P24117
Gene name |
dnaN (MCAP_0002) |
Protein name |
Beta sliding clamp |
Names |
Beta clamp, Sliding clamp, Beta-clamp processivity factor, DNA polymerase III beta sliding clamp subunit, DNA polymerase III subunit beta |
Species |
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) |
KEGG Pathway |
mcp:MCAP_0002 |
EC number |
|
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
1 structures for P24117
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P24117-F1 | Predicted | AlphaFoldDB |
No variants for P24117
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P24117 | |||||
No associated diseases with P24117
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| DNA polymerase III complex | The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3'-5' exonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA-directed DNA polymerase activity | Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNFSINRIVL | LDNLSKAAKV | IDYKNVNPSL | SGIYLNVLND | QVNVITTSGI | LSFKSILNNQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NSDLEVKQEG | KVLLKPKYVL | EMLRRLDDEF | VVFSMVEDNE | LIIKTNNSDF | SIGVLNSEDY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLIGFREKGI | EFNLNPKEVK | KTIYQVFVSM | NENNKKLILT | GLNLKLNNNQ | AIFSTTDSFR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ISQKILEIQS | DNNEDIDITI | PFKTALELPK | LLDNAENLKI | IIVEGYITFI | IDNVIFQSNL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IDGKFPNVQI | AFPTKFETII | TVKQKSILKV | LSRFDLVADD | GLPAIVNIKV | NEDKIEFKSF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ISEVGKYEED | FDDFVIEGNK | SLSISFNTRF | LIDAIKTLSE | DRIELKLINS | TKPIVINNVY |
| 370 | |||||
| DEHLKQVILP | TFLSN |