Q8PTN8
Gene name |
MM_2675 |
Protein name |
Uncharacterized serpin-like protein MM_2675 |
Names |
|
Species |
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) |
KEGG Pathway |
mma:MM_2675 |
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 Q8PTN8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8PTN8-F1 | Predicted | AlphaFoldDB |
No variants for Q8PTN8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8PTN8 | |||||
No associated diseases with Q8PTN8
1 regional properties for Q8PTN8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Myc-type, basic helix-loop-helix (bHLH) domain | 129 - 193 | IPR011598 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type endopeptidase inhibitor activity | Binds to and stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSRIKIILLA | CMLALLFSGC | VENSAVFEKN | TATLKENTIN | ADSVRGYDIA | SANNAFAFDM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YSQLTQQVTG | DYENILFSPY | SISAAMAICY | EGAENTTKEQ | ISNVFYFPTN | KTVLKVRLER |
| 130 | 140 | 150 | 160 | 170 | 180 |
| INDRINSGSG | DYELQTANAL | WIQEGYPVKE | EYLFNVKKYY | DGEVANLDFV | RKPDDSRNTI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NEWVETRTSD | KIKDLVPKSM | ITPDTRIIIT | NAIYFNGKWA | YTFDKQLTEK | RAFYPANGEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ASVDMMYMYN | NFNYGENSKA | KIIELPYKGN | DLSMYIVLPK | DNNIKEFETE | FTINDYTELK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NEMDSTVNVD | ILIPKFKFET | KTELSDSFVE | MGVVDAFRQA | NFSGISNSPL | KVSEVIHQTF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IDVKEEGTEA | AAATGVGMTV | GMDFSWDSKQ | REFKADHPFM | FFIEDRRTNC | ILFMGKVEYP |
| EYKNDT |