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 Q2VF18
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2VF18-F1 | Predicted | AlphaFoldDB |
No variants for Q2VF18
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2VF18 | |||||
No associated diseases with Q2VF18
6 regional properties for Q2VF18
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ribonuclease III domain | 968 - 1131 | IPR000999-1 |
| domain | Ribonuclease III domain | 1153 - 1375 | IPR000999-2 |
| domain | Helicase, C-terminal | 412 - 582 | IPR001650 |
| domain | Dicer dimerisation domain | 603 - 704 | IPR005034 |
| domain | DEAD/DEAH box helicase domain | 65 - 228 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 59 - 257 | IPR014001 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| helicase activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix. |
| metal ion binding | Binding to a metal ion. |
| ribonuclease III activity | Catalysis of the endonucleolytic cleavage of RNA with 5'-phosphomonoesters and 3'-OH termini; makes two staggered cuts in both strands of dsRNA, leaving a 3' overhang of 2 nt. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| defense response to virus | Reactions triggered in response to the presence of a virus that act to protect the cell or organism. |
| gene silencing by RNA | A process in which an RNA molecule reduces expression of target genes. This can occur pre-transcriptionally by assembly of heterochromatin and prevention of transcription or co- or post-transcriptionally by targeting RNAs for degradation or by interfering with splicing or translation. This process starts once the inhibitory RNA molecule has been transcribed, and includes processing of the RNA such as cleavage, modifications, transport from the nucleus to the cytoplasm, loading onto the RISC complex, and the effect on transcription or translation. |
| regulation of defense response to virus | Any process that modulates the frequency, rate or extent of the antiviral response of a cell or organism. |
| RNA processing | Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAYYTDSSSS | ESEDFEDVIN | QVVAEEDITG | AAWYDGHLSE | EDSPGGKPRP | KEQLPKDIVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MDARAYQLEM | LEASLKENII | CAMDTGSGKT | HVAILRIKAE | LEEMPEGQVV | WFLTPTVSLC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQQYAVVKAQ | IPSVQTKIVT | GADKVDSWSS | TTWDGALLNV | KVIITTPQVL | LDALLHGFVN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ISSLALMVFD | EAHHCNKNHA | YSRVMKEFYW | ESKTKHEPVP | RILGLTASPV | VRSDISSLKR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LESTLDAVCR | SPTRHREELI | ANSQRPALFS | IIYNPKLQPY | AAGFSESLTK | LMAARNKLNI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LEDPYVVSLR | AEISDRSRRK | LEKAIKEKRT | YVQDTMKSFC | RRSMEMAKEL | GAWAADWFIS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EAIRLFLAGI | YRQGASSKSF | RDAEVIFLAR | VFQDANIEPP | PPLTTHSGLS | EKVQRIIEVL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LNYDKDARAI | CFVKERATTV | VLSHILTTHP | EVSSKFRIGT | MVGTSFVPGV | KRDFLDLPET |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GGSQCLEAFR | EGRKNMLVAT | SVLEEGIDVP | ACNLIICFDK | PNNLRAFIQR | RGRARMRQSH |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LYLFVEDEAE | ADWEALEAQM | KLQYEDEKRE | HERLEAIENS | EALDYPEELR | VESTGARLTI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NDAKSHLQHF | VSTLASRKFV | QTQPDYLIEK | VSQGYQPGDQ | PLLKATVLLP | VSVPQALRQV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TSSRTWVSEK | NACMDAAFQA | YKALYEAGLV | DDHLLPLRDR | LELELEVRPG | MREVRGLYNP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| WLSIAAACTQ | GDVPLCRRAL | KVSDGNNSEL | CEFELAIPVA | LPEMKPMVVW | WDHRAQLTLR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IDSDAVMADT | DVRHADQTTI | NQQDHTSVLL | SLAYGHRNMT | IRDDCILRLV | SKSGPLSMEQ |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LGQVEFAPGL | VTANGSSYLV | RDERDQSRHP | YYFESVLPSK | PPAESIRKVY | RGFDEDPTEA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TYLSVRKWPK | KTGFFHRPCS | PQHSPSTKPY | AYILPAETTT | VDRIPLVYAQ | MGLLMPSLVC |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| YTELYLVAAE | LSRKVLAPLR | ISNVSMLVEA | ICAKSARTPE | NYERIEFLGD | SILKTCITVN |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LAATKLHLPE | GILSLMKDRL | VSNARLCRAA | CDAELDQFLV | TQQLVTKGWQ | PPYMSDLAKQ |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| DQEPESKRIL | SPKTLADVVE | ALIGVSFVDG | GLPKALECIR | LFIPESQPRP | FSEVRDILFG |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| AAEPKGMKLP | ADLQLLEQLI | EYSFCEKALL | VEAVTHPSYN | VSGTVACYDR | LEFIGDAILD |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| YIIVEEVFAL | EPALENWQMH | LLRTALVNAD | ILGFLIMEWS | YKQMGFEVCR | ANEGDSDSKS |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| SGDSTSDKAS | PRLEQTEVPI | PLWSFMRQSS | AELTMEREIT | KARFEELRDP | ILEAMRSGTH |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| YPWALFARLH | AQKFYSDFFE | ALVGAIWVDA | GPGFDACRAF | VARSGVLPYL | KRLLRDQVHV |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| LHPKEELGRL | AGRERVEYVV | KETLKDDGDG | KEWACEVRVG | GRYVTDVTGC | LFKEESRVKA |
| 1450 | |||||
| ATQACEILKR | K |