ID A0A242CGK2_9ENTE Unreviewed; 837 AA.
AC A0A242CGK2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A5880_000046 {ECO:0000313|EMBL:OTO09367.1};
OS Enterococcus sp. 4G2_DIV0659.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834181 {ECO:0000313|EMBL:OTO09367.1, ECO:0000313|Proteomes:UP000195139};
RN [1] {ECO:0000313|EMBL:OTO09367.1, ECO:0000313|Proteomes:UP000195139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G2_DIV0659 {ECO:0000313|EMBL:OTO09367.1,
RC ECO:0000313|Proteomes:UP000195139};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 4G2_DIV0659.";
RL Submitted (MAY-2017) 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: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:OTO09367.1}.
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DR EMBL; NGLE01000001; OTO09367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242CGK2; -.
DR STRING; 1834181.A5880_000046; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000195139; 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; 3.40.50.620; 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; 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; 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 39..169
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..398
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 412..571
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 608..637
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 687..799
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 609..613
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 837 AA; 95416 MW; 535794AA3E6A6EEE CRC64;
MSYDHKKIEK KWQKYWAKHN SFITRDDSSK KKFYALDMFP YPSGQGLHVG HPEGYTATDI
LSRMKRSQGY SVLHPMGWDA FGLPAEQYAL DTGNDPAEFT KKNIETFKRQ INSLGFSYDW
NREINTTDPE YYKWTQWIFT KLYEHGLAYE AEVAVNWVPE LGTVISNEEV IDGKSERGGY
DVVRKPMRQW MLKITAYADR LLDDLELVDW PENIKDMQRN WIGRSEGANV TFEVAGTQET
FTVFTTRPDT LFGATYTVLA PELELVKKIT TPEQKEAVEA YIDAASKKSD LNRTDLAKEK
TGVFTGTYAI NPVNGAEVPI WIADYVLASY GTGAIMAVPA HDERDYEFAK AFNIEIIPVL
EGGDVEKAPF TGDGSHINSD FLNGLNKEEA ISKINVWLEE KGVGKKEVSY RLRDWLFSRQ
RYWGEPIPVI HWEDGTTTTV PEKDLPLTLP KTDDIKPSGT GESPLANITE WINVVDPETG
KKGKRETNTM PQWAGSSWYH LRYIDPHNKN ELANYEKLER WLPVDIYIGG AEHAVLHLLY
ARFWHKFLYD IGVVPTKEPY QKLYNQGMIL GQSFRDSRGV LVPTNLVEKR DGAWVSTETG
EELEEAPAKM SKSLKNVVNP DDVIEKYGAD TLRMYEMFMG PLDASIAWSE NGLEGSRKFL
DRVWRLIVDE NDKMRDRITT VNDGRLTKVY NQTVKKVTED MENLHFNTAI SQLMVFVNEA
NKVDVLPYEY IEGFVQLLAP IAPHIGEELW AILGNEESLT NVPWPTFDES ALVEDEVEVV
FQVNGKVRAK VKVARGLSKD ELEEKALATE EIQSFIDGKT VRKVIVVPEK LVNIVAN
//
