We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU01366
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01366
General rule information
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| Accession | PRU01366 |
| Dates | 05-MAY-2023 (Created)
05-MAY-2023 (Last updated, Version 2) |
| Data class | Domain; |
| Predictors |
PROSITE; PS52022; PV_NS1_NUC |
Name | Parvovirus (PV) NS1 nuclease (NS1-Nuc) domain profile |
| Function | The PV NS1-Nuc domain plays an important role in the "rolling hairpin" replication of the single-stranded parvoviral DNA genome, recognizing origin of replication sequences in double-stranded DNA, and cleaving (i.e., nicking) single-stranded DNA at a nearby site known as the terminal resolution site (trs). Since the DNA encountered by NS1 is double- stranded, it is assumed that binding of NS1 to its target sequences in dsDNA induces strand separation nearby, allowing for the endonuclease activity of NS1 to cleave at the trs site. |
| Scope(s) |
Viruses |
| Example(s) | P07300; |
Propagated annotation
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Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=a divalent metal cation; Xref=CHEBI:60240; |
| end case | |
| SUBCELLULAR LOCATION | Host nucleus. |
Keywords
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| DNA-binding | |
| Host nucleus | |
| DNA replication | |
| Nucleotide-binding | |
| case <FTTag:act_site> | |
| Endonuclease | |
| Hydrolase | |
| Nuclease | |
| Covalent protein-DNA linkage | |
| end case | |
| case <FTGroup:1> | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0006260; Biological process:DNA replication | |
| GO:0003677; Molecular function:DNA binding | |
| GO:0042025; Cellular component:host cell nucleus | |
| case <FTGroup:1> | |
| GO:0046872; Molecular function:metal ion binding | |
| end case | |
| case <FTTag:act_site> | |
| GO:0004519; Molecular function:endonuclease activity | |
| end case | |
Features
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| From: PS52022 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="PV NS1-Nuc #" | |||||||||
| MOTIF | 100 | 102 | /note="RCR-2" | H-[FWILMVACGTSYPH]-H | ||||||||
| MOTIF | 175 | 179 | /note="RCR-3" | Y-x(3)-K | ||||||||
| ACT_SITE | 175 | 175 | /note="For nuclease activity" | act_site | Y | |||||||
| BINDING | 93 | 93 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
[ED] | 1 | |||||||
| BINDING | 100 | 100 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
H | 1 | |||||||
| BINDING | 102 | 102 | /ligand="a divalent metal cation #1" /ligand_id="ChEBI:CHEBI:60240" |
H | 1 | |||||||
Additional information
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| Size range | 69-253 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Viruses [26] All [ 26 ]
- Retrieve set of proteins with 3D structure for this domain