ID A0A0F2TFL9_STRR3 Unreviewed; 960 AA.
AC A0A0F2TFL9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=VM95_15220 {ECO:0000313|EMBL:KJS61361.1};
OS Streptomyces rubellomurinus (strain ATCC 31215).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS61361.1, ECO:0000313|Proteomes:UP000033699};
RN [1] {ECO:0000313|EMBL:KJS61361.1, ECO:0000313|Proteomes:UP000033699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS61361.1,
RC ECO:0000313|Proteomes:UP000033699};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJS61361.1}.
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; JZKH01000027; KJS61361.1; -; Genomic_DNA.
DR RefSeq; WP_045696794.1; NZ_JZKH01000027.1.
DR AlphaFoldDB; A0A0F2TFL9; -.
DR PATRIC; fig|359131.3.peg.3382; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000033699; 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:UP000033699}.
FT DOMAIN 70..173
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 299..504
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 807..921
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 732..736
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 960 AA; 105866 MW; 3255ECB8BF8BD2AB CRC64;
MSETTPASGA AEAATEPFRY SAALAAEIES RWQDIWEKEG TFHVPNPVGP LADPSAGDVA
AKPHSFIMDM FPYPSGAGLH VGHPLGYIAT DVFARYQRMT GHNVLHTLGY DAFGLPAEQY
AVQTGTHPRV STEANIANMR RQLRRLGLGH DPRRSFSTID PEYYRWTQWI FLQIFNSWYD
ADAAKARPIA ELVQQFADGT REVPGGRAWA SLTAGERDEV LAEYRLAYAK EVPVNWCPGL
GTVLANEEVT ADGRSERGNF PVFKSNLRQW MMRITAYSDR LINDLDMLDW PEAIKLQQRN
WIGRSEGARV DFAVDGEKIT VFTTRPDTLF GATYMVLAPE HDLVDAIVPA AWPEGVPAEW
TGGAATPAEA VAAYRAAAAA KSDVERQVEA KVKTGVFTGA HAVNPVSGES VPVFIADYVL
MGYGTGAIMA VPAHDHRDFA FARAFGLPMR CVVEPTDGRG ADPAQWDDAF DTYDSVIVNS
VRDGELSLDG LSVVDAKAHV TAWLAERGIG EGTVNYRLRD WLFSRQRYWG EPFPIVYDED
GVMHALPDSM LPVEVPEVDD YSPRTFDPFD ASSSPETPLS RNEAWVNVEL DLGDGVKKYR
RETNTMPNWA GSCWYELRYV DPSNTSAVAD PANERYWLGP TDTKPAGGAD LYVGGAEHAV
LHLLYARFWH KVLHDLGHVS SVEPFHKLFN QGMITADVYR DERGFPVPAA EVEERDGGYF
WEGEPVKREA GKMGKSLKNA VAPDDISDEY GADTLRLYEM SMGPLDVSRP WDTRAVVGPY
RFLQRLWRNI VSETTGELVV TDEQPDEATL RVLHKAIDGI RGDMAALRFN TAVAKAIELN
NYLVKRGSTP REVAEQLVLM VAPLAPHVAE ELWRRLGHTE SLAHADYPVA DPAYVVDESV
TCVVQIKGKV KARLEVAPGI TDAELETLAL AEPAVVAAIG DAAVRKVIVR APKLVNIVTG
//
