A7E449
Gene name |
dbp2 (SS1G_00071) |
Protein name |
ATP-dependent RNA helicase dbp2 |
Names |
|
Species |
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) |
KEGG Pathway |
ssl:SS1G_00071 |
EC number |
3.6.4.13: Acting on ATP; involved in cellular and subcellular movement |
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 A7E449
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7E449-F1 | Predicted | AlphaFoldDB |
No variants for A7E449
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A7E449 | |||||
No associated diseases with A7E449
5 regional properties for A7E449
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 301 - 309 | IPR000629 |
| domain | Helicase, C-terminal | 383 - 530 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 173 - 343 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 168 - 371 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 149 - 177 | IPR014014 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.13 | 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 |
|---|---|
| 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. |
| ribonucleoprotein complex | A macromolecular complex that contains both RNA and protein molecules. |
6 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. |
| mRNA binding | Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| RNA helicase activity | Unwinding of an RNA helix, driven by ATP hydrolysis. |
| snoRNA binding | Binding to a small nucleolar RNA. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| messenger ribonucleoprotein complex assembly | The aggregation, arrangement and bonding together of proteins and messenger RNA (mRNA) molecules to form a messenger ribonucleoprotein (mRNP) complex. |
| nuclear polyadenylation-dependent mRNA catabolic process | The chemical reactions and pathways occurring in the nucleus and resulting in the breakdown of a messenger RNA (mRNA) molecule, initiated by the enzymatic addition of a sequence of adenylyl residues (polyadenylation) at the 3' end the target mRNA. |
| nuclear-transcribed mRNA catabolic process, nonsense-mediated decay | The nonsense-mediated decay pathway for nuclear-transcribed mRNAs degrades mRNAs in which an amino-acid codon has changed to a nonsense codon; this prevents the translation of such mRNAs into truncated, and potentially harmful, proteins. |
| rRNA processing | Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules. |
| termination of RNA polymerase II transcription | A transcription termination process that completes the production of a primary RNA polymerase II transcript. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSYGGGYGGG | RGGGNGYGNG | DSSYGRGNSY | SNGYSNGGSN | GYSGGGGGGY | GGGRGGSGGG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NVNGYSGGGG | GYGGGGGYGG | GGGAGGDRMN | NLGANLQKQN | WDLNTLPKFE | KSFYKEDPVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AARSEEDVAK | FRAQHNIAVQ | GPNIPKPVET | FDEAGFPAYV | MTEVKAQGFP | APTPIQSQGW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PMALSGRDVV | GIAETGSGKT | LTYCLPAIVH | INAQPLLAPG | DGPIVLVLAP | TRELAVQIQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EITKFGKSSR | IRNTCVYGGV | PKGGQIRDLA | KGVEVCIATP | GRLIDMIESG | KTNLRRVTYL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VLDEADRMLD | MGFEPQIRKI | LGQIRPDRQT | CMWSATWPKE | VRALASDYLN | DFIQVNIGSL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ELSANHRITQ | IVEVVSEFEK | RDKMTKHLEK | IMEDKDNKIL | IFTGTKRVAD | DITRFLRQDG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WPALSIHGDK | QQNERDWVLN | EFKTGKSPIM | VATDVASRGI | DVRNITHVFN | YDYPNNSEDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IHRIGRTGRA | GQKGTAITLF | TTDNQKQARD | LVNVLTEAKQ | VIDPRLAEMT | RFGGGGGGRG |
| 550 | 560 | 570 | |||
| YGGRGYGGGR | GRGGGGNFSS | SNAAPLGGGR | RW |