQK KISQWFFKIT DYAERLLKDH EKIDWSERTV KAQKEWIGRS EGIEIKFLIF
SLKADPAQWR DNSQFSIDIF TTRPDTLFGA TYVVLAPENQ IISNLKSQIL NFDEVNEYIE
KSAKKTKEER IKEGGEKTGV ELKGIKAVNP ATGKEISVWI SDYVLAEYGT GAVMAVPAHD
QRDFEFAKKF GLPIKQVICL NWPKKNCPIL DKAYEGEGNL IDSGQFSETH SLDAIKKITE
WLEKENIGKK EIKYHLRDWL ISRQRYWATP IPIIYCDKCL ENRKNTELTT VDGKEYAIVP
VPEKDLPIEL PLKKDFSVLS KGKSPLAEIE SFVNTICPDC GGKAVRETDT MDNFIDSAWY
YFRYISTEFN DRPFDKKRAK KWLPVNMYIG GHEHANLHLL YTRFITKVLY DLKFIDFDEP
FKKFRANGLL VREGAKISKS KGNIINPDNY VDRYGADTLR MYLMFLGRYE EGGDFQDGGI
VGIERFLNRV QDLVGIFLKQ ENTDKNSPIL KERHKTIKKV TEDIESLQFN TAIASLMEFI
NVAQEKNITK EDIEALLILL APFAPHLTEE LWSQIYPEQY EKDAKYSVHN QKWPGYDIEL
TKEKTFDMVM QINGKMRGIF NAEIGISEDE AKEIAFQNNR IQPYIAGKNI KKIIFVKNKL
INIVL
//
