P05055
Gene name |
pnp |
Protein name |
Polyribonucleotide nucleotidyltransferase |
Names |
Polynucleotide phosphorylase, PNPase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b3164 |
EC number |
2.7.7.8: 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
12 structures for P05055
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1SRO | NMR | - | A | 617-692 | PDB |
| 3CDI | X-ray | 260 A | A | 2-711 | PDB |
| 3CDJ | X-ray | 280 A | A | 2-547 | PDB |
| 3GCM | X-ray | 250 A | A/B/C | 1-549 | PDB |
| 3GLL | X-ray | 270 A | A | 1-549 | PDB |
| 3GME | X-ray | 240 A | A | 1-549 | PDB |
| 3H1C | X-ray | 357 A | A/B/C/G/I/K/M/O/R/T/V/X | 1-549 | PDB |
| 6QH2 | NMR | - | A | 545-711 | PDB |
| 7OGK | EM | 340 A | A/B/C | 1-711 | PDB |
| 7OGL | EM | 340 A | A/B/C | 1-711 | PDB |
| 7OGM | EM | 370 A | L/N/O | 1-711 | PDB |
| AF-P05055-F1 | Predicted | AlphaFoldDB |
No variants for P05055
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P05055 | |||||
No associated diseases with P05055
9 regional properties for P05055
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Exoribonuclease, phosphorolytic domain 1 | 16 - 144 | IPR001247-1 |
| domain | Exoribonuclease, phosphorolytic domain 1 | 324 - 456 | IPR001247-2 |
| domain | S1 domain | 619 - 690 | IPR003029 |
| domain | K Homology domain | 552 - 617 | IPR004087 |
| domain | K Homology domain, type 1 | 556 - 614 | IPR004088 |
| domain | Exoribonuclease, phosphorolytic domain 2 | 147 - 210 | IPR015847-1 |
| domain | Exoribonuclease, phosphorolytic domain 2 | 460 - 527 | IPR015847-2 |
| domain | Polyribonucleotide nucleotidyltransferase, RNA-binding domain | 242 - 320 | IPR015848 |
| domain | RNA-binding domain, S1 | 620 - 690 | IPR022967 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.8 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| bacterial degradosome | The degradosome is a protein complex playing a key role in mRNA degradation and RNA processing. It includes a RNA helicase, a 3'-5' phosphate-dependent PNPase and a RNase E bound-enolase. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3'-5'-exoribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of an RNA molecule. |
| cyclic-di-GMP binding | Binding to cyclic-di-GMP, cyclic dimeric guanosine monophosphate. |
| identical protein binding | Binding to an identical protein or proteins. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| polyribonucleotide nucleotidyltransferase activity | Catalysis of the reaction: RNA(n+1) + phosphate <=> RNA(n) + a nucleoside diphosphate. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA catabolic process | The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| RNA catabolic process | The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. |
| RNA processing | Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q8TCS8 | PNPT1 | Polyribonucleotide nucleotidyltransferase 1, mitochondrial | Homo sapiens (Human) | PR |
| Q8K1R3 | Pnpt1 | Polyribonucleotide nucleotidyltransferase 1, mitochondrial | Mus musculus (Mouse) | PR |
| Q6KAI0 | PNP2 | Polyribonucleotide nucleotidyltransferase 2, mitochondrial | Oryza sativa subsp japonica (Rice) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLNPIVRKFQ | YGQHTVTLET | GMMARQATAA | VMVSMDDTAV | FVTVVGQKKA | KPGQDFFPLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VNYQERTYAA | GRIPGSFFRR | EGRPSEGETL | IARLIDRPIR | PLFPEGFVNE | VQVIATVVSV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NPQVNPDIVA | MIGASAALSL | SGIPFNGPIG | AARVGYINDQ | YVLNPTQDEL | KESKLDLVVA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GTEAAVLMVE | SEAQLLSEDQ | MLGAVVFGHE | QQQVVIQNIN | ELVKEAGKPR | WDWQPEPVNE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALNARVAALA | EARLSDAYRI | TDKQERYAQV | DVIKSETIAT | LLAEDETLDE | NELGEILHAI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EKNVVRSRVL | AGEPRIDGRE | KDMIRGLDVR | TGVLPRTHGS | ALFTRGETQA | LVTATLGTAR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DAQVLDELMG | ERTDTFLFHY | NFPPYSVGET | GMVGSPKRRE | IGHGRLAKRG | VLAVMPDMDK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FPYTVRVVSE | ITESNGSSSM | ASVCGASLAL | MDAGVPIKAA | VAGIAMGLVK | EGDNYVVLSD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ILGDEDHLGD | MDFKVAGSRD | GISALQMDIK | IEGITKEIMQ | VALNQAKGAR | LHILGVMEQA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| INAPRGDISE | FAPRIHTIKI | NPDKIKDVIG | KGGSVIRALT | EETGTTIEIE | DDGTVKIAAT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DGEKAKHAIR | RIEEITAEIE | VGRVYTGKVT | RIVDFGAFVA | IGGGKEGLVH | ISQIADKRVE |
| 670 | 680 | 690 | 700 | 710 | |
| KVTDYLQMGQ | EVPVKVLEVD | RQGRIRLSIK | EATEQSQPAA | APEAPAAEQG | E |