B1WBB4
Gene name |
endou-b |
Protein name |
Poly(U)-specific endoribonuclease-B |
Names |
Protein endoU-B, Uridylate-specific endoribonuclease-B, XendoU-B |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:100189581 |
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 B1WBB4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1WBB4-F1 | Predicted | AlphaFoldDB |
No variants for B1WBB4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1WBB4 | |||||
No associated diseases with B1WBB4
5 regional properties for B1WBB4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | RNA recognition motif domain | 66 - 145 | IPR000504-1 |
| domain | RNA recognition motif domain | 153 - 233 | IPR000504-2 |
| domain | RNA recognition motif domain | 306 - 384 | IPR000504-3 |
| domain | HuB, RNA recognition motif 3 | 303 - 388 | IPR034914 |
| domain | HuB, RNA recognition motif 2 | 148 - 231 | IPR034999 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
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 |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEANRGQVNH | ELSKLFNELW | DADVNRMKAG | KDYRISLQGK | AGYVPARSNQ | AKDSASYPLF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QFVDEEKLKS | KKTFATFISL | LDNYEMDTGV | AEVVTPEEIA | ENNNFLDAIL | ETKVMKMAHD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YLVRKNQAKP | SQNDFKVQLY | SIWFQLYSRA | PGSRPDSCGF | EHVFVGESKR | GKEMMGLHNW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VQFYLQEKRK | NIDYKGYVAR | QNKSRPDEDD | QVLNLQFSWK | EMVKPVGSSF | IGVSPEFEFA |
| 250 | 260 | 270 | 280 | 290 | |
| LYTIVFLASQ | AKMSREVIRL | EEYELQIVVN | RHGRYIGTAY | PALLSTNNPD | LY |