P53052
Gene name |
cpdB |
Protein name |
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase |
Names |
|
Species |
Yersinia enterocolitica |
KEGG Pathway |
|
EC number |
3.1.3.6: Phosphoric monoester hydrolases |
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 P53052
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P53052-F1 | Predicted | AlphaFoldDB |
No variants for P53052
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P53052 | |||||
No associated diseases with P53052
5 regional properties for P53052
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Calcineurin-like phosphoesterase domain, ApaH type | 29 - 264 | IPR004843 |
| conserved_site | 5'-Nucleotidase, conserved site | 29 - 41 | IPR006146-1 |
| conserved_site | 5'-Nucleotidase, conserved site | 114 - 125 | IPR006146-2 |
| domain | 5'-Nucleotidase, C-terminal | 360 - 554 | IPR008334 |
| domain | CpdB, N-terminal metallophosphatase domain | 29 - 326 | IPR041827 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.6 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| periplasmic space | The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity | Catalysis of the reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate. |
| 3'-nucleotidase activity | Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| metal ion binding | Binding to a metal ion. |
| nucleotide binding | Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| nucleotide catabolic process | The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFKRPLTLSL | LASLIALTTS | TAQAATVDLR | VLETTDLHSN | MMDFDYYKDK | PTEKFGLVRT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ASLIEAARQQ | ATNSVLVDNG | DLIQGSPLGD | YMAAKGLKAG | EIHPVYKAMN | TLDYAVGNIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NHEFNYGLDY | LKKSLAGAKF | PYVNANVIDV | KTGKPLFQPY | LIVDTPVKDR | DGKNHNLRIG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YIGFGPPQVM | IWDKANLTGK | VTVDDITETA | KKWVPEMRKQ | GANLVVAIPH | SGLSSDPYKT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MAENSVYYLS | QVPGIDAIMF | GHAHAVFPSK | DFATIKGADI | AQGTLNGIPA | VMPGQWGDHL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GVVDFVLNND | QGQWQVTQAK | AEARPIFDKA | TQKSLAAENA | NLMKVLAADH | QGTRDFVSQP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IGTASDNMYS | YLSLIQDDPT | VQIVNNAQRA | YTEHFIQGDP | DLADLPVLSA | AAPFKAGGRK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NDPASFVEVE | KGELTFRNAA | DLYLYPNTLV | VVKASGADVK | QWLECSAAQF | NQIDVNSSKP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QSLINWDSFR | TYNFDVIDGV | NYEIDVSQPA | RYDGECALIN | DKAERIKNLT | FNGKPIDPQA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TFLIGTNNYR | AYSGKFAGTG | DSHIAFASPD | ENRAVLSAYI | SAETKKHGQV | TPQADNNWRL |
| 610 | 620 | 630 | 640 | 650 | |
| ATLNSQQPLD | IRFETSPSTK | AAEFIKQKAQ | YPMKAMGTDE | IGFAVFKIDL | QK |