ID A0A1B1SCF0_9BACT Unreviewed; 923 AA.
AC A0A1B1SCF0; A0A1Z2XGJ5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=A4V02_12015 {ECO:0000313|EMBL:ANU64370.1};
OS Muribaculum intestinale.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Muribaculum.
OX NCBI_TaxID=1796646 {ECO:0000313|EMBL:ANU64370.1, ECO:0000313|Proteomes:UP000186351};
RN [1] {ECO:0000313|Proteomes:UP000186351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL27 {ECO:0000313|Proteomes:UP000186351};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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:RU363035}.
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; CP015402; ANU64370.1; -; Genomic_DNA.
DR RefSeq; WP_068961651.1; NZ_PUEE01000003.1.
DR AlphaFoldDB; A0A1B1SCF0; -.
DR STRING; 1796646.A4V02_12015; -.
DR GeneID; 65537598; -.
DR KEGG; pary:A4V02_12015; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000186351; Chromosome.
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 Gene3D; 3.40.50.620; HUPs; 3.
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; 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 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:UP000186351}.
FT DOMAIN 12..145
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 276..456
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 770..886
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 697..701
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 923 AA; 105236 MW; 55E7F3A8C1374606 CRC64;
MEYNHKEIES RWQQYWKDHK TYKTEIDRSR PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
YSRYKRLNGF NVLHPMGYDS YGLPAEQYAI QTGQHPEKTT FENIDRYRSQ LDKIGFCYDW
DREIRTCDPS YYKWTQWAFM KMYEHYYDRN ADKAMPVVDL IAHFEKSGTE GVNAACGKDM
EFTAEEWKGM SPKEKSDTLM NYRIAFLADT MVNWCPKLGT VLANDEVSEG VSLRGGYPVE
QKLMYQWCLR VSAYAQRLLD GLDTIDWTDS LKETQRNWIG RSEGAEMRFP IDGSDVELEI
FTTRADTVFG VTFMVLAPES VYVDMITTPE QRGAVDAYLD EVKHKTERER MIDKKVSGVF
TGAYAVNPLT GKNIPVWVSD YVLAGYGTGA IMAVPAHDSR DYAFARHFNL PVIPLIEGAD
VSEESFDAKS GKMINSASAE LDLNGMEVKD AIATTKKFIE EKGIGKVKVN YRLRDAIFSR
QRYWGEPFPV YYKDGIPTLL PEESLPLELP EVDKFLPTET GEPPLGRAKN WKTAEGYPLE
LNTMPGFAGS SAYYLRYMDP KNDNALVSEE ADGYWQDVDL YIGGTEHATG HLIYSRFWNK
FLYDLGVVCR DEPFRKLVNQ GMIQGRSNFV YRIKDTNTFV SAGLRKEYDT TPIHVDVNIV
SNDVLDTEKF RAWRPEFKDA EFILEDGKYV CGYAVEKMSK SMFNVVNPDD IVERYGADTL
RLYEMFLGPI EASKPWDTNG IDGVNRFLRK LWSLFYKGDN LLVSDESASK DALKAVHKLI
KKVTADIESF SYNTSVAAFM ICVNELTQLK CHSREALEPL VVLIAPFAPH IAEELWHALG
HDTTVCDAKW PVHNEEYLVE STVTMAVSFN GKARYNIQVP ADAPREEIEK IALAHEGAAK
WIEGKQIRKI IVVPGKIVNI VVG
//
