ID A0A4T0UQN3_9NEIS Unreviewed; 872 AA.
AC A0A4T0UQN3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, 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=E5K04_11305 {ECO:0000313|EMBL:TIC81168.1};
OS Crenobacter intestini.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Crenobacter.
OX NCBI_TaxID=2563443 {ECO:0000313|EMBL:TIC81168.1, ECO:0000313|Proteomes:UP000308891};
RN [1] {ECO:0000313|EMBL:TIC81168.1, ECO:0000313|Proteomes:UP000308891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GY 70310 {ECO:0000313|EMBL:TIC81168.1,
RC ECO:0000313|Proteomes:UP000308891};
RA Shi S.;
RT "Crenobacter sp. nov.";
RL Submitted (APR-2019) 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:TIC81168.1}.
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DR EMBL; STGJ01000012; TIC81168.1; -; Genomic_DNA.
DR RefSeq; WP_136554119.1; NZ_STGJ01000012.1.
DR AlphaFoldDB; A0A4T0UQN3; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000308891; 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:000003; Leucine--tRNA ligase; 1.
DR FunFam; 2.20.28.290:FF:000001; Leucine--tRNA ligase; 1.
DR FunFam; 3.10.20.590:FF:000001; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000124; Leucine--tRNA ligase; 1.
DR FunFam; 3.90.740.10:FF:000012; 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:UP000308891}.
FT DOMAIN 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..413
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 427..603
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 713..835
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
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 872 AA; 96164 MW; A3968B7C52CCAE2A CRC64;
MQEHYSPREV ETAAQQKWKA TAAFRAVEDT SRPKYYALSM FPYPSGKLHM GHVRNYTITD
ALARFMRFKG YNVLQPMGWD AFGLPAENAA MKSGGAPAAW TYANIEYMKG QLDSLGFALD
WERELATCKP DYYRWEQWLF TRLFEKGVIY KKNGVVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYFAITKYAD ELLSSLDTLD GWPEQVKTMQ RNWIGKSFGA DVVFAYDEAS
IGHAGEMKVY TTRPDTLMGA TYVAVAAEHP LAAQAAANNP ALQAFIAECK AGSVAEADVA
TMEKKGMATG LSVVHPLTGA RLPVWVANYV LWGYGEGAVM AVPAHDERDF EFANKYALPI
RQVYAPKAGD NDFDAAVWKE WYASKDGSLS TLNSGAFDGL DFQGAFDAIV SALEAKSAGA
KKTQFRLRDW GISRQRYWGC PIPIIHCDCC GDVPVPADQL PVVLPENVIP DGAGSPLAKM
PEFYETTCPK CGGAARRETD TMDTFVESSW YYARYASPKC DTAMVDKAAA DYWLQVDQYV
GGIEHAILHL LYARFFHKLM RDEGLVSSDE PFKSLLTQGM VVCETFYRDL DNGSKDWIAP
ADVILERDGK GKIVAAKHRV DGLPVTVGGV EKMSKSKNNG VDPQAFIEQY GADTARLFMM
FAAPPEQSLE WSDAGVEGAF RFLKRLWRVV GEHVAGGVVA PYQGGELDGA LKELRYKLHA
TIQKVGDDYG RRQQFNTAIA AVMELLNTYD KTARAGDAGR AVAQEVLEAA VILLSPIVPH
VGEALWNELR PGSELLAQAW PAVDEAALVK SELELMVQVC GKLRGSIVVA ADASREAIEQ
AALAHENVQK FMEGKPAKKV IVVPGRLVNV VV
//
