ID A0A151AN94_9CLOT Unreviewed; 812 AA.
AC A0A151AN94;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JAN-2026, entry version 43.
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 ECO:0000313|EMBL:KYH29102.1};
GN ORFNames=CLCOL_12390 {ECO:0000313|EMBL:KYH29102.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH29102.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH29102.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH29102.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) 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:RU363039}.
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:KYH29102.1}.
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DR EMBL; LTBB01000005; KYH29102.1; -; Genomic_DNA.
DR RefSeq; WP_061858110.1; NZ_LTBB01000005.1.
DR AlphaFoldDB; A0A151AN94; -.
DR STRING; 1121305.CLCOL_12390; -.
DR PATRIC; fig|1121305.3.peg.1241; -.
DR Proteomes; UP000075374; 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; 3.10.20.590: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:000056; Leucine--tRNA ligase; 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 HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 2.
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};
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:UP000075374}.
FT DOMAIN 40..186
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..396
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 568..602
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 658..774
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 812 AA; 92726 MW; 6EFDA5C5739463AD CRC64;
MANYGTSVDK KWQTKWEESG LHNFDENAPG EKLYVLEMFS YPSGAKLHAG HWFNYGPTDS
WARFKKMQGY NVFQPMGFDA FGLPAENYAI KTGIHPKDST MQNIANMEEQ LRAMGAMFNW
DHEVITCLPE YYKWTQWVFL KLFEKGLAYR KNAPVNWCPS CNTVLANEQV IEGHCERCDS
EVEKKDLTQW FLKITHYADE LLEKLDELDW PEKTKAMQKH WIGKSKGAQV TFKVENSDLT
FDVFTTRVDT LNGVTYVVLA PETPLVDKIT LPEYKDAVEE YKIQAQKQSD IERQSTSREK
TGVFTGSYAI NPINGKRVPI WVGDYVLATY GTGCVMAVPA HDERDFAFAT KYNLPIIRVV
DGGDSLPYTG YGPLVNSGEF DGLSGDKAKE AIVNKLKEQG LGDWKINYRL RDWLVSRQRY
WGAPIPVVYC DKCGIVPVPE DQLPVELPYD IEFTPDGKSP LSKSESFLNT TCPKCGGHAT
RESDTLDTFV CSSFYYLRYV DNKNKEKCFD SDKVNAMLPV DKYVGGPEHA TMHLLYARFI
TKALRDMGYL NFDEPFKSLT HQGLILGPDG QKMSKSKGNT ISPDDYIKEF GADVFRMYLM
FGFAYSEGGA WSDEGIKSIG RFVDRVERLL EQCRNEINSS KNTNTSMNKA EKELNYARHY
AIKHVTEDTE KFQFNTSIAR IMEFTNALSK YLNEENKNVK FLEETVIDYI KLLAPFAPHF
AEEQWELLQK DFSIFNESWP KFDPSALVKD EVEIAIQVSG KIRARMNIPT TLTEDEIKEA
ALNNETIQQF INGKTIMKVI VVKGRLVNIV AK
//
