P9WHF3
Gene name |
rho |
Protein name |
Transcription termination factor Rho |
Names |
ATP-dependent helicase Rho |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv1297 |
EC number |
|
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
2 structures for P9WHF3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 7OQH | EM | 332 A | A/B/C/D/E/F | 1-602 | PDB |
| AF-P9WHF3-F1 | Predicted | AlphaFoldDB |
No variants for P9WHF3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WHF3 | |||||
No associated diseases with P9WHF3
6 regional properties for P9WHF3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | 334 - 538 | IPR000194 |
| domain | AAA+ ATPase domain | 345 - 530 | IPR003593 |
| domain | Rho termination factor, N-terminal | 36 - 78 | IPR011112 |
| domain | Rho termination factor, RNA-binding domain | 223 - 303 | IPR011113 |
| domain | Cold shock domain | 227 - 288 | IPR011129 |
| domain | Transcription termination factor Rho, ATP binding domain | 332 - 579 | IPR041703 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| peptidoglycan-based cell wall | A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli. |
| 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-dependent activity, acting on RNA | Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of RNA, and it drives another reaction. |
| helicase activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix. |
| hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| termination of RNA polymerase I transcription | A transcription termination process that completes the production of a ribosomal RNA transcript. RNAP I termination requires binding of a terminator protein to specific sequences downstream of the transcription unit. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDTDLITAG | ESTDGKPSDA | AATDPPDLNA | DEPAGSLATM | VLPELRALAN | RAGVKGTSGM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKNELIAAIE | EIRRQANGAP | AVDRSAQEHD | KGDRPPSSEA | PATQGEQTPT | EQIDSQSQQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RPERRSATRE | AGPSGSGERA | GTAADDTDNR | QGGQQDAKTE | ERGTDAGGDQ | GGDQQASGGQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QARGDEDGEA | RQGRRGRRFR | DRRRRGERSG | DGAEAELRED | DVVQPVAGIL | DVLDNYAFVR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TSGYLPGPHD | VYVSMNMVRK | NGMRRGDAVT | GAVRVPKEGE | QPNQRQKFNP | LVRLDSINGG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVEDAKKRPE | FGKLTPLYPN | QRLRLETSTE | RLTTRVIDLI | MPIGKGQRAL | IVSPPKAGKT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TILQDIANAI | TRNNPECHLM | VVLVDERPEE | VTDMQRSVKG | EVIASTFDRP | PSDHTSVAEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AIERAKRLVE | QGKDVVVLLD | SITRLGRAYN | NASPASGRIL | SGGVDSTALY | PPKRFLGAAR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NIEEGGSLTI | IATAMVETGS | TGDTVIFEEF | KGTGNAELKL | DRKIAERRVF | PAVDVNPSGT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RKDELLLSPD | EFAIVHKLRR | VLSGLDSHQA | IDLLMSQLRK | TKNNYEFLVQ | VSKTTPGSMD |
| SD |