Q8CP23
Gene name |
dnaG |
Protein name |
DNA primase |
Names |
|
Species |
Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) |
KEGG Pathway |
sep:SE_1249 |
EC number |
2.7.7.101: Nucleotidyltransferases |
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 Q8CP23
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8CP23-F1 | Predicted | AlphaFoldDB |
No variants for Q8CP23
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8CP23 | |||||
No associated diseases with Q8CP23
6 regional properties for Q8CP23
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, CHC2-type | 4 - 97 | IPR002694 |
| domain | TOPRIM domain | 260 - 341 | IPR006171 |
| domain | DNA primase, DnaG | 2 - 416 | IPR006295 |
| domain | DNA helicase, DnaB-like, N-terminal | 459 - 556 | IPR007693 |
| domain | DNA primase, catalytic core, N-terminal | 127 - 253 | IPR013264 |
| domain | Bacterial DnaG primase, TOPRIM domain | 260 - 338 | IPR034151 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.101 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| DNA-directed RNA polymerase complex | A protein complex that possesses DNA-directed RNA polymerase activity. |
| primosome complex | Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
| DNA primase activity | Catalysis of the synthesis of a short RNA primer on a DNA template, providing a free 3'-OH that can be extended by DNA-directed DNA polymerases. |
| zinc ion binding | Binding to a zinc ion (Zn). |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRIDQSVIDE | IKNKTDILDL | VSEYVKLEKR | GRNYIGLCPF | HDEKTPSFTV | SEDKQICHCF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GCKKGGNVFQ | FTQEIKDVSF | VEAVKDLGER | VNIQVDIGQN | QTNSSTKIAS | DELKMIEMHE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LIKDYYHYAL | MKTVEGEEAL | NYLHERGFTD | DLIKEREIGY | APDNSHFCHD | FLEKKGYDIE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LAFEAGLLSR | NEENFTYFDR | FRNRIMFPLK | NGQGRIVGYS | GRTYTDQEPK | YLNSPETPIF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QKRRILYNLN | KARKFIRKQD | EIILLEGFMD | VIKSDYAGLK | QVVASMGTQL | SQEHITFLQK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTQNVTLMFD | GDYAGKEATL | KTGQALLNQG | LNVYVVQLPS | GMDPDDYIRK | YDNEQFLKFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QQDKQSFVLF | KVKMYQNEIN | HNDLAYEKHF | KETVRDLSLV | NSGIIRNKLI | QNIADIFKVN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PETIQYELDA | TYQHQMSSNT | YPTFQDEPSK | QQLILGRLTK | NEKAERALIK | HLTKDKDTFL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NYYQKIVPED | FTNSYLKRIF | SYLYDYYSKN | DYYTISDMMQ | YIESNELREV | LIELDQYHLN |
| 550 | 560 | 570 | 580 | 590 | |
| DEPYENEIED | YIQIIKNNNN | EDSLESLNYK | LREASRIGDS | ELQKYYLQLI | VNKNKNRM |