ID A0A1K1LPJ6_9BACT Unreviewed; 949 AA.
AC A0A1K1LPJ6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN02910409_0329 {ECO:0000313|EMBL:SFW11574.1};
OS Prevotellaceae bacterium HUN156.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1520830 {ECO:0000313|EMBL:SFW11574.1, ECO:0000313|Proteomes:UP000182805};
RN [1] {ECO:0000313|EMBL:SFW11574.1, ECO:0000313|Proteomes:UP000182805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUN156 {ECO:0000313|EMBL:SFW11574.1,
RC ECO:0000313|Proteomes:UP000182805};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPIT01000003; SFW11574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1LPJ6; -.
DR STRING; 1520830.SAMN02910409_0329; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000182805; 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 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; 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; 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:UP000182805}.
FT DOMAIN 35..139
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..458
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 796..909
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 717..721
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 949 AA; 108976 MW; A59FEAF7136EB56A CRC64;
MEYNFRDIEQ KWQKRWVEMQ TYRVKEDPTK KKFYVLNMFP YPSGAGLHVG HPLGYIASDI
YARFKRLQGY NVLNPMGYDA YGLPAEQYAI QTGQHPEKTT TENINRYRQQ LDKIGFSFDW
EREVRTCDPI YYKWTQWAFQ RMFKSYYSTA SHKAQPTIKL IEHFELMGTE DCHALGSEEL
HFTAAEWNAF SEKKKQEVLM NYRIAYLAET MVNWCPALGT VLANDEVING VSERGGYPVE
QKKMRQWCLR VSAYAQRLLD GLEDIDWTDS LKETQRNWIG RSEGTEVEFN VADSDKHFTI
FTTRADTMFG VTFMVLAPES DLVAELTTAD QKEEVEKYLA YVKKRTERDR ISDKKVTGVF
SGSYAINPFN DKKIPIWISE YVLAGYGTGA IMAVPAHDSR DYAFAKHFNL PIIPLIEGAD
VSEESYDAKE GIVCNSASDK FSLNGLTVKE AIAATKKYVT EQGLGRVKVN YRLRDAIFSR
QRYWGEPFPV YYKDDMPYMI PKECLPLQLP EIDEYKPTET GEPPLGRAKK WAWDTKTNTV
VDCSAIDNDT VFPLELNTMP GFAGSSAYYL RYMDPKNEQA LVGKDADEYW RNVDLYVGGT
EHATGHLIYS RFWNKFLFDS GYSCEDEPFK KLVNQGMIQG RSNFVYRIED EGADKGKFVS
LNLRKNYKET TPIHVDVNIV SADVLDVEAF KAWRPEYNNA EFILEDGKYI CGWAVEKMSK
SMFNVVNPDM IVEKYGADTL RLYEMFLGPV EQSKPWDTNG IDGCHRFLKK FWALYYGNSR
DNADTIIVDD AEPAKESLKS VHKLIKKVTQ DIEVFSYNTS ISAFMICVNE LAQQKCHNRE
LLKTLVVLIA PFAPHIAEEL WEALGGEGSV CDAKWPTWNE EYLVENSVKL GVAFNGKTRF
DMEFPADADN DTIQKAVLAD ERSPKYIDGK PIIKVIIVPK RMVNIVLGK
//
