ID A0A936YVJ5_9HYPH Unreviewed; 876 AA.
AC A0A936YVJ5;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
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=JJB09_19135 {ECO:0000313|EMBL:MBL0374142.1};
OS Rhizobium setariae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=2801340 {ECO:0000313|EMBL:MBL0374142.1, ECO:0000313|Proteomes:UP000633219};
RN [1] {ECO:0000313|EMBL:MBL0374142.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KVB221 {ECO:0000313|EMBL:MBL0374142.1};
RA Kang M.;
RT "Rhizobium sp. strain KVB221 16S ribosomal RNA gene Genome sequencing and
RT assembly.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469, 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: 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:MBL0374142.1}.
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DR EMBL; JAEQNC010000011; MBL0374142.1; -; Genomic_DNA.
DR RefSeq; WP_201661906.1; NZ_JAEQNC010000011.1.
DR AlphaFoldDB; A0A936YVJ5; -.
DR Proteomes; UP000633219; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 1.10.730.10:FF:000002; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000633219}.
FT DOMAIN 38..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..411
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 431..587
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 631..671
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 716..838
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 876 AA; 98295 MW; 732A095285FA295B CRC64;
MASERYNPRE VEPRWQQQWN EAKVFETAND DPRDKYYVLE MFPYPSGRIH MGHVRNYAMG
DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMKNKVHPKT WTYENIASMR KQLKSMGLSL
DWSREFATCD VEYYHRQQYL FLDMMEKGLV YRKNSKVNWD PVDMTVLANE QVIDGRGWRS
DALVEQRELT QWFFKITDFA QDLLDQLDTL DQWPEKVRLM QKNWIGRSEG MTIRWQVVAS
ATHPDLSEIK VYTTRPDTLF GASFLAISAD HPVAKAAAAQ SAEIAAFCDE CRKTGTSVAA
LETAEKMGMD TGIRVAHPFD ASWQVPVYIA NFVLMDYGTG AIFGCPSGDQ RDLDFANKYG
LPVVPVVMPA NEDKATFAIT DEAYVGDGIM INSRFLDGMS PEAAFQDVAS RLGQSQIDGA
PQGERKVNFR LRDWGISRQR YWGCPIPVIH CEVCGVVPVP KKDLPVKLPD DVTFDVPGNP
LDRHPTWRHV GCPQCGKAAR RETDTMDTFV DSSWYYARFT APWEDAPTDP RAADAWLPVD
QYIGGIEHAI LHLLYSRFFT RAMRATGHVG MDEPFKGLFT QGMVVHETYS RGEGHGREWI
EPIFVKIDEI DGKRQATHLE SGEPISIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
SDSPPERDVI WSESGVEGAH RFVQRVWRLI SEAADVLQSA PSRAASEGEA LAISQIAHRT
LKQVQADYDR LGFNKAVARI YELVNALAQP LATVAAGKAD TAMVSAVREA SEILVHLISP
MTPHLAEECW RVLGNDDLLA QAIWPAFDEG LVVDNQITMP IQVNGKKRAD LTIARDADQT
SIEQAVLALE SIKAALDGKT PKKIIIVPQR IVNVVV
//
