Q7T6Y4
Gene name |
MIMI_L318 |
Protein name |
Probable DNA polymerase family X |
Names |
|
Species |
Acanthamoeba polyphaga mimivirus (APMV) |
KEGG Pathway |
vg:9924935 |
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
0 structures for Q7T6Y4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for Q7T6Y4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7T6Y4 | |||||
No associated diseases with Q7T6Y4
6 regional properties for Q7T6Y4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DNA-directed DNA polymerase X | 10 - 346 | IPR002054 |
| domain | DNA polymerase beta-like, N-terminal domain | 29 - 81 | IPR010996 |
| domain | DNA polymerase lambda, fingers domain | 104 - 155 | IPR018944 |
| binding_site | DNA polymerase family X, binding site | 190 - 209 | IPR019843 |
| domain | DNA polymerase beta, palm domain | 161 - 274 | IPR028207 |
| domain | DNA polymerase beta, thumb domain | 281 - 346 | IPR029398 |
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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| virion component | Any constituent part of a virion, a complete fully infectious extracellular virus particle. |
3 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. |
| lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| 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 |
| MNSKIIEQFN | LLEKQVDAEY | LNSKVENDLK | EETMNRFRLK | SIKKALSILK | NLDFEITDAN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DVKGIPGIGA | GTIKRIKEIL | ETGKLHDLKD | KFSPEKQKQI | EGIQELENVI | GIGSSTAKKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ISQYGIRSVD | DLKKAIETGK | VKVSTSIMLG | LKYYGIVQRD | IPRKEITAIE | KLLSKEAHKI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DPDLEIIICG | SYRRGKKTSG | DIDVLMYHPK | MKTSKEMLHP | EKFDLEPYFN | LYIDRLTEKG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FLIDDITFNP | NKKYMGFCKY | KLNPVRRIDI | RFIPYNSLAP | AMLYFTGPME | LNTKMRSAAK |
| 310 | 320 | 330 | 340 | 350 | |
| KRKMILNEYG | LFKTDKNGAQ | IPLDTKSEAD | IFHALGMDYL | TPQQRELYSS | GKIH |