ID A0A081XQ23_STRTO Unreviewed; 958 AA.
AC A0A081XQ23;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=BU52_19175 {ECO:0000313|EMBL:KES05646.1};
OS Streptomyces toyocaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=55952 {ECO:0000313|EMBL:KES05646.1, ECO:0000313|Proteomes:UP000028341};
RN [1] {ECO:0000313|EMBL:KES05646.1, ECO:0000313|Proteomes:UP000028341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES05646.1,
RC ECO:0000313|Proteomes:UP000028341};
RA Hong H.-J., Kwun M.J.;
RT "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL Submitted (FEB-2014) 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 -!- 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:KES05646.1}.
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; JFCB01000016; KES05646.1; -; Genomic_DNA.
DR RefSeq; WP_037935775.1; NZ_JFCB01000016.1.
DR AlphaFoldDB; A0A081XQ23; -.
DR STRING; 55952.BU52_19175; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000028341; 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; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000028341}.
FT DOMAIN 64..167
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 294..499
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 805..920
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 728..732
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 554..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 958 AA; 106775 MW; CB148BA0D7ACFED5 CRC64;
MSETNPAAAE AAPHRYTAAL AAEIEARWQD FWDAEGTYAA PNPKGDLAGD PELAARPKKF
IMDMFPYPSG AGLHVGHPLG YIATDVFARF QRMTGHNVLH TLGFDAFGLP AEQYAVQTGT
HPRVSTEANM ENMKSQLRRL GLGHDKRRSF ATIDPDYYKW TQWIFLQIFN SWYDDEAGRA
RPITELVAQF ESGERAVPGH TRPWGELSEA ERADVLGGFR LAYASDAPVN WCPGLGTVLA
NEEVTAEGRS ERGNFPVFKA KLRQWNMRIT AYADRLLDDL DALDWPEAIK LQQRNWIGRS
EGARVDFPID GENITVFTTR PDTLFGATYM VLAPEHPLVE KFTPDAWPEG THEVWTGGHA
TPAEAVAAYR AQAASKSDVE RQAEAKDKTG VFIGAYATNP VNGEQVPVFI ADYVLMGYGT
GAIMAVPAGD QRDFEFARAF ELPIRCVVEP TDGRGTDTST WEDAFGSYDA KIINSANDEI
SLDGLGVVEA KARITEWLER EGRGEGTVNF RLRDWLFSRQ RYWGEPFPIV YDEDGIAHAL
PESMLPLELP EVEDYSPRTF DPDDADTQPE TPLSRNEDWV HVTLDLGDGR GPRRYRRETN
TMPNWAGSCW YELRYLDPHN GEKLVDPEIE RYWMGPRQGM PHGGVDLYVG GAEHAVLHLL
YARFWSKVLY DLGHVSSAEP FHKLFNQGMI QAYVYRDSRG IAVPAAEVEE RDGGYWYQGE
KVTRLLGKMG KSLKNAVTPD EICAEYGADT LRLYEMAMGP LDVSRPWDTR AVVGQFRLLQ
RLWRNIVDEA TGEVTVVDTD DVDEDTLRAL HKAIDGVRGD LEGMRFNTAI AKVTELNNHL
TKRGGALPRP VAESLVLLVA PLAPHVAEEL WRKLGHAESV VHQDFPVADP AYVVDETVTC
VVQIKGKVKA RLEVSPDISE DELEKAALAD ERVVAALDGA GIRKVIVRAP KLVNIVPA
//
