Q18253
Gene name |
dpf-2 (C27C12.7) |
Protein name |
Dipeptidyl peptidase family member 2 |
Names |
|
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_C27C12.7 |
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 Q18253
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q18253-F1 | Predicted | AlphaFoldDB |
No variants for Q18253
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q18253 | |||||
No associated diseases with Q18253
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. |
| dipeptidyl-peptidase activity | Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain. |
| serine-type peptidase activity | Catalysis of the hydrolysis of 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. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MENDNYDVEE | QGCSVFNGKH | GYFARSCCVV | FILIICVIFV | FSVIFTFMQN | PINLNSDNGF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NQTSGNTSSL | EATTLKPKFS | SLMTTTRRFT | FEQLFSGKQF | LVDYYDYIWL | PDGSFVQMND |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DFTIRKQMKK | IPLGSSVAEP | FFNNGEYVKA | LSSNMKYAYG | SKKVNELWRH | SAEYLYHIVK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| INNKTVSTEQ | WHVGPEENSL | IQAFYWNPNA | SSNDFVYVHN | YNLYYQKDPE | KPDGAIQLTV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GGSTFNRFGL | ANWLYEEEIL | EASSAVWWSP | SGRYVSYLRF | DDREVNRIFL | PKYTDDDSYV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EYFELPYPKA | GVQNNTLVTQ | YIWDSENHKI | VETAPPNELS | AANGDYYVLT | NKWITMPRNG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SDLGEERLVT | VWANRDQNHV | YFSLCNEQDC | VMALSFQFSI | DNRQLWVSPK | DVRGVFPTET |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GFLTVLPHKH | DDGNIYNHVA | HVELDGTGTG | KITKWIGENF | DVILVLGYSS | KIDALTFSAY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GDGVGEFSTY | IVREAMYSNK | KTTLQKVTDQ | FEDCKTLGSQ | SADPTGQRIV | VQCEKPFDNT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RLYLVDVVDT | TKKIMLEGGT | KAVIPFDVPN | MKFGKLKLPS | GIDGHYMMLT | PANLLDGAKI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PLLLDIYGGP | DSKQVFQKTP | TAHAIQIVSQ | YDIAYARIDV | RGTGGRGWDV | KEAVYRKLGD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AEVVDTLDMI | RAFINTFGFI | DEDRIAVMGW | SYGGFLTSKI | AIKDQGELVK | CAISIAPVTD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| FKYYDSAYTE | RYLGQPAENL | QGYINTNVIP | HARNVTNVKY | LLAHGERDDN | VHYQNSARWS |
| 790 | 800 | 810 | 820 | ||
| EALQQNGIHF | TQLVYANEAH | SLSHKLFHLY | GEVQRFLMND | CFKSNLDLL |