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0SYSM_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSARS2
DescriptionSeryl-trna synthetase, mitochondrial precursor (ec 6.1.1.11) (serine-- trna ligase) (serrsmt).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (ISS)
0005524 ATP binding (ISS)
0004828 serine-tRNA ligase activity (ISS)
0006434 seryl-tRNA aminoacylation (ISS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
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.Class-II tRNA synthetases do not share a high degree of similarity.owever at least three conserved regions are present . This domain includes the glycine.istidine.roline.hreonine and serine tRNA synthetases.
  IPR002314:tRNA synthetase, class II (G, H, P and S)
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.Class-II tRNA synthetases do not share a high degree of similarity.owever at least three conserved regions are present . Seryl-tRNA synthetase () exists as monomer and belongs to class IIa .
  IPR002317:Seryl-tRNA synthetase, class IIa
The tRNA-binding arm domain is conserved between class I and class II enzymes.onsisting of two alpha helices in an antiparallel hairpin with a left-handed twist. The appended tRNA-binding domains recognize a small number of nucleotides that are conserved specifically in each cognate tRNA species for the discrimination between the cognate and noncognate tRNAs . These nucleotides are called identity elements.nd constitute the identity set. The tRNA-binding arm occurs as the C-terminal domain in some class I enzymes.uch as valyl-tRNA synthetase.nd as the N-terminal domain in some class II enzymes.uch as phenylalanyl-tRNA synthetase.The methicillin resistance protein.emA (factors essential for methicillin resistance).ontains a probable tRNA-binding arm that is similar in structure to those found in tRNA synthetases. In FemA.he tRNA-binding arm is inserted into the C-terminal NAT-like domain.nd is thought to bind tRNA-glycine. FemA.long with FemB and FemX.lays a vital role in peptidoglycan biosynthesis specific to Staphylococci .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR010978:tRNA-binding arm
IPR002314:tRNA-synt_2b 
Evalue:-35.9586067199707 
Location:238-413IPR002317:Seryl_tRNA_N 
Evalue:-1.50863826274872 
Location:58-174IPR002317:TRNASYNTHSER 
Evalue:0 
Location:420-436
SequencesProtein: SYSM_HUMAN (518 aa)
mRNA: CR618695 NM_017827
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 assignmentK01875
  Level 3 annotation:
    seryl-tRNA synthetase
  Level 2 annotation:
    Glycine
     serine and threonine metabolism
    Aminoacyl-tRNA biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 162 residues, 44097746-44098229Exon2: 24 residues, 44098320-44098386Exon3: 33 residues, 44098516-44098609Exon4: 33 residues, 44098700-44098794Exon5: 38 residues, 44100203-44100313Exon6: 31 residues, 44100400-44100488Exon7: 17 residues, 44100573-44100619Exon8: 38 residues, 44100901-44101010Exon9: 18 residues, 44101245-44101293Exon10: 37 residues, 44102241-44102347Exon11: 23 residues, 44102565-44102629Exon12: 20 residues, 44103871-44103926Exon13: 49 residues, 44104006-44104147Exon14: 12 residues, 44104717-44104747Exon15: 34 residues, 44108684-44108780Exon16: 144 residues, 44112949-44113376Exon17: 2 residues, -Jump to SYSM_HUMANExon1: 151 residues, 44097778-44098229Exon2: 24 residues, 44098320-44098386Exon3: 33 residues, 44098516-44098609Exon4: 33 residues, 44098700-44098794Exon5: 36 residues, 44100203-44100307Exon6: 33 residues, 44100394-44100488Exon7: 17 residues, 44100573-44100619Exon8: 38 residues, 44100901-44101010Exon9: 18 residues, 44101245-44101293Exon10: 37 residues, 44102241-44102347Exon11: 23 residues, 44102565-44102629Exon12: 20 residues, 44103871-44103926Exon13: 49 residues, 44104006-44104147Exon14: 12 residues, 44104717-44104747Exon15: 34 residues, 44108684-44108780Exon16: 98 residues, 44112949-44113238Exon17: 2 residues, -Jump to SYSM_HUMAN  
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Loci Cluster (Details)Loci: 3108 43830166-43913010 ~-83K 18756(ACTN4)(+)Loci: 4387 43953451-43955988 ~-3K 18760(LGALS7)(-)Loci: 3109 43971693-43974232 ~-3K 18761(LGALS7)(+)Loci: 4388 44061041-44082201 ~-21K 18769(SIRT2)(-)Loci: 3110 44082454-44091373 ~-9K 18775(NFKBIB)(+)Loci: 4389 44097746-44113376 ~-16K 18777(SARS2)(-)Loci: 3111 44113187-44115497 ~-2K 18779(MRPS12)(+)Loci: 3112 44308259-44361886 ~-54K 18787(PAK4)(+)Loci: 3107 43616179-43770042 ~-154K 18750(RYR1)(+)Link out to UCSC