ID A0A011Q6V4_9LACT Unreviewed; 805 AA.
AC A0A011Q6V4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=ADIAL_1438 {ECO:0000313|EMBL:EXJ23081.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23081.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ23081.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) 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:EXJ23081.1}.
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DR EMBL; JANL01000034; EXJ23081.1; -; Genomic_DNA.
DR RefSeq; WP_034301856.1; NZ_JANL01000034.1.
DR AlphaFoldDB; A0A011Q6V4; -.
DR STRING; 1229520.ADIAL_1438; -.
DR PATRIC; fig|1229520.3.peg.1403; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000020164; 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; 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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 39..170
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..612
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 650..767
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; 92090 MW; D567E2153CEB0DB7 CRC64;
MTFDHKTIEK KWQDFWDKHQ TFKTTEEEDK EYFYALDMFP YPSGQGLHVG HPEGYTATDI
VSRMKRAQGY NVLHPMGWDA FGLPAEQYAL DTGNDPAEFT EQNIQTFKRQ IKSLGFSYDW
EKEINTTDPD YYKWTQWIFT KLVEKDLAYE AEVPVNWCPA LGTVLANEEV IDGKSERGGH
PVYRKPMKQW MLKITAYADR LLDDLEEVNW PEHIKDMQRN WIGKSEGAEI TFKVKDSEHT
FDVFTTRPDT LFGATYAVLA PESDLVDQIT TPEQAEAVEA YRKEANLKSD LERTDLNKNK
TGVFTGAYAV NPVTDETMPI WIADYVLASY GTGSIMAVPA HDERDYEFAQ KYDLEIRPVI
EGGDTDEEAY TGDGLHINSD FINGLNQKEA TDKIISFLEE KQLGSQKTTY RLRDWLFARQ
RYWGEPIPVI HWEDGTTSTV PEEELPVTLP KTKEIKPSGT GESPLAIIDE WVNVVDEKTG
LKGKRDTNTM PQWAGSSWYF LRFIDPHNPD QLADPEKIKK WLPVDLYIGG AEHAVLHLLY
ARFWHKFLYD LGIVPTKEPF EKLYNQGMIL GENNEKMSKS KGNVVNPDVV VEAYGADTLR
LYEMFMGPLD AAIAWSEDGL EGSRKFLDRV WRLFIDENGR VRDRITTYND KSLEVVYHQT
VKKVTEDYDN LQFNTAISQL MVFVNAAYKA DGLPLEYVKG FIQLLAPIAP HVSEELWSLI
IQSGLSLAYE SWPTYDETKL VTDEVEVVFQ VNGKVRARAQ ASKSVSKDAL QEMAMQDGKI
QEMLEGKTVR KVIVVPGKLV NIVAN
//
