ID A0A2U1JTK1_9BACI Unreviewed; 805 AA.
AC A0A2U1JTK1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=DCC39_15090 {ECO:0000313|EMBL:PWA08259.1};
OS Pueribacillus theae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pueribacillus.
OX NCBI_TaxID=2171751 {ECO:0000313|EMBL:PWA08259.1, ECO:0000313|Proteomes:UP000245998};
RN [1] {ECO:0000313|EMBL:PWA08259.1, ECO:0000313|Proteomes:UP000245998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T8 {ECO:0000313|EMBL:PWA08259.1,
RC ECO:0000313|Proteomes:UP000245998};
RA Niu L.;
RT "Camelliibacillus theae gen. nov., sp. nov., isolated from Pu'er tea.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:RU363039}.
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:PWA08259.1}.
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DR EMBL; QCZG01000039; PWA08259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1JTK1; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000245998; 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 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; 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; 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; SSF50677; ValRS/IleRS/LeuRS editing domain; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245998}.
FT DOMAIN 39..170
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..399
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 411..604
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 656..768
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 92124 MW; 697DF0E8B9A6C080 CRC64;
MAFDHRAIEA KWQKYWEENK TFKTEEEGDK PKFYALDMFP YPSGSGLHVG HPEGYTATDI
LSRMKRMQGW NVLHPMGWDA FGLPAEQYAI DTGNNPREFT NKNIETFKRQ IQSLGFSYDW
DREINTTDPE YYKWTQWIFL QLYKKGLAYV DEVPVNWCPA LGTVLANEEV IDGKSERGGH
PVIRKPMKQW MLKITAYADR LLEDLEELDW PESIKEMQRN WIGRSEGAEV HFQIDGHDES
FTVFTTRPDT LFGATYCVLS PEHPLVKEIT TEEQQGKVEA YQKEIESKSD LERTELSKEK
TGVFTGAYAL HPITGDKLPI WIADYVLMGY GTGAIMAVPA HDERDWEFAK TFGLEIKEVV
SGGNVDEEAY AGDGILVNSD FLNGLKKQEA IEKMISWLEE NGKGARKVSY RLRDWLFSRQ
RYWGEPIPII HLEDGTMKPV PEEELPLRLP EMNEIKPSGT GESPLANAKE WLEVTDPETG
MKGKRETNTM PQWAGSCWYY LRFIDPHNDN ALADSEKLKR WLPVDIYIGG AEHAVLHLLY
ARFWHKVLYD LGVVPTKEPF QKLFNQGMIL GENNEKMSKS KGNVVNPDDI INSHGADTLR
LYEMFMGPLD ASIAWSENGL DGSRRFLDRI WRLFVTEDGS LNPKIKDETG SKEMELVYHQ
TVKKVTEDYE ALHFNVAISQ LMVFINEANK QEVLPKGYME AFVKMLSPVA PHISEELWEK
LGHANTIAYE TWPTYDETKL VKDEVEIVVQ VNGKIKAKLN IPASAAKEEM EEIAKADETI
QKQLEGKTIR KVIAVPGKLV NIVAN
//
