Q0V1R1
Gene name |
CPYA (SNOG_02053) |
Protein name |
Carboxypeptidase Y homolog A |
Names |
|
Species |
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
KEGG Pathway |
pno:SNOG_02053 |
EC number |
3.4.16.5: Serine-type carboxypeptidases |
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 Q0V1R1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0V1R1-F1 | Predicted | AlphaFoldDB |
No variants for Q0V1R1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0V1R1 | |||||
No associated diseases with Q0V1R1
No regional properties for Q0V1R1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q0V1R1 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.16.5 | Serine-type carboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type carboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from the C-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRVAASALLA | GAASAAVAPQ | QQILKFPSSF | SELKEDLWSK | PLHNLEESLK | SLTGEAKATW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DEVATMYPES | FDKAAFFSTP | KPHTRKHDSE | WDHIVKGADV | QSVWVENAQG | EKEREIDGKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EQFDLRVKKV | DPSVLGVDKV | KQYSGYLDDN | EEDKHLFYWF | FESRNDPKND | PVVLWLNGGP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GCSSLMGLFM | ELGPASVMKD | GKLKHNDYSW | NANASVIFLD | QPVNVGYSYS | SGSVSNTVAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GKDIYALLTL | FFKQFPEYSK | QPFHISGESY | AGHYIPVFAS | EILSHKKRNI | NLQSVLIGNG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTDGLTQYEY | YRPMACGEGG | WPAVLDESSC | QAMDNAYPRC | ASLIENCYKS | ESVWSCVPAS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IYCNNAMIGP | YQRTGQNVYD | VRRPCGDNQL | CYDEIDYISA | FLNKKEVMKA | VGAEVSSYDS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CNFDINRNFL | LQGDWMKPYH | RVVPGLLEEI | PVLVYAGDAD | YICNWLGNKA | WTEALEWKGH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EEYKKAEMKD | FKIDGDGKKV | GEVKSSGNFT | FMKIHAGGHM | VPFDQPEASL | EMVNRWLSGE |
| FWE |