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0SYLM_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLARS2
DescriptionProbable leucyl-trna synthetase, mitochondrial precursor (ec 6.1.1.4) (leucine--trna ligase) (leurs).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state.nd have limited sequence homology . The 20 aminoacyl-tRNA synthetases are divided into two classes. and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric .hile class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation.lanked byalpha-helices .nd are mostly dimeric or multimeric. In reactions catalysed by the class I aminoacyl-tRNA synthetases.he aminoacyl group is coupled to the 2-hydroxyl of the tRNA.hile.nclass II reactions.he 3-hydroxyl site is preferred. The synthetases specific for arginine.ysteine.lutamic acid.lutamine.soleucine.eucine.ethionine.yrosine.ryptophan and valine belong to class I synthetases.The synthetases specific for alanine.sparagine.spartic acid.lycine.istidine.ysine.henylalanine.roline.erine.nd threonine belong to class-II synthetases .The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold.hich is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses.. and c.ccording to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases.
  IPR002300:Aminoacyl-tRNA synthetase, class Ia
This domain is found valyl and leucyl tRNA synthetases. It binds to the anticodon of the tRNA.
  IPR013155:tRNA synthetase, valyl/leucyl, anticodon-binding
The aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state.nd have limited sequence homology . The 20 aminoacyl-tRNA synthetases are divided into two classes. and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric .hile class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation.lanked byalpha-helices .nd are mostly dimeric or multimeric. In reactions catalysed by the class I aminoacyl-tRNA synthetases.he aminoacyl group is coupled to the 2-hydroxyl of the tRNA.hile.nclass II reactions.he 3-hydroxyl site is preferred. The synthetases specific for arginine.ysteine.lutamic acid.lutamine.soleucine.eucine.ethionine.yrosine.ryptophan and valine belong to class I synthetases.The synthetases specific for alanine.sparagine.spartic acid.lycine.istidine.ysine.henylalanine.roline.erine.nd threonine belong to class-II synthetases .The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold.hich is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses.. and c.ccording to sequence homology. tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. Leucyl tRNA synthetase () is an alpha monomer that belongs to class Ia. There are two different families of leucyl-tRNA synthetases. This family includes the eubacterial and mitochondrial synthetases.The crystal structure of leucyl-tRNA synthetase from the hyperthermophile Thermus thermophilus has an overall architecture that is similar to that of isoleucyl-tRNA synthetase.xcept that the putative editing domain is inserted at a different position in the primary structure. This feature is unique to prokaryote-like leucyl-tRNA synthetases.s is the presence of a novel additional flexibly inserted domain .
  IPR002302:Leucyl-tRNA synthetase bacterial/mitochondrial, class Ia
Certain aminoacyl-tRNA synthetases prevent potential errors in protein synthesis through deacylation of mischarged tRNAs. The close homologs isoleucyl-tRNA synthetase (IleRS) and valyl-tRNA synthetase (ValRS) deacylate Val-tRNAIle and Thr-tRNAVal.espectively. These reactions strictly require the presence of the cognate tRNA. In the absence of tRNA.he enzymatically generated misactivated adenylates remain in the active site.equestered from hydrolysis. Upon addition of cognate tRNA the misactivated amino acids are hydrolyzed.egenerating the free tRNA and amino acid.hile converting 1 equivalent of ATP to AMP. A prominent mechanism for editing misactivated amino acids is the rapid hydrolysis of transiently mischarged tRNA. This reaction is catalyzed at a second active site on IleRS and ValRS. This site is located within a large insertion (termed CP1) into the canonical class I aminoacyl-tRNA synthetase active-site fold. The CP1 domain as an isolated polypeptide hydrolyzes its cognate mischarged tRNA .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009008:ValRS-IleRS-LeuRS editing
The twenty aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA (tRNA) molecule in a highly specific two-step reaction. All of these proteins fall into one of two classes comprised of ten enzymes each: class 1 (Arg.ys.lu.ln.le.eu.et.yr.rp and Val) and class 2 (Ala.sn.ly.is.ys.he.ro.er.nd Thr). Class 1 enzymes are mostly monomeric.nd contain a characteristic Rossman binding fold that bind the tRNA acceptor stem from the minor groove side.sing two highly conserved sequences. In contrast.lass 2 enzymes share an anti-parallel beta-sheet formation that binds to the major groove side of the acceptor stem. Based on their mode of binding to the tRNA acceptor stem.oth classes of tRNA synthetases have been subdivided into three subclasses.esignated 1a.b.c and 2a.b.c. Class 1a (Arg.ys.le.eu.et.al) possess an RNA-binding domain with an alpha-helix-bundle fold; the binding of the anticodon of tRNA to the RNA-binding domain induces a conformation change in the catalytic domain of the enzyme .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009080:Aminoacyl-tRNA synthetase, class 1a, anticodon-binding
IPR002300:tRNA-synt_1 
Evalue:-9 
Location:639-679IPR013155:Anticodon_1 
Evalue:-6.03151702880859 
Location:725-871IPR009008:ValRS_IleRS_edit 
Evalue:0 
Location:277-450IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:554-576IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:515-533IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:176-193IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:202-218IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:235-248IPR001412:AA_TRNA_LIGASE_I 
Evalue:0 
Location:91-102IPR002302:TRNASYNTHLEU 
Evalue:0 
Location:587-597
SequencesProtein: SYLM_HUMAN (903 aa)
mRNA: NM_015340
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01869
  Level 3 annotation:
    leucyl-tRNA synthetase
  Level 2 annotation:
    Valine
     leucine and isoleucine biosynthesis
    Aminoacyl-tRNA biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 33 residues, 45405078-45405176Exon2: 24 residues, 45408078-45408144Exon3: 87 residues, 45410928-45411183Exon4: 45 residues, 45416740-45416869Exon5: 32 residues, 45433977-45434069Exon6: 22 residues, 45436164-45436225Exon7: 32 residues, 45463386-45463476Exon8: 50 residues, 45475238-45475382Exon9: 38 residues, 45490738-45490846Exon10: 55 residues, 45492963-45493123Exon11: 37 residues, 45502187-45502292Exon12: 40 residues, 45505192-45505308Exon13: 96 residues, 45508012-45508296Exon14: 35 residues, 45512770-45512869Exon15: 48 residues, 45516937-45517075Exon16: 35 residues, 45529630-45529731Exon17: 63 residues, 45532589-45532772Exon18: 58 residues, 45534398-45534568Exon19: 28 residues, 45536714-45536792Exon20: 39 residues, 45540492-45540604Exon21: 44 residues, 45558324-45558452Exon22: 497 residues, 45563846-45565332Exon23: 2 residues, -Jump to SYLM_HUMAN  
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Loci Cluster (Details)Loci: 4597 45771951-45812966 ~-41K 25552(SLC6A20)(-)Loci: 3352 45405078-45565332 ~-160K 25548(LARS2)(+)Link out to UCSC