Q503V9
Gene name |
endoub (zgc:110053) |
Protein name |
Uridylate-specific endoribonuclease B |
Names |
Protein endoU-B |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:553584 |
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 Q503V9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q503V9-F1 | Predicted | AlphaFoldDB |
No variants for Q503V9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q503V9 | |||||
No associated diseases with Q503V9
1 regional properties for Q503V9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | EndoU ribonuclease, C-terminal | 4 - 278 | IPR018998 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| endoribonuclease activity | Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks. |
| lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
| metal ion binding | Binding to a metal ion. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTEGDRELSA | LIQELWDNDT | NRLRPGIDYR | ISLQGKAGDL | AGVPDDSDGA | GMPLFSFVDE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NIFKKETFLA | FISLLDNYES | DTGEPEIVTP | EEEMENHRFL | DSVIKTPTMK | IAHKYLVEKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LSPEDTTGFK | QQLYKIWFEL | YARKGSSKPD | SSGFEHVFVG | ETRGGHTVIG | FHNWIQLYLQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKLGHIDYKG | YSVNANSPQP | DENKHMLALQ | FSWKNGIKPK | GSIFIGVSPE | FEFSLYTLCF |
| 250 | 260 | 270 | 280 | ||
| LMSPNERVKV | SFNLYDVEIV | CHHYNQKHIG | TTYPVPVKYL | NV |