Q1RJM1
Gene name |
dnaQ (RBE_0362) |
Protein name |
DNA polymerase III subunit epsilon |
Names |
|
Species |
Rickettsia bellii (strain RML369-C) |
KEGG Pathway |
rbe:RBE_0362 |
EC number |
2.7.7.7: 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 Q1RJM1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1RJM1-F1 | Predicted | AlphaFoldDB |
No variants for Q1RJM1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1RJM1 | |||||
No associated diseases with Q1RJM1
3 regional properties for Q1RJM1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 7 - 14 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 193 - 206 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 338 - 352 | IPR018181-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.7 | Nucleotidyltransferases |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| exonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' or 5' end. |
| metal ion binding | Binding to a metal ion. |
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 |
| MSSLREIILD | TETTGLDPKG | GHRIVEIGAI | EMVNKVLTGR | HFHFYLNPER | DMPFEAYRIH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GISGEFLKDK | PLFHTIADDF | LEFIADSKLV | IHNAPFDVKF | LNHELSLLKR | AEIKLLELEH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AIDTLVMARS | MFPGSKYSLD | ALCKRFKVDN | SGRQLHGALK | DAALLAEVYV | ELTGGRQSAF |
| 190 | 200 | 210 | 220 | ||
| KMLDKAAKIN | NLSYNRLDSQ | AHRNIPVIKP | TKEELQKHKE | FLSRVLKQA |