Q9C291
Gene name |
mus-23 (B11O9.50, NCU08730) |
Protein name |
Double-strand break repair protein mus-23 |
Names |
Recombinational repair protein mus-23 |
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU08730 |
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 Q9C291
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9C291-F1 | Predicted | AlphaFoldDB |
No variants for Q9C291
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9C291 | |||||
No associated diseases with Q9C291
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| Mre11 complex | Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins. |
| site of double-strand break | A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3'-5'-exodeoxyribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| single-stranded DNA endodeoxyribonuclease activity | Catalysis of the hydrolysis of ester linkages within a single-stranded deoxyribonucleic acid molecule by creating internal breaks. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| double-strand break repair via homologous recombination | The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule. |
| double-strand break repair via nonhomologous end joining | The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear. |
| meiotic DNA double-strand break formation | The cell cycle process in which double-strand breaks are generated at defined hotspots throughout the genome during meiosis I. This results in the initiation of meiotic recombination. |
| mitochondrial double-strand break repair via homologous recombination | The repair of a double-strand break in mitochondrial DNA in which the broken DNA molecule is repaired using homologous sequences. |
| mitotic G2 DNA damage checkpoint signaling | A mitotic cell cycle checkpoint that detects and negatively regulates progression through the G2/M transition of the cell cycle in response to DNA damage. |
| mitotic intra-S DNA damage checkpoint signaling | A mitotic cell cycle checkpoint that slows DNA synthesis in response to DNA damage by the prevention of new origin firing and the stabilization of slow replication fork progression. |
| telomere maintenance | Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPRSEADTIR | ILVSTDNHVG | YAERHPVRKD | DSWRTFDEIM | QIAKKQDVDM | VLLGGDLFHE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NKPSRKSMYQ | VMRSLRKHCL | GMKPCELEFL | SDAAEVFEGA | FPFVNYEDPD | INVAIPVFSI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HGNHDDPSGD | GHYCSLDLLQ | AAGLVNYFGR | VPEADNIHVK | PILLQKGRTK | MALYGLSNVR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DERMHRTFRD | NKVRFYRPNQ | QKNDWFNLLA | LHQNHYAHTR | TSYVAENMLP | DFMDLVIWGH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EHECLIDPVR | NPETGFHVMQ | PGSSVATSLV | PGEAVPKHVA | ILNITGRKFE | VDKIPLKTVR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PFVTREIVLA | SDKRFKGLDK | QNNRHEITKR | LMVIVNEMIE | EANAEWRAVH | AEDDDMDEDM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EPPLPLVRLK | VDYTAPDGAR | YEVENPHRFS | NRFTGKVANH | NDVVRFHCNT | KGKKNVATAP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GVREDIAEIL | ESADTIKVDN | LVQEFFAQQS | LKILPQAPFS | DAVNQFVSKD | DKHAVEMFVI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ESLSTQVKEL | LQLDDDKIVD | LDAHIQDFRQ | VMEKSFDAGQ | HKQAQRTKRF | KRKPDGWDSD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LDGHWINQPQ | ALEDIPAEVE | PKGNDRPTKR | VPTSGVTFSD | EDEDMDMDNQ | PVPIRAAPKR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GAAAKTTAAA | KKAAPGKKAA | PAKKAAPAKK | AAPAKKAPAR | GRKKKTPFVD | SDEEEEEDYP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EDDDEEEEEA | DEEEEDVIME | DDEEDPPAPP | PKPKATSRVA | STRASARATP | VRATPARATQ |
| 730 | |||||
| ARLRLRRPPK | PGLLARRLG |