P96614
Gene name |
cshA |
Protein name |
DEAD-box ATP-dependent RNA helicase CshA |
Names |
|
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU04580 |
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 P96614
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P96614-F1 | Predicted | AlphaFoldDB |
No variants for P96614
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P96614 | |||||
No associated diseases with P96614
5 regional properties for P96614
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 150 - 158 | IPR000629 |
| domain | Helicase, C-terminal | 215 - 375 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 27 - 192 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 22 - 219 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 3 - 31 | 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 |
|---|---|
| bacterial nucleoid | The region of a bacterial cell to which the DNA is confined. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
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. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| RNA helicase activity | Unwinding of an RNA helix, driven by ATP hydrolysis. |
| RNA strand annealing activity | An activity that facilitates the formation of a complementary double-stranded RNA molecule. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| response to cold | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. |
| ribosomal large subunit assembly | The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit. |
| RNA catabolic process | The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. |
| RNA secondary structure unwinding | The process in which a secondary structure of RNA are broken or 'melted'. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTITFQDFNL | SSDLMKAINR | MGFEEATPIQ | AQTIPLGLSN | KDVIGQAQTG | TGKTAAFGIP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LVEKINPESP | NIQAIVIAPT | RELAIQVSEE | LYKIGQDKRA | KVLPIYGGQD | IGRQIRALKK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NPNIIVGTPG | RLLDHINRRT | IRLNNVNTVV | MDEADEMLNM | GFIDDIESIL | SNVPSEHQTL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LFSATMPAPI | KRIAERFMTE | PEHVKVKAKE | MTVSNIQQFY | LEVQERKKFD | TLTRLLDIQS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PELAIVFGRT | KRRVDELAEA | LNLRGYAAEG | IHGDLTQAKR | MVALRKFKEG | AIEVLVATDV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AARGLDISGV | THVYNFDVPQ | DPESYVHRIG | RTGRAGKTGM | AMTFITPREK | SMLRAIEQTT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KRKMDRMKEP | TLDEALEGQQ | QVTVERLRTT | ISENNLNFYM | TAAAELLEDH | DAVTVVAAAI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KMATKEPDDT | PVRLTDEAPM | VSKRYKNQRS | SKRRDGQGGG | YRGGKGKSNN | RSSYDKKRSN |
| 490 | |||||
| DRRSSGDRRQ | KKSY |