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0DNL4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLIG4
DescriptionDna ligase iv (ec 6.5.1.1) (polydeoxyribonucleotide synthase ).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (TAS)
0003677 DNA binding (TAS)
0003910 DNA ligase (ATP) activity (TAS)
0000012 single strand break repair (TAS)

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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:
This domain belongs to a more diverse superfamily.ncluding catalytic domain of the mRNA capping enzyme () and NAD-dependent DNA ligase () .
  IPR012310:ATP dependent DNA ligase, central
This region is found in many but not all ATP-dependent DNA ligase enzymes (). It is thought to constitute part of the catalytic core of ATP dependent DNA ligase .
  IPR012309:ATP dependent DNA ligase, C-terminal
The BRCT domain (after the C_terminal domain of a breast cancer susceptibility protein) is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage .or example as found in the breast cancer DNA-repair protein BRCA1. The domain is an approximately 100 amino acid tandem repeat.hich appears to act as a phospho-protein binding domain .A chitin biosynthesis protein from yeast also seems to belong to this group.
  IPR001357:BRCT
This region is found in many but not all ATP-dependent DNA ligase enzymes (). It is thought to be involved in DNA binding and in catalysis. In human DNA ligase I ().nd in Saccharomyces cerevisiae ().his region was necessary for catalysis.nd separated from the amino terminus by targeting elements. In vaccinia virus () this region was not essential for catalysis.ut deletion decreases the affinity for nicked DNA and decreased the rate of strand joining at a step subsequent to enzyme-adenylate formation .
  IPR012308:DNA ligase, N-terminal
DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication.NA repair and DNA recombination. There are two forms of DNA ligase.ne requires ATP ().he other NAD ().he latter being restricted to eubacteria. Eukaryotic.rchaebacterial.iral and some eubacterial DNA ligases are ATP-dependent. The first step in the ligation reaction is the formation of a covalent enzyme-AMP complex. The co-factor ATP is cleaved to pyrophosphate and AMP.ith the AMP being covalently joined to a highly conserved lysine residue in the active site of the ligase. The activated AMP residue is then transferred to the 5phosphate of the nick.efore the nick is sealed by phosphodiester-bond formation and AMP elimination .Vertebrate cells encode three well-characterized DNA ligases (DNA ligases I.II and IV).ll of which are related in structure and sequence. With the exception of the atypically small PBCV-1 viral enzyme.wo regions of primary sequence are common to all members of the family. The catalytic region comprises six conserved sequence motifs (I.II.IIa.V.-VI).otif I includes the lysine residue that is adenylated in the first step of the ligation reaction. The function of the second.ess well-conserved region is unknown. When folded.ach protein comprises of two distinct sub-domains: a large amino-terminal sub-domain (domain 1) and a smaller carboxy-terminal sub-domain (domain 2). The ATP-binding site of the enzyme lies in the cleft between the two sub-domains. Domain 1 consists of two antiparallel beta sheets flanked by alpha helices.hereas domain 2 consists of a five-stranded beta barrel and a single alpha helix.hich form the oligonucleotide-binding fold .
  IPR000977:ATP-dependent DNA ligase
IPR012310:DNA_ligase_A_M 
Evalue:-83.0604782104492 
Location:248-451IPR012309:DNA_ligase_A_C 
Evalue:-18.0222759246826 
Location:476-549IPR001357:BRCT 
Evalue:-15.161150932312 
Location:654-730IPR001357:BRCT 
Evalue:-9.69896984100342 
Location:808-898IPR012308:DNA_ligase_A_N 
Evalue:-4.16115093231201 
Location:14-209
SequencesProtein: DNL4_HUMAN (844 aa)
mRNA: BC037491 NM_002312
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK01971
  Level 3 annotation:
    DNA ligase (ATP)
  Level 2 annotation:
    Other replication
     recombination and repair proteins
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1285 residues, 107657793-107661645Exon2: 26 residues, 107664886-107664959Exon3: 19 residues, 107665832-107665883Exon4: 2 residues, -Jump to DNL4_HUMANExon1: 1285 residues, 107657793-107661645Exon2: 83 residues, 107664886-107665131Exon3: 2 residues, -Jump to DNL4_HUMAN  
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