Q75F95
Gene name |
DRS1 (AAL164C) |
Protein name |
ATP-dependent RNA helicase DRS1 |
Names |
|
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_AAL164C |
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 Q75F95
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q75F95-F1 | Predicted | AlphaFoldDB |
No variants for Q75F95
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q75F95 | |||||
No associated diseases with Q75F95
5 regional properties for Q75F95
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 371 - 379 | IPR000629 |
| domain | Helicase, C-terminal | 436 - 599 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 244 - 414 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 238 - 440 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 219 - 247 | 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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| preribosome, large subunit precursor | A preribosomal complex consisting of 27SA, 27SB, and/or 7S pre-rRNA, 5S rRNA, ribosomal proteins including late-associating large subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic large ribosomal subunit. |
4 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. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| RNA helicase activity | Unwinding of an RNA helix, driven by ATP hydrolysis. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| ribosomal large subunit assembly | The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit. |
| rRNA processing | Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGTKKVNQFK | DFVPTISDSE | EDIPDLDASD | DEYETAGKVK | SRKKTKKGRK | GGAVIADDED |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHADLNPEFH | FNDEGAEGTT | DFSGWDFVGD | GERAEQKDVD | LDGIIRRKGG | LVQLAGVEES |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EEEVEEAESA | AGASDDEELA | LDGFGMGAVA | QREAAGAADE | SDSESDKDSD | NSAEEAVELD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GVEFGDEQEE | AREEDTAEEM | AQFYAPSNEG | EEAKNVVHST | FNSLSLSRPV | LKGLAALGYT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KPSPIQGATI | PIALLGKDVI | AGAVTGSGKT | AAFMIPIIER | LLYKPAKIAS | TRVLVLTPTR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELAIQVADVG | KKLGKFVSGL | TFGLAVGGLN | LRQQEQALKL | RPDIVIATPG | RIIDHIRNSA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SFSVDSVEVL | VIDEADRMLE | DGFQDELNEI | MSLIPSKRQT | LLFSATMNSR | IKQLISLSLK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KPVRIMIDPP | KQAANKLTQE | FVRLRKREHL | KPALLYHLLR | KLDSTGQKRI | VVFVARKEVA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HRLRVILGLL | GMKAGELHGS | LTQEQRLQSV | NNFKSLDVPV | LVCTDLASRG | LDIPKIEVVI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NYDMPKTYEI | YLHRVGRTAR | AGREGKSVTL | VGESTQERSI | VKDAIKSVDG | SKGSGRACGR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VVDWKQVEEI | HKLVQAKEDV | IGEILEEEKQ | EKEILRAEME | IRKGENMLKF | KEEINARPRR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TWFQSESEKK | NSSILQALSK | NKKVTNSKKR | KREEAQQEVG | SRQYKKTQKD | RTTNQELAFR |
| 730 | |||||
| KQKKGGNKKK | KVRK |