ID A0A368VYC5_9ACTN Unreviewed; 973 AA.
AC A0A368VYC5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DFQ14_101554 {ECO:0000313|EMBL:RCW47208.1};
OS Halopolyspora algeriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC Halopolyspora.
OX NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW47208.1, ECO:0000313|Proteomes:UP000253495};
RN [1] {ECO:0000313|EMBL:RCW47208.1, ECO:0000313|Proteomes:UP000253495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW47208.1,
RC ECO:0000313|Proteomes:UP000253495};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RCW47208.1}.
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DR EMBL; QPJC01000001; RCW47208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VYC5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000253495; 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; 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.
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}; Cytoplasm {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:UP000253495}.
FT DOMAIN 71..175
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 305..511
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 817..934
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 742..746
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 973 AA; 109292 MW; C701493489F7EE6B CRC64;
MSGAAENSAD GRADRSGTEE VPSFRYTAEM AGEIERRWQQ RWEELGTFHT PNPSGSLQGD
TSGAEKLFVQ DMFPYPSGSG LHVGHPLGFI GTDVYARFHR MLGRNVLHTM GFDAFGLPAE
QYAAQTGTHP RTTTENNIER YLSQIRRLGL GHDERRRIAT TDIDFYRWTQ WIFLQIFHAW
YDFDADDGKG RARPIGELEQ QFESGERATP DGRPWGDLTR AEQRAVLDSY RLVYLSEEPV
NWCPGLGTVV ANEEVTAEGL SERGNFPVFR RNLKQWMMRI TAYADRLVDD LDRLEWPEKV
KTMQRNWIGR SRGANVVFEL PGSTSGIEVF TTRPDTLFGA TYMVLAPEHP LVDELIAARG
EDQGWPEGTD ERWTQGAASP AEAVAAYRHA ASMKSELDRQ ETREKTGVFT GAHATNPVNG
ESIPVFIADY VLMAYGTGAI MAVPGQDQRD WDFASVFGLP IVRTVEPPQD FEGEAYTGDG
PAINSSSQVT GLSLNGLDVE EAKKEIISWL EEHGHGSGSV QYKLRDWLFA RQRYWGEPFP
VVYDSDGTPL GLPEDQLPVV LPEVADYSPR TFDPDDANSE PEPPLARAGD WGAVELDLGD
GLRKYERDNN VMPQWAGSCW YQLRYIDPDN DERFVDPDNE RYWMGPRPDR HGPDDPGGLD
LYVGGVEHAV LHLLYSRFWH KVLYDLGHVS SEEPYRRLYN QGYIQAYAFT DSRGVYVPAE
EVQERDGKFF HNGQEVTREY GKMGKSLKNS VSPDEMADAY GADTLRLYEM SMGPLEASRP
WATKDVVGSH RFLQRLWRNI IDEHTGQLRA VDIEPDLEMR RALHKTIAGV REDYGELRFN
TAVAKLIELN NRVTKEYSAV AGTPREVVEA LVLMVAPLTP HLAEELWSRL GHEAGLAHGP
FPVADEQYLV EDTVEYPIQF NGKVRSRTVV AASAGQDEIR EAALADEKIA AALDGKEPRK
VIVVPGRLVN VVG
//
