P04526
Gene name |
44 |
Protein name |
Sliding-clamp-loader large subunit |
Names |
EC 3.6.4.- , Clamp loader gp44 subunit , Gene product 44 , gp44 |
Species |
Enterobacteria phage T4 (Bacteriophage T4) |
KEGG Pathway |
vg:1258787 |
EC number |
3.6.4.-: Acting on ATP; involved in cellular and subcellular movement |
Protein Class |
REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT (PTHR11669) |
Descriptions
Clamp loaders are AAA+ ATPases that facilitate high-speed DNA replication. The difference between the active and inactive conformations of the AAA+ module is mainly due to a change in the angle between Domain 1 (residues 1-120) and Domain 2 (residues 160-230) of the AAA+ module. In switching from the active to the inactive conformaion, Domain 2 rotates towards Domain1. This leads to a more closed conformation for the AAA+ module in the inactive conformation.
Autoinhibitory domains (AIDs)
Target domain |
1-120 (AAA+ ATPase domain) |
Relief mechanism |
Ligand binding |
Assay |
Mutagenesis experiment, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
7 structures for P04526
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3U5Z | X-ray | 350 A | B/C/D/E/L/M/N/O | 1-319 | PDB |
| 3U60 | X-ray | 334 A | B/C/D/E | 1-319 | PDB |
| 3U61 | X-ray | 320 A | B/C/D/E | 1-319 | PDB |
| 8UH7 | X-ray | 263 A | B/C/D/E | 1-319 | PDB |
| 8UK9 | X-ray | 310 A | B/C/D/E/K/L/M/N | 1-319 | PDB |
| 8UNF | EM | 315 A | B/C/D/E | 1-319 | PDB |
| 8UNH | EM | 321 A | B/C/D/E | 1-319 | PDB |
No variants for P04526
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P04526 | |||||
No associated diseases with P04526
4 regional properties for P04526
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.- | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR11669 | REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT |
| PANTHER Subfamily | PTHR11669:SF5 | REPLICATION FACTOR C SUBUNIT 2 |
| PANTHER Protein Class | DNA-directed DNA polymerase | |
| PANTHER Pathway Category |
DNA replication RFC |
|
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 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 |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA clamp loader activity | Facilitating the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their closing around the DNA duplex, driven by ATP hydrolysis. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| bidirectional double-stranded viral DNA replication | A viral DNA replication process where replication occurs in both directions from the starting point. This creates two replication forks, moving in opposite directions. |
| 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 the origin recognition complex, 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MITVNEKEHI | LEQKYRPSTI | DECILPAFDK | ETFKSITSKG | KIPHIILHSP | SPGTGKTTVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KALCHDVNAD | MMFVNGSDCK | IDFVRGPLTN | FASAASFDGR | QKVIVIDEFD | RSGLAESQRH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRSFMEAYSS | NCSIIITANN | IDGIIKPLQS | RCRVITFGQP | TDEDKIEMMK | QMIRRLTEIC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KHEGIAIADM | KVVAALVKKN | FPDFRKTIGE | LDSYSSKGVL | DAGILSLVTN | DRGAIDDVLE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SLKNKDVKQL | RALAPKYAAD | YSWFVGKLAE | EIYSRVTPQS | IIRMYEIVGE | NNQYHGIAAN |
| 310 | |||||
| TELHLAYLFI | QLACEMQWK |