P40352
SS
Gene name |
RAD26 (GTA1085, YJR035W, J1606) |
Protein name |
DNA repair and recombination protein RAD26 |
Names |
ATP-dependent helicase RAD26 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YJR035W |
EC number |
3.6.4.12: Acting on ATP; involved in cellular and subcellular movement |
Protein Class |
|
Descriptions
Rhp26 is a model protein related to CSB/ERCC6 (Cockayne syndrome B protein/excision repair cross complementation group 6) proteins with key roles in gene expression and DNA repair system. The leucine latch motif at the N-terminus of Rhp26 is responsible for the autoinhibition of the ATPase and chromatin-remodelling activity through its interactions with lobe 2 of the core ATPase domain. The disruption of the leucine latch motif or deletion of the N terminus eliminates the autoinhibition of ATPase and remarkably enhances the chromatin remodelling activity resulting in a hyperactive Rhp26.
Autoinhibitory domains (AIDs)
Target domain |
273-498 (ATPase domain) |
Relief mechanism |
Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for P40352
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5VVR | EM | 580 A | M | 1-1085 | PDB |
| AF-P40352-F1 | Predicted | AlphaFoldDB |
20 variants for P40352
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s10-497352 | 2 | E>A | No | SGRP | |
| s10-497403 | 19 | K>R | No | SGRP | |
| s10-497582 | 79 | T>A | No | SGRP | |
| s10-497595 | 83 | S>Y | No | SGRP | |
| s10-497860 | 171 | K>N | No | SGRP | |
| s10-497978 | 211 | E>Q | No | SGRP | |
| s10-497988 | 214 | E>G | No | SGRP | |
| s10-498141 | 265 | S>L | No | SGRP | |
| s10-498445 | 366 | Q>H | No | SGRP | |
| s10-498571 | 408 | D>E | No | SGRP | |
| s10-498728 | 461 | V>I | No | SGRP | |
| s10-498951 | 535 | N>S | No | SGRP | |
| s10-499151 | 602 | H>N | No | SGRP | |
| s10-500343 | 999 | N>S | No | SGRP | |
| s10-500355 | 1003 | G>D | No | SGRP | |
| s10-500381 | 1012 | I>L | No | SGRP | |
| s10-500400 | 1018 | T>M | No | SGRP | |
| s10-500574 | 1076 | D>A | No | SGRP | |
| s10-500575 | 1076 | D>E | No | SGRP | |
| s10-500595 | 1083 | N>S | No | SGRP |
No associated diseases with P40352
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.12 | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromatin | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent activity, acting on DNA | Catalytic activity that acts to modify DNA, driven by ATP hydrolysis. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| histone H2A-H2B dimer displacement | OBSOLETE. The removal of a H2A-H2B histone dimer from a nucleosome within chromatin. |
| nucleotide-excision repair | A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). |
| regulation of protein complex stability | Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly. |
| regulation of response to DNA damage stimulus | Any process that modulates the frequency, rate or extent of response to DNA damage stimulus. |
| regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage | Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a UV damage stimulus. |
| transcription-coupled nucleotide-excision repair | The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEDKEQQDNA | KLENNESLKD | LGVNVLSQSS | LEEKIANDVT | NFSNLQSLQQ | EETRLERSKT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALQRYVNKKN | HLTRKLNNTT | RISVKQNLRD | QIKNLQSDDI | ERVLKDIDDI | QSRIKELKEQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VDQGAENKGS | KEGLQRPGET | EKEFLIRTGK | ITAFGHKAGF | SLDTANREYA | KNDEQKDEDF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EMATEQMVEN | LTDEDDNLSD | QDYQMSGKES | EDDEEEENDD | KILKELEDLR | FRGQPGEAKD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DGDELYYQER | LKKWVKQRSC | GSQRSSDLPE | WRRPHPNIPD | AKLNSQFKIP | GEIYSLLFNY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QKTCVQWLYE | LYQQNCGGII | GDEMGLGKTI | QVIAFIAALH | HSGLLTGPVL | IVCPATVMKQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WCNEFQHWWP | PLRTVILHSM | GSGMASDQKF | KMDENDLENL | IMNSKPSDFS | YEDWKNSTRT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KKALESSYHL | DKLIDKVVTD | GHILITTYVG | LRIHSDKLLK | VKWQYAVLDE | GHKIRNPDSE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ISLTCKKLKT | HNRIILSGTP | IQNNLTELWS | LFDFIFPGKL | GTLPVFQQQF | VIPINIGGYA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NATNIQVQTG | YKCAVALRDL | ISPYLLRRVK | ADVAKDLPQK | KEMVLFCKLT | KYQRSKYLEF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LHSSDLNQIQ | NGKRNVLFGI | DILRKICNHP | DLLDRDTKRH | NPDYGDPKRS | GKMQVVKQLL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LLWHKQGYKA | LLFTQSRQML | DILEEFISTK | DPDLSHLNYL | RMDGTTNIKG | RQSLVDRFNN |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ESFDVFLLTT | RVGGLGVNLT | GANRIIIFDP | DWNPSTDMQA | RERAWRIGQK | REVSIYRLMV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GGSIEEKIYH | RQIFKQFLTN | RILTDPKQKR | FFKIHELHDL | FSLGGENGYS | TEELNEEVQK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| HTENLKNSKS | EESDDFEQLV | NLSGVSKLES | FYNGKEKKEN | SKTEDDRLIE | GLLGGESNLE |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TVMSHDSVVN | SHAGSSSSNI | ITKEASRVAI | EAVNALRKSR | KKITKQYEIG | TPTWTGRFGK |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| AGKIRKRDPL | KNKLTGSAAI | LGNITKSQKE | ASKEARQENY | DDGITFARSK | EINSNTKTLE |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| NIRAYLQKQN | NFFSSSVSIL | NSIGVSLSDK | EDVIKVRALL | KTIAQFDKER | KGWVLDEEFR |
| NNNAS |