ID A0A1M4V1S2_9FIRM Unreviewed; 803 AA.
AC A0A1M4V1S2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=SAMN02746064_00888 {ECO:0000313|EMBL:SHE62850.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHE62850.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHE62850.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHE62850.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; FQTU01000004; SHE62850.1; -; Genomic_DNA.
DR RefSeq; WP_073269872.1; NZ_FQTU01000004.1.
DR AlphaFoldDB; A0A1M4V1S2; -.
DR STRING; 1120975.SAMN02746064_00888; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184251; 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; 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-RELATED; 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 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}; Cytoplasm {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:UP000184251}.
FT DOMAIN 12..218
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 220..404
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..614
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 656..764
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 581..585
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 803 AA; 92307 MW; 8C788985AF510D81 CRC64;
MKSYNYKNIE SKWQKIWEDK ELFKAVDFSD KPKFYGLVEF PYPSGIGLHV GHVRAYTSLE
VISRKRRLEG YNVLFPIGWD AFGLPTENYA IQTGRHPRLV TDENIKVFTE QLKEIGYSFD
WDRTVDTTDE NYYKWTQWIF LKLFEKGLAY KNKTYVNFCN DCKVVLANEE SQDGKCDRCG
SEVVQMEKDV WFLKIREYSE KLLEGLEKVD FLPRIKLEQE NWIGKSSGAE VDFQIDGTDD
KLSVFTTRPD TLYGVTFMVV APEHPLIEKY SEKISNMDQI KEYQEQAKKK TEFERVQLAK
DKSGVEVKGV KVRNPLNGEL VPLWVADYVM MGYGTGAIMA VPGHDGRDWE FAKKFDIPII
EVIQGGNVLE EAFTDIENGI LVNSDIINGM NVKEAKEKII SHLESHGVGK RTVNYKMKDW
AFNRQRYWGE PIPVVHCETC GIVGVPENEL PVKLPQVKNY KPTDTGESPL ASIEEWVNTT
CPKCGQKAKR ETDTMPQWAG SSWYFLRYID PRNNEEFASQ DKLKYWLQID WYNGGMEHVS
RHLIYSRFWH RFLYDIGEVP VDEPYAKRTA QGLILGADGE KMSKSRGNVI NPREIIGEYG
ADTLRTYIMF IGDYEKPAPW SDNGVKGCRR FLDRVWKLEN ILVDGNEYSK DNEVMMNKTI
KKVTEDYENL KFNTAIAALM TLINEFNAKG KINKKEFSDF LLLLNPVAPH ITEELWEVCG
IGGVLHEQGW PGFDPEKTVE DVIEMAVQVN GKVRGKIQIP VKSTQAEANA AAMTEESIKA
HIEGKTIVKE IFVPGRIYNI VVK
//