Q29FC1
Gene name |
Gen (GA10481) |
Protein name |
Flap endonuclease GEN |
Names |
Flap structure-specific endonuclease GEN, Xpg-like endonuclease |
Species |
Drosophila pseudoobscura pseudoobscura (Fruit fly) |
KEGG Pathway |
dpo:Dpse_GA10481 |
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 Q29FC1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q29FC1-F1 | Predicted | AlphaFoldDB |
No variants for Q29FC1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q29FC1 | |||||
No associated diseases with Q29FC1
4 regional properties for Q29FC1
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5'-3' exodeoxyribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule. |
| 5'-flap endonuclease activity | Catalysis of the cleavage of a 5' flap structure in DNA, but not other DNA structures; processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. |
| crossover junction endodeoxyribonuclease activity | Catalysis of the endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). |
| double-stranded DNA 3'-5' exodeoxyribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a double-stranded DNA molecule. |
| endodeoxyribonuclease activity | Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks. |
| four-way junction DNA binding | Binding to a DNA segment containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices. |
| metal ion binding | Binding to a metal ion. |
| single-stranded DNA 3'-5' exodeoxyribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA catabolic process, endonucleolytic | The chemical reactions and pathways resulting in the breakdown of DNA, involving the hydrolysis of internal 3',5'-phosphodiester bonds in one or two strands of deoxyribonucleotides. |
| DNA catabolic process, exonucleolytic | The chemical reactions and pathways resulting in the breakdown of DNA, involving the hydrolysis of terminal 3',5'-phosphodiester bonds in one or two strands of deoxyribonucleotides. |
| double-strand break repair | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGVKELWTVL | TPHAERKPIN | ELRGKKVAID | LAGWVCESLN | VVDYFVHPRH | HLKNLFFRTC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YLIWEQVTPV | FVLEGVAPKL | KGQVIAKRNE | LQFRGVRPKD | AATGTQTAAK | VDKGRTRFNH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLKQCETLLL | SMGIQCVQGP | GEAEAYAAFL | NKHGLVDGVI | SQDSDCFAYG | AIRVYRNFSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| STQGAQAAAG | GAVDIYDMRE | ITSRMDFGQH | KIIVMALLCG | CDYCPDGIGG | IGKDGVLKLF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NKYKESEILD | RLRNWRAETD | KYNALEMRVD | DKSICSNCGH | IGRTQSHTKS | GCSVCRTKRG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CDKTLWKEQR | LSIKAELILR | RKALLAPEFP | NEEIISEFLS | EPPTIPNLNL | GWRQPNLVKF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IKQIGHLLQW | PEIYCFQKFF | PILTRWQVQQ | AARTNAIGRV | ELVQPVDIIK | KRTVKGVASL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ELRWQDPSGS | FQGLIPDKQI | SEFELEHPKG | IEELYYTVEP | LDMLEAAYPD | LVASFLKSKE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KPPKKATRKK | KTDPLSAIEN | IPETLDKQKA | NPAKPKRVVK | KKKAPTEQAQ | PSLQQFLRRE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KIGGTPVKDS | LPQMAQLPQQ | CSTPITKFLP | SDLESDCDAV | EFDMSDVVNG | IISNPNARPT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VTRHEGRQLH | YEALSDDLSM | RLAQLSLRKD | ELQEEPLPPV | AEHKRDLSLV | EHLPQSKRLS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LDDSFDLLVK | GDLKKVPHLI | QPIRTPVDRF | KHQHRISEHL | PQPAVEPAAN | VSYFFNQSSD |
| 730 | 740 | 750 | |||
| NADAFEQLMN | SSLGIQEQAE | EDEEEEDDLV | VISD |