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 Q5XUW8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5XUW8-F1 | Predicted | AlphaFoldDB |
No variants for Q5XUW8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5XUW8 | |||||
No associated diseases with Q5XUW8
5 regional properties for Q5XUW8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M12B, ADAM/reprolysin | 198 - 393 | IPR001590 |
| domain | Disintegrin domain | 395 - 476 | IPR001762 |
| domain | Peptidase M12B, propeptide | 47 - 152 | IPR002870 |
| conserved_site | Disintegrin, conserved site | 432 - 451 | IPR018358 |
| domain | Reprolysin domain, adamalysin-type | 198 - 391 | IPR034027 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| peptidase activator activity | Binds to and increases the activity of a peptidase, any enzyme that catalyzes the hydrolysis peptide bonds. |
| toxin activity | Interacting selectively with one or more biological molecules in another (target) organism, initiating pathogenesis (leading to an abnormal, generally detrimental state) in the target organism. The activity should refer to an evolved function of the active gene product, i.e. one that was selected for. Examples include the activity of botulinum toxin, and snake venom. |
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 |
| MIQVLLVTIC | LAAFPYQGSS | IILESGNVND | YEVVYARKVT | ELPKGAVQQK | YEDAMQYEFK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VNGEPVVLHL | EKNKGLFSED | YSETHYSPDG | RQIITYPPFE | DHCYYHGRIE | NDADSTASIS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ACNGLKGHFK | LQGETYLIEP | LKLPDSEAHA | VYKYENVEKE | DEAPKMCGVT | ETNWESYEPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKASQSNLTP | EQQKFSPRYI | ELAVVADHGM | FTKYNSNLNT | IRTRVHEMVN | TLNGFFRSVN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VDASLANLEV | WSKKDLIKVE | KDSSKTLTSF | GEWRERDLLP | RISHDHAQLL | TTIVFDQQTI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GLAYTAGMCD | PRQSVAVVMD | HSKKNLRVAV | TMAHELGHNL | GMDHDDTCTC | GAKSCIMAST |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ISKGLSFEFS | KCSQNQYQTY | LTDHNPQCIL | NKPLTTVSGN | ELLEAGEECD | CGAPENPCCD |
| 430 | 440 | 450 | 460 | 470 | |
| AATCKLRPRA | QCAEGLCCDQ | CRFKGAGKIC | RRARGDNPDD | RCTGQSADCP | RNRFHA |