P83370
Gene name |
|
Protein name |
Venom prothrombin activator hopsarin-D |
Names |
vPA, Venom coagulation factor Xa-like protease |
Species |
Hoplocephalus stephensii (Stephens' banded snake) |
KEGG Pathway |
|
EC number |
3.4.21.6: Serine endopeptidases |
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 P83370
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P83370-F1 | Predicted | AlphaFoldDB |
No variants for P83370
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P83370 | |||||
No associated diseases with P83370
1 regional properties for P83370
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Transposase IS4-like domain | 119 - 385 | IPR002559 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.6 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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 |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| peptidase activator activity | Binds to and increases the activity of a peptidase, any enzyme that catalyzes the hydrolysis peptide bonds. |
| 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). |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| blood coagulation | The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. |
| envenomation resulting in positive regulation of blood coagulation in another organism | A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the resultant activation, maintenance or an increase in the frequency, rate or extent of blood coagulation in the bitten organism. |
| positive regulation of blood coagulation in another organism | Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot. |
| 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 |
| MAPQLLLCLI | LTFLWSVPEA | ESNVFLKSKV | ANRFLQRTKR | SNSLFEEIRP | GNIERECIEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KCSKEEAREV | FEDNEKTETF | WNVYVDGDQC | SSNPCHYHGT | CKDGIGSYTC | TCLPNYEGKN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CEKVLFKSCR | AFNGNCWHFC | KRVQSETQCS | CAESYRLGVD | GHSCVAEGDF | SCGRNIKARN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KREASLPDFV | QSQKATLLKK | SDNPSPDIRI | VNGMDSKLGE | CPWQAVLINE | KGEVFCGGTI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSPIHVLTAA | HCINQTKSVS | VIVGEIDISR | KETRRLLSVD | KIYVHTKFVP | PNYYYGHQNF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DRVAYDYDIA | IIRMKTPIQF | SENVVPACLP | TADFANEVLM | KQDSGIVSGF | GRIRFKEPTS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NTLKVITVPY | VDRHTCMLSS | DFRITQNMFC | AGYDTLPQDA | CEGDSGGPHI | TAYGDTHFIT |
| 430 | 440 | 450 | |||
| GIVSWGEGCA | RKGKYGVYTK | VSRFIPWIKK | IMSLK |