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IPR000977 is a DNA ligase, ATP-dependent.
This entry represents DNA ligases from the three domains of life. <p>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, DNA repair and DNA recombination. There are two forms of DNA ligase, one requires ATP ([ec:6.5.1.1]), the other NAD ([ec:6.5.1.2]), the latter being restricted to eubacteria. Eukaryotic, archaebacterial, viral 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, with 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 5'phosphate of the nick, before the nick is sealed by phosphodiester-bond formation and AMP elimination [[cite:PUB00004738], [cite:PUB00000083]].</p> <p>Vertebrate cells encode three well-characterised DNA ligases (DNA ligases I, III and IV), all of which are related in structure and sequence. With the exception of the atypically small PBCV-1 viral enzyme, two regions of primary sequence are common to all members of the family. The catalytic region comprises six conserved sequence motifs (I, III, IIIa, IV, V-VI), motif I includes the lysine residue that is adenylated in the first step of the ligation reaction. The function of the second, less well-conserved region is unknown. When folded, each 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 antiparallelβ-sheets flanked by α-helices, whereas domain 2 consists of a five-stranded β-barrel and a single α-helix, which form the oligonucleotide-binding fold [[cite:PUB00004409], [cite:PUB00010654]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | DNA ligase (ATP) activity | Catalysis of the reaction: ATP + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + diphosphate + deoxyribonucleotide(n+m). | ||
| Molecular function | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Biological process | DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. | ||
| Biological process | DNA recombination | Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. | ||
| Biological process | DNA biosynthetic process | The cellular DNA metabolic process resulting in the formation of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: DNA ligase 1-like isoform X1 [Cicer arietinum] gi|502145536|ref|XP_004506069.1| | 26 | ||
| – | DNA ligase; TAIR: AT1G66730.1 DNA LIGASE 6; Swiss-Prot: sp|F4HPZ9|LIG6_ARATH DNA ligase 6; TrEMBL-Plants: tr|G7KV95|G7KV95_MEDTR DNA ligase; Found in the gene: LotjaGi1g1v0545100 | 31 | ||
| – | DNA ligase; TAIR: AT1G66730.1 DNA LIGASE 6; Swiss-Prot: sp|F4HPZ9|LIG6_ARATH DNA ligase 6; TrEMBL-Plants: tr|A0A0L9TDF0|A0A0L9TDF0_PHAAN DNA ligase; Found in the gene: LotjaGi1g1v0545100 | 34 | ||
| – | DNA ligase; TAIR: AT1G08130.1 DNA ligase 1; Swiss-Prot: sp|Q42572|DNLI1_ARATH DNA ligase 1; TrEMBL-Plants: tr|A0A072UVT2|A0A072UVT2_MEDTR DNA ligase; Found in the gene: LotjaGi3g1v0485100 | 27 | ||
| – | DNA ligase; TAIR: AT5G57160.1 DNA ligase IV; Swiss-Prot: sp|Q9LL84|DNLI4_ARATH DNA ligase 4; TrEMBL-Plants: tr|K7MBU8|K7MBU8_SOYBN DNA ligase; Found in the gene: LotjaGi6g1v0235200 | 36 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 20.00 |