P40084
Gene name |
RTR1 (YER139C) |
Protein name |
RNA polymerase II subunit B1 CTD phosphatase RTR1 |
Names |
RNA polymerase II-associated protein 2 homolog RTR1, Regulator of transcription 1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YER139C |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
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 P40084
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5C2Y | X-ray | 260 A | A/B | 1-178 | PDB |
| AF-P40084-F1 | Predicted | AlphaFoldDB |
3 variants for P40084
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s05-451221 | 6 | D>E | No | SGRP | |
| s05-451010 | 77 | L>V | No | SGRP | |
| s05-450568 | 224 | R>K | No | SGRP |
No associated diseases with P40084
1 regional properties for P40084
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Rtr1/RPAP2 domain | 50 - 136 | IPR007308 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| myosin phosphatase activity | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. |
| RNA polymerase core enzyme binding | Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme. |
| RNA polymerase II CTD heptapeptide repeat phosphatase activity | Catalysis of the reaction: phospho-(DNA-directed RNA polymerase II) + H2O = (DNA-directed RNA polymerase II) + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dephosphorylation of RNA polymerase II C-terminal domain | The process of removing a phosphate group from an amino acid residue in the C-terminal domain of RNA polymerase II. Some dephosphorylation occurs during transcription while some may occur after the enzyme is released from the template in order to prepare it for the beginning of the transcription cycle again. RNA polymerase II with little or no phosphorylation is referred to as the hypophosphorylated or II(A) form. |
| transcription by RNA polymerase II | The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATIEDIKET | ALIPFQKHRQ | LSMHEAEVIT | LEIIGLLCDS | ECKDEKTLKY | LGRFLTPDMY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QDLVDERNLN | KRCGYPLCGK | SPERIRDPFS | MNDTTKKFLL | ENNPYAYLSH | YCSKFHFRCS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QFYQVQLSDE | ALFARTGVHL | FEDPEQDKHD | IDFKVTLFEE | LLREKASEED | IKSLISGLKK |
| 190 | 200 | 210 | 220 | ||
| LGLNPDSGTT | EKDDTELEDD | LSKWLAQIKI | VENDNPSILG | DFTRED |