O27088
Gene name |
top6B |
Protein name |
Type 2 DNA topoisomerase 6 subunit B |
Names |
Type II DNA topoisomerase VI subunit B, TopoVI-B |
Species |
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) |
KEGG Pathway |
mth:MTH_1007 |
EC number |
5.6.2.2: Enzymes altering nucleic acid conformation |
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 O27088
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O27088-F1 | Predicted | AlphaFoldDB |
No variants for O27088
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O27088 | |||||
No associated diseases with O27088
1 regional properties for O27088
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha carbonic anhydrase domain | 28 - 64 | IPR001148 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.2.2 | Enzymes altering nucleic acid conformation |
| 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 |
3 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 topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA topological change | The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number. |
| DNA unwinding involved in DNA replication | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MARQALDLFD | EGFQELTPSE | FFRKNKQMLG | FTGKIRSLTI | VFHELITNSF | DAAEEAGILP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EIKIDLKRIG | KDHYILRHQD | NGPGIPEKYI | PKVFCTMFAG | SKFRNIQSRG | QQGLGCSGCV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLSQMTTGKP | VKVISGTMEN | GELKGVKMTL | KMDVKKNQGL | ILEKEEVEVD | GTGVCIELHF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KDVSYSLSEQ | GAYEYIRRTM | IANPHARIVF | NDPTGNRYVF | NRASDVIPPM | PKEVLPHPWG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VTADDLIFMA | KHTDKRRFGS | MLKSNLSRMS | SMKIKELEEL | TGIDLNKRPK | DMKWEEAEQI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VEAFKKMKFM | SPPTSGLIPI | GEEQIDKGMK | EILQPEFTAT | VTRKPKTYRG | GIAFIVEAGI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AYGGNSGRLV | GDQRKAEIMR | FANRVPLTFD | AGSCAITEGV | KSLDWKRYGI | RDLENAPISI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FVNVVSTNVP | YLSTGKQSVS | PEPEILGEIR | QATMIVARKL | HKYLRKKKAA | KEEAQRAKIF |
| 490 | 500 | 510 | 520 | ||
| ESYVPVIIKQ | AALLAEREEP | DYRELLDTVT | RRAKLEILGG | ITE |