Q7SEF9
Gene name |
rrd-2 (NCU03269) |
Protein name |
Serine/threonine-protein phosphatase 2A activator 2 |
Names |
Peptidyl-prolyl cis-trans isomerase PTPA-2, PPIase PTPA-2, Rotamase PTPA-2, Phosphotyrosyl phosphatase activator 2 |
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU03269 |
EC number |
5.2.1.8: Cis-trans isomerases |
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 Q7SEF9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7SEF9-F1 | Predicted | AlphaFoldDB |
No variants for Q7SEF9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7SEF9 | |||||
No associated diseases with Q7SEF9
No regional properties for Q7SEF9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q7SEF9 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 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. |
| protein phosphatase type 2A complex | A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
| protein tyrosine phosphatase activator activity | Binds to and increases the activity of a phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a tyrosyl phenolic group of a protein. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| mitotic spindle organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDSSVTTGRS | GIGTGQGSPA | ASGQPISKAG | QAIPNLRDRI | PKLEPRRRKQ | EPSNPTPVPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TPALPPRPDP | STLVFQTPVR | RILLLKDHEL | FLASPSFNLI | LSFVFSLSES | VADTPISAIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DSDLSEPVKA | ILRILDETEA | LCKESPPDDQ | GGSRFGNKTF | RLFLDKVKQR | GHQWHAAFLG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GKLPDAAVTE | ASAYLNQSFG | NRTRIDYGSG | HELNFIMWLL | CLYQLSVLEQ | SDFKAVVLRV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FARYLEVMRL | IQMTYYLEPA | GSHGVWGLDD | YQFLPFLFGA | SQLLHHHFIT | PRAIHQELTL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EEFGHDFLYL | GQVAFVNSTK | TVKGLRWHSP | MLDDISSAKN | WEKIEGGMRR | MFVSEVLKKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PVMQHFLFGS | LIPAAEGMSE | QDPNALGSEE | NEEEGGEVEV | YDDSDGKRHV | HQPTGWGDCC |
| 430 | 440 | ||||
| GIKVPSSLAA | AEEMRKRGQV | ESLRRIPFD |