Q2KWI6 (PNP_BORA1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 40.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Polyribonucleotide nucleotidyltransferase EC=2.7.7.8 Alternative name(s): Polynucleotide phosphorylase Short name=PNPase | ||||
| Gene names |
| ||||
| Organism | Bordetella avium (strain 197N) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360910 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 718 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity. HAMAP MF_01595 |
| Catalytic activity | RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. HAMAP MF_01595 |
| Subunit structure | Homotrimer. Organized into a structure (processome or RNA degradosome) containing a number of RNA-processing enzymes By similarity. |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01595. |
| Sequence similarities | Belongs to the polyribonucleotide nucleotidyltransferase family. Contains 1 KH domain. Contains 1 S1 motif domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | RNA-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | RNA processing Inferred from electronic annotation. Source: InterPro mRNA catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3'-5'-exoribonuclease activity Inferred from electronic annotation. Source: InterPro RNA bindingInferred from electronic annotation. Source: UniProtKB-KW polyribonucleotide nucleotidyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 718 | 718 | Polyribonucleotide nucleotidyltransferase HAMAP MF_01595 | PRO_0000329535 | |||||
Regions | |||||||||
| Domain | 558 – 617 | 60 | KH | ||||||
| Domain | 627 – 695 | 69 | S1 motif | ||||||
Sequences
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References
| [1] | "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 197N. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM167904 Genomic DNA. Translation: CAJ50278.1. |
| RefSeq | YP_787166.1. NC_010645.1. |
3D structure databases | |
| ProteinModelPortal | Q2KWI6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2KWI6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6266139. |
| GenomeReviews | Gene locus BAV2667 in contig AM167904_GR. |
| KEGG | bav:BAV2667. |
| NMPDR | fig|521.1.peg.291. |
| PATRIC | 21131611. VBIBorAvi43433_2697. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG382411. |
| OMA | YGETVVL. |
| ProtClustDB | PRK11824. |
Enzyme and pathway databases | |
| BioCyc | ABAU360910:BAV2667-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01595. PNPase. [Tree] |
| InterPro | IPR001247. ExoRNase_PH_dom1. IPR015847. ExoRNase_PH_dom2. IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR012162. PNPase. IPR015848. PNPase_PH_RNA-bd_bac/org-type. IPR003029. Rbsml_prot_S1_RNA-bd_dom. IPR020568. Ribosomal_S5_D2-typ_fold. IPR022967. RNA-binding_domain_S1. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit. |
| KO | K00962. |
| PANTHER | PTHR11252. PNPase. 1 hit. |
| Pfam | PF00013. KH_1. 1 hit. PF03726. PNPase. 1 hit. PF01138. RNase_PH. 2 hits. PF03725. RNase_PH_C. 2 hits. PF00575. S1. 1 hit. [Graphical view] |
| PIRSF | PIRSF005499. PNPase. 1 hit. |
| SMART | SM00322. KH. 1 hit. SM00316. S1. 1 hit. [Graphical view] |
| SUPFAM | SSF46915. 3_ExoRNase. 1 hit. SSF55666. 3_ExoRNase. 2 hits. SSF50249. Nucleic_acid_OB. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits. |
| TIGRFAMs | TIGR03591. Polynuc_phos. 1 hit. |
| PROSITE | PS50084. KH_TYPE_1. 1 hit. PS50126. S1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PNP_BORA1 | ||||||||
| Accession | Primary (citable) accession number: Q2KWI6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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