Q9USG9
Gene name |
SPCP31B10.05 |
Protein name |
Probable tyrosyl-DNA phosphodiesterase |
Names |
Tyr-DNA phosphodiesterase |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPCP31B10.05 |
EC number |
|
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 Q9USG9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9USG9-F1 | Predicted | AlphaFoldDB |
No variants for Q9USG9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9USG9 | |||||
No associated diseases with Q9USG9
No regional properties for Q9USG9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9USG9 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3'-deoxyribose phosphate lyase activity | Catalysis of the conversion of a 3'-deoxyribose phosphate in DNA to a 3'-phosphate. |
| 3'-tyrosyl-DNA phosphodiesterase activity | Catalysis of the hydrolysis of 3'-phosphotyrosyl groups formed as covalent intermediates (in DNA backbone breakage) between DNA topoisomerase I and DNA. |
| double-stranded DNA binding | Binding to double-stranded DNA. |
| exonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' or 5' end. |
| single-stranded DNA binding | Binding to single-stranded DNA. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| base-excision repair | In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. |
| double-strand break repair | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. |
| single strand break repair | The repair of single strand breaks in DNA. Repair of such breaks is mediated by the same enzyme systems as are used in base excision repair. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTLEPEKRR | QHEDKSNEII | DSPIFLNKIS | ALPESENVHC | LLLKQLIGSP | QLKQTWQFNF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CVDLNFLLEN | MHASVFPTVD | VRITHGYDSK | SDSLARLTAQ | MNHCPVNVKL | YSVYVPMWGT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HHSKIMVNFF | KDDSCQIVIH | TANLVEPDWI | GMSQAIFKTP | LLYPKANDSL | STSSVPEYGN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PSKIRKHEGS | LDIKDDRNCD | IIDVDSAFEN | FKHKSDTRSS | DDLGVIGRQF | QQDFLAYLKN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YRHTYELIEK | LKMYDFSAIR | AIFIGSVPGK | FEGEEESSWG | LGKLKKILKM | LEKDSKKDEK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TKFEESDICI | SQCSSMGSFG | PKQEYIAELT | DGFGCQRGNW | KFLFPTVKEV | QQSMLGWQSG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SSIHFNILGK | TAASQVETLK | KGKNLCKWVA | MKAGRQRVAP | HIKTYMRFSN | DGELLRWVLV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TSANLSKPAW | GTLEGHKAKS | RSTRGLRIRS | YEAGVLLYPK | LFEESQRAPC | IMTPTYKTNT |
| 490 | 500 | 510 | 520 | 530 | |
| PNLDEKRREF | YGKRVIGVRM | CWDFPPVEYE | DKDEIWSPVI | NRTDKDWLGY | VWPPNW |