P03132
Gene name |
Rep68 |
Protein name |
Protein Rep68 |
Names |
|
Species |
Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2) |
KEGG Pathway |
vg:4192013 |
EC number |
3.6.4.12: Acting on ATP; involved in cellular and subcellular movement |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
11 structures for P03132
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1S9H | X-ray | 240 A | A/B/C | 225-490 | PDB |
| 1U0J | X-ray | 210 A | A | 225-490 | PDB |
| 4ZO0 | X-ray | 230 A | A/B/C | 1-206 | PDB |
| 4ZQ9 | X-ray | 260 A | A/B/C | 1-208 | PDB |
| 5DCX | X-ray | 260 A | A/B/C/D/E/F/G/H/I/J/K | 1-224 | PDB |
| 6XB8 | X-ray | 330 A | A/B/C/D | 1-206 | PDB |
| 7JSE | EM | 460 A | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 1-536 | PDB |
| 7JSF | EM | 670 A | A/B/C/D/E/F/G | 2-536 | PDB |
| 7JSG | EM | 520 A | A/B/C/D/E/F/G | 2-536 | PDB |
| 7JSH | EM | 440 A | A/B/C/D/E/F/G | 2-536 | PDB |
| 7JSI | EM | 501 A | A/B/C/D/E/F | 1-536 | PDB |
No variants for P03132
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P03132 | |||||
No associated diseases with P03132
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.12 | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
| modulation by virus of host G1/S transition checkpoint | Any viral process that modulates the frequency, rate or extent of the host cell G1/S transition checkpoint. |
| permeabilization of host organelle membrane involved in viral entry into host cell | Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. |
| suppression by virus of G2/M transition of host mitotic cell cycle | Any viral process that decreases the rate or extent of progression from G2 phase to M phase of the host mitotic cell cycle. |
| viral DNA genome replication | The replication of a viral DNA genome. |
| viral entry via permeabilization of inner membrane | The entry of a non-enveloped virus into the cytoplasm of a host prokaryotic cell, following fusion with the outer membrane, via permeabilization of the plasma (inner) membrane. In the case of some double stranded RNA viruses of prokaryotes this occurs via interaction of a membrane-interacting component of the capsid, leading to depolarization an permeabilization of the plasma membrane. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPGFYEIVIK | VPSDLDGHLP | GISDSFVNWV | AEKEWELPPD | SDMDLNLIEQ | APLTVAEKLQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RDFLTEWRRV | SKAPEALFFV | QFEKGESYFH | MHVLVETTGV | KSMVLGRFLS | QIREKLIQRI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YRGIEPTLPN | WFAVTKTRNG | AGGGNKVVDE | CYIPNYLLPK | TQPELQWAWT | NMEQYLSACL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NLTERKRLVA | QHLTHVSQTQ | EQNKENQNPN | SDAPVIRSKT | SARYMELVGW | LVDKGITSEK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QWIQEDQASY | ISFNAASNSR | SQIKAALDNA | GKIMSLTKTA | PDYLVGQQPV | EDISSNRIYK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ILELNGYDPQ | YAASVFLGWA | TKKFGKRNTI | WLFGPATTGK | TNIAEAIAHT | VPFYGCVNWT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NENFPFNDCV | DKMVIWWEEG | KMTAKVVESA | KAILGGSKVR | VDQKCKSSAQ | IDPTPVIVTS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NTNMCAVIDG | NSTTFEHQQP | LQDRMFKFEL | TRRLDHDFGK | VTKQEVKDFF | RWAKDHVVEV |
| 490 | 500 | 510 | 520 | 530 | |
| EHEFYVKKGG | AKKRPAPSDA | DISEPKRVRE | SVAQPSTSDA | EASINYADRL | ARGHSL |