Q4L5V2
Gene name |
topA |
Protein name |
DNA topoisomerase 1 |
Names |
DNA topoisomerase I, Omega-protein, Relaxing enzyme, Swivelase, Untwisting enzyme |
Species |
Staphylococcus haemolyticus (strain JCSC1435) |
KEGG Pathway |
sha:SH1664 |
EC number |
5.6.2.1: 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 Q4L5V2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4L5V2-F1 | Predicted | AlphaFoldDB |
No variants for Q4L5V2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4L5V2 | |||||
No associated diseases with Q4L5V2
1 regional properties for Q4L5V2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha carbonic anhydrase domain | 28 - 64 | IPR001148 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.2.1 | Enzymes altering nucleic acid conformation |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromosome | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. |
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 topoisomerase type I (single strand cut, ATP-independent) activity | Catalysis of a DNA topological transformation by transiently cleaving one DNA strand at a time to allow passage of another strand; changes the linking number by +1 per catalytic cycle. |
| metal ion binding | Binding to a metal ion. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADNLVIVES | PAKAKTIEKY | LGKKYKVIAS | MGHVRDLPRS | QMGVDVEDNY | EPKYITIRGK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPVVKDLKKY | AKKAKNVFLA | SDPDREGEAI | AWHLSKILEL | DDSKENRVVF | NEITKDAVKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SFKHPRGIEM | DLVDAQQARR | ILDRLVGYNI | SPVLWKKVKK | GLSAGRVQSV | ALRLVIDREN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EIRNFKPEEY | WSIEGEFRYK | KSKFTAKFLH | YKNKPFKLKT | KKDVEKVTAE | LDGDKFEITN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VNKKEKTRNP | ANPFTTSTLQ | QEAARKLNFK | ARKTMMLAQQ | LYEGIDLKRQ | GTVGLITYMR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TDSTRISQTA | KDEAKQYIED | KYGKDYLSNR | TAKGKQGDQD | AHEAIRPTST | LRTPYEMKAY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LTRDQHRLYK | LIWERFVASQ | MAPAILDTVA | LDVTQNNIKF | RANGQTIKFK | GFMTLYVEAK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DDKDNEKENK | LPNLSKGDEV | TATQIEPAQH | FTQPPPRYTE | ARLVKTLEEL | KIGRPSTYAP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TIDTIQKRNY | VKLESKRFVP | TELGEIVYEQ | VKDYFPEIID | VEFTVNMETL | LDKIAEGDIG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| WRKVIDNFYG | SFKLDVERAE | EEMEKVEIKD | EPAGEDCEVC | GSPMVIKMGR | YGKFMACSNF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PDCRNTKAIV | KTIGVTCPKC | KDGDVVERKS | KKNRLFYGCS | NYPECDFISW | DKPVGRDCPK |
| 670 | 680 | ||||
| CNHYLMEHKK | GRSSQVICSN | CDYKEEVQK |