P0A4D8
Gene name |
cshA |
Protein name |
DEAD-box ATP-dependent RNA helicase CshA |
Names |
Exported protein 9 |
Species |
Streptococcus pneumoniae (strain ATCC BAA-255 / R6) |
KEGG Pathway |
spr:spr1440 |
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 P0A4D8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0A4D8-F1 | Predicted | AlphaFoldDB |
No variants for P0A4D8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0A4D8 | |||||
No associated diseases with P0A4D8
5 regional properties for P0A4D8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 148 - 156 | IPR000629 |
| domain | Helicase, C-terminal | 213 - 373 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 26 - 190 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 20 - 217 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 1 - 29 | 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 |
|---|---|
| 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. |
3 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. |
| 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 |
| MKFNELNLSA | DLLAEIEKAG | FVEASPIQEQ | TIPLALEGKD | VIGQAQTGTG | KTAAFGLPTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKIRTEEATI | QALVIAPTRE | LAVQSQEELF | RFGRSKGVKV | RSVYGGSSIE | KQIKALKSGA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HIVVGTPGRL | LDLIKRKALK | LQDIETLILD | EADEMLNMGF | LEDIEAIISR | VPENRQTLLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SATMPDAIKR | IGVQFMKAPE | HVKIAAKELT | TELVDQYYIR | VKEQEKFDTM | TRLMDVAQPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LAIVFGRTKR | RVDELTRGLK | IRGFRAEGIH | GDLDQNKRLR | VLRDFKNGNL | DVLVATDVAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RGLDISGVTH | VYNYDIPQDP | ESYVHRIGRT | GRAGKSGQSI | TFVAPNEMGY | LQIIENLTKK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RMKGLKPASV | EESFQSKKQV | ALKKIERDFA | DETIRANFEK | FGKDARKLAA | EFTPEELAMY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ILSLTVQDPD | SLPEVEIARE | KPLPFKPSGN | GFGGKAKGGR | GGRRGDDRRE | RDRRGNGRRD |
| 490 | 500 | 510 | 520 | ||
| EFKKGSRGND | RFDKEKRYRK | DNKKPRNTLS | EKQTGFVIRN | KGDK |