O59196
Gene name |
frvX (PH1527) |
Protein name |
Tetrahedral aminopeptidase |
Names |
TET, TET aminopeptidase, Leucyl aminopeptidase, PhTET2 |
Species |
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
KEGG Pathway |
pho:PH1527 |
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
No variants for O59196
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O59196 | |||||
No associated diseases with O59196
No regional properties for O59196
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for O59196 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
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. |
| metal ion binding | Binding to a metal ion. |
| metallopeptidase activity | Catalysis of the hydrolysis of peptide bonds 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. |
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 |
| MEVRNMVDYE | LLKKVVEAPG | VSGYEFLGIR | DVVIEEIKDY | VDEVKVDKLG | NVIAHKKGEG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PKVMIAAHMD | QIGLMVTHIE | KNGFLRVAPI | GGVDPKTLIA | QRFKVWIDKG | KFIYGVGASV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PPHIQKPEDR | KKAPDWDQIF | IDIGAESKEE | AEDMGVKIGT | VITWDGRLER | LGKHRFVSIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FDDRIAVYTI | LEVAKQLKDA | KADVYFVATV | QEEVGLRGAR | TSAFGIEPDY | GFAIDVTIAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DIPGTPEHKQ | VTHLGKGTAI | KIMDRSVICH | PTIVRWLEEL | AKKHEIPYQL | EILLGGGTDA |
| 310 | 320 | 330 | 340 | 350 | |
| GAIHLTKAGV | PTGALSVPAR | YIHSNTEVVD | ERDVDATVEL | MTKALENIHE | LKI |