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Links from Protein

Items: 12

1.

NrS-1 polymerase HBD domain

This entry represents the helix bundle domain (HBD) domain of NrS-1 polymerase [1] which together with the N-terminal Prim/Pol domain, is responsible for DNA polymerization and de novo primer synthesis activities. This domain is critical for the primer synthesis activity of NrS-1 polymerase [1]. [1]. 32016421. Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase. Chen X, Su S, Chen Y, Gao Y, Li Y, Shao Z, Zhang Y, Shao Q, Liu H, Li J, Ma J, Gan J;. Nucleic Acids Res. 2020;48:3343-3355. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046818.1
Method:
HMM
2.

DUF5906 domain-containing protein

This is a family of proteins of unknown function found in viruses. This family is a P-loop member whose proteins are thought to be SF3 helicases, which are involved in replication initiation. (from Pfam)

Date:
2024-08-14
Family Accession:
NF040238.4
Method:
HMM
3.

D5 N terminal like

This domain is found in D5 proteins of DNA viruses and bacteriophage P4 DNA primases phages. [1]. 11929537. Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins. Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G;. Mol Microbiol. 2002;43:855-867. [2]. 7636979. The vaccinia virus D5 protein, which is required for DNA replication, is a nucleic acid-independent nucleoside triphosphatase. Evans E, Klemperer N, Ghosh R, Traktman P;. J Virol 1995;69:5353-5361. (from Pfam)

Date:
2024-10-16
Family Accession:
NF020289.5
Method:
HMM
4.

primase-like DNA-binding domain-containing protein

This family includes D5 from Poxviruses which is necessary for viral DNA replication, and is a nucleic acid independent nucleoside triphosphatase. Members of this family are also found outside of poxviruses. This domain is a DNA-binding winged HTH domain. [1]. 7636979. The vaccinia virus D5 protein, which is required for DNA replication, is a nucleic acid-independent nucleoside triphosphatase. Evans E, Klemperer N, Ghosh R, Traktman P;. J Virol 1995;69:5353-5361. (from Pfam)

Date:
2024-10-16
Family Accession:
NF015259.5
Method:
HMM
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
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.

phage/plasmid primase, P4 family

This HMM represents a clade within a larger family of proteins from viruses of bacteria and animals. Members of this family are found in phage and plasmids of bacteria and archaea only. The model describes a domain of about 300 residues, found generally toward the protein C-terminus.

GO Terms:
Molecular Function:
DNA primase activity (GO:0003896)
Biological Process:
DNA replication (GO:0006260)
Date:
2021-09-13
Family Accession:
TIGR01613.1
Method:
HMM
12.

DNA primase family protein

phage/plasmid-associated DNA primase family protein

Date:
2021-03-25
Family Accession:
13928233
Method:
Sparcle
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