ID D1VSF2_9FIRM Unreviewed; 803 AA.
AC D1VSF2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:EFA90559.1};
GN ORFNames=HMPREF0628_0735 {ECO:0000313|EMBL:EFA90559.1};
OS Peptoniphilus lacrimalis 315-B.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA90559.1, ECO:0000313|Proteomes:UP000005711};
RN [1] {ECO:0000313|EMBL:EFA90559.1, ECO:0000313|Proteomes:UP000005711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=315-B {ECO:0000313|EMBL:EFA90559.1,
RC ECO:0000313|Proteomes:UP000005711};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL Submitted (DEC-2009) 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}.
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:EFA90559.1}.
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DR EMBL; ADDO01000021; EFA90559.1; -; Genomic_DNA.
DR RefSeq; WP_004824096.1; NZ_ADDO01000021.1.
DR AlphaFoldDB; D1VSF2; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000005711; 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; 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; 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.
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:UP000005711}.
FT DOMAIN 39..185
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..607
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 654..765
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; 93015 MW; 0F85329A943B88C2 CRC64;
MKDYKPEVIE KKWQDYWDEH QTYKALNDDD RGKIYLLVEF PYPSGQGLHV GHPRPYTALD
IVARKRRYQG YNVLFPMGWD AFGLPTENYA IKNKIHPAIV TKQNIKHFKD QLKSIGFSFD
WSREINTTDP EYYKWTQWIF LQLYKHGLAY KKESPINWCP SCKTGLANEE VIGGKCERCN
TEVVRRVKSQ WMLKITGYAD RLIDDLDDVD YIERVKTQQK NWIGRSEGAS ILFPIKDSDE
KLEVFTTRPD TIFGATYMVI APEHPLLEKY KDRILNLDEI NAYKEEVAKK SDFERTELAK
DKTGVEIKGL KAINPISKKE IPVWISDYVL MSYGTGAIMA VPAHDTRDYD FAKKFGLDIV
EVIKGGDISK EAYTDTNNGK LVNSEFLNGL EVKDAKEKMI KYLLENNLGN KKINFKLRDW
VFSRQRYWGE PIPIVHCPKC GFVPVPEEQL PLLLPEVENY EPTDDGESPL ANIKEFVETT
CPKCGCHAHR ETDTMPQWAG SSWYFLRYAD PHNKDALASK DALNYWTPVD WYNGGMEHTT
LHLLYSRFWH KFLYDIGVVP TKEPYVKRTS HGMILGENNE KMSKSRGNVV NPDDIVRDYG
ADTLRTYEMF IGDFEKPVPW METGVRGCRR FLDRVWNLSD ILVDGDKYSE SLEKLIHKTI
KKVSYDYENL KANTAIAALM SLLNEFVANK NITKADFRTF LMLLNPVAPH ITEELWEQNN
LGGYLNESSW PVYDEEKTID NIVEMPVQFN GKLRFTIEVS KDANVDQARE IAMKNEAYAK
NITDKKVIKE IFVPGKIYNI VVK
//
