B7MAD3
Gene name |
cca |
Protein name |
Multifunctional CCA protein |
Names |
|
Species |
Escherichia coli O45:K1 (strain S88 / ExPEC) |
KEGG Pathway |
ecz:ECS88_3454 |
EC number |
2.7.7.72: Nucleotidyltransferases |
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 B7MAD3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7MAD3-F1 | Predicted | AlphaFoldDB |
No variants for B7MAD3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7MAD3 | |||||
No associated diseases with B7MAD3
4 regional properties for B7MAD3
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.72 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
9 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity | Catalysis of the reaction: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate. |
| CTP:3'-cytidine-tRNA cytidylyltransferase activity | Catalysis of the reaction: a tRNA with a 3' cytidine + CTP = a tRNA with a 3' CC end + diphosphate. |
| CTP:tRNA cytidylyltransferase activity | Catalysis of the reaction: a tRNA precursor + CTP = a tRNA with a 3' cytidine end + diphosphate. |
| cyclic-nucleotide phosphodiesterase activity | Catalysis of the reaction: a nucleoside cyclic phosphate + H2O = a nucleoside phosphate. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phosphatase activity | Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. |
| tRNA binding | Binding to a transfer RNA. |
| tRNA cytidylyltransferase activity | Catalysis of the reaction: CTP + tRNA(n) = diphosphate + tRNA(n+1). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| RNA repair | Any process that results in the repair of damaged RNA. |
| tRNA 3'-terminal CCA addition | Post-transcriptional addition of the terminal 3' CCA sequence to a tRNA which does not encode this sequence within the primary transcript. CCA addition proceeds by the sequential addition of CTP, CTP, and then ATP to the 3' end of the tRNA, yielding a diphosphate with each nucleotide addition. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIYLVGGAV | RDALLGLPVK | DRDWVVVGST | PQEMLDAGYQ | QVGRDFPVFL | HPQTHEEYAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ARTERKSGSG | YTGFTCYAAP | DVTLEDDLKR | RDLTINALAQ | DDNGEIIDPY | NGLGDLQNRL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRHVSPAFGE | DPLRVLRVAR | FAARYAHLCF | RIADETLALM | REMTHAGELE | HLTPERVWKE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TENALTTRNP | QVFFQVLRDC | GALRVLFPEI | DALFGVPAPA | RWHPEIDTGI | HTLMTLSMAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLSPQVDVRF | ATLCHDLGKG | LTPPELWPRH | HGHGPAGVKL | VEQLCQRLRV | PNEIRDLARL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VAEFHDLIHT | FPMLNPKTIV | KLFDSIDAWR | KPQRVEQLAL | TSEADVRGRT | GFESADYPQG |
| 370 | 380 | 390 | 400 | 410 | |
| RWLREAWEVA | QSVPTKAVVE | AGFKGVEIRE | ELTRRRIAAV | AGWKEQRCPK | PE |