Summary: Toprim domain
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Toprim domain Provide feedback
This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins . Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity . DNA primase EC:22.214.171.124 is a nucleotidyltransferase it synthesises the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division . This family also includes the atypical archaeal A subunit from type II DNA topoisomerases . Type II DNA topoisomerases catalyse the relaxation of DNA supercoiling by causing transient double strand breaks.
Aravind L, Leipe DD, Koonin EV; , Nucleic Acids Res 1998;26:4205-4213.: Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. PUBMED:9722641 EPMC:9722641
Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P; , Nature 1997;386:414-417.: An atypical topoisomerase II from Archaea with implications for meiotic recombination. PUBMED:9121560 EPMC:9121560
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR006171
This entry represents the Toprim (topoisomerase-primase) domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR/M DNA repair proteins [PUBMED:9722641]. The Toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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This is families that have a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins .
The clan contains the following 7 members:DUF2220 DUF2399 DUF3854 Toprim Toprim_2 Toprim_3 Toprim_4
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Pfam-B_500 (release 4.2)|
|Author:||Bashton M, Bateman A|
|Number in seed:||136|
|Number in full:||24868|
|Average length of the domain:||107.80 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||17.30 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
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 Toprim domain has been found. There are 82 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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