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
0 structures for P11622
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P11622
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P11622 | |||||
No associated diseases with P11622
1 regional properties for P11622
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase S39B, luteovirus | 207 - 407 | IPR000382 |
1 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| 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). |
| serine-type exopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or 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). |
2 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. |
| viral process | A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNRFTAYAAL | FFIFSLCSTA | KEAGFQHPAF | NFRGTSTMSA | LSGDYSAAPT | PLYKSWALPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLNLTTQPPP | LLTDRSYYEL | VQALISKMRL | DCQTVGDMTW | RHLSEMLFAS | WNSVKEVSLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AASVTLWAII | SIWFGLYWTL | ARLITLFLWT | FSIEALCLIL | LGCITSLIYK | GALSLSEHLP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VFLFMSPLKI | IWRAAFSKRN | YKNEKAVEGY | KGFSVPQKPP | KSAVIELQHE | NGSHLGYANC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IRLYSGENAL | VTAEHCLEGA | FATSLKTGNR | IPMSTFFPIF | KSARNDISIL | VGPPNWEGLL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVKGAHFITA | DKIGKGPASF | YTLEKGEWMC | HSATIDGAHH | QFVSVLCNTG | PGYSGTGFWS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SKNLLGVLKG | FPLEEECNYN | VMSVIPSIPG | ITSPNYVFES | TAVKGRVFSD | ETVKELEREA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SEAVKKLARF | KSLTGKNWAN | DYDSDEDYGL | EKEAATNAPA | EKTAQTNSAE | KTAPSTSAEK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TAPTNKPLNG | RAAPPAKTNG | NSDIPDAAIS | APPMDKMVEQ | IITAMVGRIN | LSEIEEKIVS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RVSQKALQKP | KQNKRGRRGG | KNKQNNLPPT | STQSISGAPK | KKAVPQASGS | AGISPATTTP |
| 610 | 620 | 630 | |||
| APKEKPSGGK | NSAKFIPSWR | IKQQDSAGQK | PDLKLNSKA |