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23  structures 2053  species 2  interactions 3956  sequences 83  architectures

Family: DNA_ligase_A_M (PF01068)

Summary: ATP dependent DNA ligase domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

ATP dependent DNA ligase domain Provide feedback

This domain belongs to a more diverse superfamily, including PF01331 and PF01653 [3].

Literature references

  1. Subramanya HS, Doherty AJ, Ashford SR, Wigley DB; , Cell 1996;85:607-615.: Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. PUBMED:8653795 EPMC:8653795

  2. Tomkinson AE, Levin DS; , Bioessays 1997;19:893-901.: Mammalian DNA ligases. PUBMED:9363683 EPMC:9363683

  3. Aravind L, Koonin EV; , J Mol Biol 1999;287:1023-1040.: Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. PUBMED:10222208 EPMC:10222208


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR012310

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), the other NAD (EC), 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 [PUBMED:1988940,PUBMED:1497311].

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 antiparallel beta sheets flanked by alpha helices, whereas domain 2 consists of a five-stranded beta barrel and a single alpha helix, which form the oligonucleotide-binding fold [PUBMED:1437556, PUBMED:11983065].

This domain belongs to a more diverse superfamily, including catalytic domain of the mRNA capping enzyme (INTERPRO) and NAD-dependent DNA ligase (INTERPRO) [PUBMED:8653795].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan DNA_ligase (CL0078), which has the following description:

This superfamily contains both ATP-dependent and NAD dependent DNA ligase enzymes. The family also includes mRNA capping enzymes. The members of this clan were shown to be related by sequence in [1].

The clan contains the following 4 members:

DNA_ligase_A_M DNA_ligase_aden mRNA_cap_enzyme RNA_ligase

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(46)
Full
(3956)
Representative proteomes NCBI
(4137)
Meta
(1269)
RP15
(555)
RP35
(1043)
RP55
(1451)
RP75
(1751)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(46)
Full
(3956)
Representative proteomes NCBI
(4137)
Meta
(1269)
RP15
(555)
RP35
(1043)
RP55
(1451)
RP75
(1751)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(46)
Full
(3956)
Representative proteomes NCBI
(4137)
Meta
(1269)
RP15
(555)
RP35
(1043)
RP55
(1451)
RP75
(1751)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_788 (release 3.0)
Previous IDs: DNA_ligase;
Type: Domain
Author: Finn RD, Bateman A
Number in seed: 46
Number in full: 3956
Average length of the domain: 187.60 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 33.16 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.9 21.9
Trusted cut-off 21.9 21.9
Noise cut-off 21.8 21.8
Model length: 202
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Interactions

There are 2 interactions for this family. More...

DNA_ligase_A_N DNA_ligase_A_C

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DNA_ligase_A_M domain has been found. There are 23 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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