ID A0A1M5XYZ7_9CLOT Unreviewed; 812 AA.
AC A0A1M5XYZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=SAMN02745196_02507 {ECO:0000313|EMBL:SHI04503.1};
OS Clostridium collagenovorans DSM 3089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHI04503.1, ECO:0000313|Proteomes:UP000184526};
RN [1] {ECO:0000313|EMBL:SHI04503.1, ECO:0000313|Proteomes:UP000184526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3089 {ECO:0000313|EMBL:SHI04503.1,
RC ECO:0000313|Proteomes:UP000184526};
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 ECO:0000256|RuleBase:RU363039}.
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; FQXP01000010; SHI04503.1; -; Genomic_DNA.
DR RefSeq; WP_072832358.1; NZ_FQXP01000010.1.
DR AlphaFoldDB; A0A1M5XYZ7; -.
DR STRING; 1121306.SAMN02745196_02507; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184526; 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; 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; 1.
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.
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:UP000184526}.
FT DOMAIN 40..186
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..397
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 410..600
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 659..773
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; 92323 MW; 9823CB0428F5B6E1 CRC64;
MSKYNTDIDK KWQNKWEETG LYKFDKNKEG EKLYVLEMFS YPSGNQLHAG HWFNYGPVDS
WARFKRMRGF NVFQPMGFDA FGLPAENFAI KTGVHPKDST ERNIVKMEEQ LKAMGAMFNW
DNELVTCDPT YYKWTQWLFL KLYEKGLAYR KKAPVNWCPS CNTVLANEQV VDGLCERCST
EVTKKDLTQW FLKITDYAEE LLTKIDELDW PEKTKAMQKH WIGKSTGAEV TFKVDNSDLD
FSVFTTRPDT LFGVTYVVLA PENELVDTLT TEDNKEAVEN YKEEAKKQSD IERQSITREK
TGIFTGSYAI NPINGRKVPI WVGDYVLNTY GTGAVMAVPA HDERDFAFAT KYDLPIEKVI
DGCEELPHTG SGNLVNSGEF DGITARQGKK AIVNKLEEIK AGSSKTNYRL RDWLVSRQRY
WGAPIPMIHC DKCGIVPVPE NQLPVELPYD VEFAPDGKSP LGKCEDFLKT TCPVCGGPAH
READTLDTFV CSSWYYLRYP DNKNSEKAFD TDLINELLPV DKYVGGPEHA CMHLLYARFI
TKALRDMGYV NFDEPFKSLT HQGLILGPDG LKMSKSKGNT ISPDEYISLY GADVFRMYLM
FGFGYTEGGA WSDDGIKSIG RFVDRIERYL DGFIDEINKG ENNKTTMDKA EKELNFWRHS
TIKAVTADTE ILQFNTAIAR MMEFLNALSK YSTESVKNLS FLKETLVDFV KLLAPFAPHF
AEEKWEALGM NFSVFNEAWP EFDKKALVKD EVEIAIQING KIKARINVAS GLGEDEIKEA
ALNTSEIVTA LEDKTVRKVI VIKGRLVNIV AN
//
