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Database: UniProt
Entry: A0A1M4V1S2_9FIRM
LinkDB: A0A1M4V1S2_9FIRM
Original site: A0A1M4V1S2_9FIRM 
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
//
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