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Links from Protein

Items: 10

1.

topoisomerase C-terminal repeat-containing protein

This domain is repeated up to five times to form the C-terminal region of bacterial topoisomerase immediately downstream of the zinc-finger motif. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024761.5
Method:
HMM
2.

DNA topoisomerase

This HMM identifies a region shared by DNA topoisomerases of different types, including ATP-independent (type I) topoisomerases such as TopA and TopB, and ATP-dependent reverse gyrases.

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
DNA topoisomerase activity (GO:0003916)
Biological Process:
DNA topological change (GO:0006265)
Date:
2024-10-16
Family Accession:
NF013311.5
Method:
HMM
3.

toprim domain-containing protein

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 [1]. 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 [1]. DNA primase EC:2.7.7.6 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 [2]. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases [4]. Type II DNA topoisomerases catalyse the relaxation of DNA supercoiling by causing transient double strand breaks. [1]. 9722641. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Aravind L, Leipe DD, Koonin EV;. Nucleic Acids Res 1998;26:4205-4213. [2]. 9224947. Cloning and analysis of the dnaG gene encoding Pseudomonas putida DNA primase. Szafranski P, Smith CL, Cantor CR;. Biochim Biophys Acta 1997;1352:243-248. [3]. 8294018. The Haemophilus influenzae dnaG sequence and conserved bacterial primase motifs. Versalovic J, Lupski JR;. Gene 1993;136:281-286. [4]. 9121560. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P;. Nature 1997;386:414-417. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013878.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
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9.
new record, indexing in progress
Family Accession:
10.

type I DNA topoisomerase

This model describes DNA topoisomerase I among the members of bacteria. DNA topoisomerase I transiently cleaves one DNA strand and thus relaxes negatively supercoiled DNA during replication, transcription and recombination events.

Gene:
topA
GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
DNA topoisomerase type I (single strand cut, ATP-independent) activity (GO:0003917)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
DNA replication (GO:0006260)
Biological Process:
DNA topological change (GO:0006265)
Date:
2021-04-27
Family Accession:
TIGR01051.1
Method:
HMM
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