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0SYH_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHARS
DescriptionHistidyl-trna synthetase (ec 6.1.1.21) (histidine--trna ligase) (hisrs).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (NAS)
0005524 ATP binding (NAS)
0004821 histidine-tRNA ligase activity (NAS)
0006412 protein biosynthesis (NAS)

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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)
A conserved domain of 46 amino acids.alled WHEP-TRS has been shown to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases. This domain is present one to sixtimes in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain.nd six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl-tRNA synthetase and histidyl-tRNA synthetase.nd the mammalian.nsect.ematode and plant glycyl-tRNA synthetases . This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
  IPR000738:WHEP-TRS
tRNA synthetases.r tRNA ligases are involved in protein synthesis. This domain is found in histidyl.lycyl.hreonyl and prolyl tRNA synthetases it is probably the anticodon binding domain .
  IPR004154: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.Class-II tRNA synthetases do not share a high degree of similarity.owever at least three conserved regions are present . Histidyl-tRNA synthetase () is an alpha2 dimer that belongs to class IIa. Every completed genome includes a histidyl-tRNA synthetase. Apparent second copies from Bacillus subtilis.ynechocystis sp..nd Aquifex aeolicus are slightly shorter.ore closely related to each other than to other hisS proteins.nd not demonstrated to act as histidyl-tRNA synthetases (see ). Theregulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c).nd related proteins from other species designated eIF-2 alpha kinase.ave a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his).n indicator of amino acid starvation.ut these regulatory proteins are not orthologous.
  IPR004516:Histidyl-tRNA synthetase, class IIa
The RNA-binding domains of the ribosomal protein S15 and the influenza virus non-structural protein NS1 share the same structural fold.onsisting of three helices in an irregular array. S15 is one of 21 proteins in the small.acterial 30S ribosomal subunit.nd is required for assembly of the subunit through its binding to 16S rRNA . The multifunctional glutamyl-prolyl-tRNA synthase (EPRS) contains three tandem repeats linking two catalytic domains.ll three of which contribute to RNA-binding; the second repeated element bears structural resemblance to the S15/NS1 RNA-binding domain .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009068:S15/NS1, RNA-binding
IPR002314:tRNA-synt_2b 
Evalue:-39.2146682739258 
Location:72-234IPR004154:HGTP_anticodon 
Evalue:-24.3665313720703 
Location:410-501IPR000738:WHEP-TRS 
Evalue:-19.7958793640137 
Location:7-60
SequencesProtein: SYH_HUMAN (509 aa)
mRNA: NM_002109
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01892
  Level 3 annotation:
    histidyl-tRNA synthetase
  Level 2 annotation:
    Histidine metabolism
    Aminoacyl-tRNA biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 142 residues, 140033674-140034097Exon2: 51 residues, 140034447-140034594Exon3: 41 residues, 140034785-140034902Exon4: 83 residues, 140036422-140036665Exon5: 44 residues, 140036757-140036885Exon6: 33 residues, 140037095-140037189Exon7: 35 residues, 140037423-140037522Exon8: 38 residues, 140037676-140037784Exon9: 44 residues, 140038770-140038896Exon10: 34 residues, 140039556-140039652Exon11: 42 residues, 140042868-140042988Exon12: 32 residues, 140050623-140050713Exon13: 59 residues, 140050983-140051155Exon14: 2 residues, -Jump to SYH_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3481 140051201-140059073 ~-8K 29557(HARSL)(+)Loci: 3482 140146059-140372113 ~-226K 29559(PCDHA1)(+)Loci: 3483 140411162-140413696 ~-3K 29584(PCDHB1)(+)Loci: 3484 140454420-140457146 ~-3K 29585(PCDHB2)(+)Loci: 3485 140460417-140463589 ~-3K 29586(PCDHB3)(+)Loci: 3486 140481764-140485385 ~-4K 29587(PCDHB4)(+)Loci: 3487 140494983-140497887 ~-3K 29588(PCDHB5)(+)Loci: 3488 140510022-140513050 ~-3K 29589(PCDHB6)(+)Loci: 3489 140532426-140536140 ~-4K 29592(PCDHB7)(+)Loci: 3490 140541163-140545979 ~-5K 29593(PCDHB16)(+)Loci: 3491 140552135-140555397 ~-3K 29594(PCDHB10)(+)Loci: 3492 140559531-140562801 ~-3K 29596(PCDHB11)(+)Loci: 3493 140568474-140571880 ~-3K 29597(PCDHB12)(+)Loci: 3494 140573692-140577177 ~-3K 29598(PCDHB13)(+)Loci: 3495 140583261-140586042 ~-3K 29599(PCDHB14)(+)Loci: 3496 140605330-140607983 ~-3K 29601(PCDHB15)(+)Loci: 4735 140662380-140663796 ~-1K 29602(SLC25A2)(-)Loci: 3497 140690435-140872730 ~-182K 29604(PCDHGA1)(+)Loci: 4736 140874772-140978691 ~-104K 29642(DIAPH1)(-)Loci: 4737 141013153-141041984 ~-29K 29650(CENTD3)(-)Loci: 4734 140033674-140051155 ~-17K 29556(HARS)(-)Link out to UCSC