P57322
Gene name |
degP (BU228) |
Protein name |
Probable serine protease do-like |
Names |
|
Species |
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) |
KEGG Pathway |
buc:BU228 |
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
1 structures for P57322
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P57322-F1 | Predicted | AlphaFoldDB |
No variants for P57322
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P57322 | |||||
No associated diseases with P57322
3 regional properties for P57322
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PDZ domain | 282 - 373 | IPR001478-1 |
| domain | PDZ domain | 395 - 470 | IPR001478-2 |
| domain | Peptidase M50 | 283 - 399 | IPR008915 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 |
| MKKSAIILSK | IILILTLLLS | FGMSWNNVFS | NTKNSIVSRE | ISPSLAPMLE | KVMPSVISIN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IEGSAITRTS | RLPHQFQPFF | GDNSPFCQGN | SPFRHSPFCH | INPDSDDKKE | KFRALGSGVI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| INADKGYAVT | NNHVVENANK | IQVQLSDGRR | YEARVIGKDS | RSDIALIQLK | NANNLSEIKI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ADSDNLRVGD | YTVAIGNPYG | LGETVTSGII | SALGRSGLNI | EHYENFIQTD | AAINRGNSGG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALVNLKGELI | GINTAILAPD | GGNIGIGFAI | PCNMVKNLTA | QMVQFGQVRR | GELGIMGMEL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NSDLAQIMKI | NSQKGAFVSR | VLPNSSAFEA | GIKAGDIIIS | LNRKPISSFS | SLRAEIGSLP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VATKMELGVF | REGRIKNITV | ELKHSVKHNL | NSENDYIGIE | GVDLSDYIFN | EQKVIKVDNV |
| 430 | 440 | 450 | 460 | 470 | |
| KPHTPASKIG | FKKDDIILNV | NQKLISNVDE | LKKFLHSKPK | ILVFNIKRGN | DTIYLVSE |