※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polyribonucleotide nucleotidyltransferase
Protein Synonyms/Alias
 PNPase
Gene Name
 pnp
Gene Synonyms/Alias
 b3164, JW5851
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
652 KEGLVHISQIADKRV S HTP [1]
Reference
 [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation.
 Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M
 Mol. Cell Proteomics 2008, Feb;7(2):299-307. [PMID:17938405]
Functional Description From UniProt
 FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Also involved, along with RNase II, in tRNA processing
Sequence Annotation From UniProt
 
Key Word From UniProt
 3D-structure; Completeproteome; Cytoplasm; Directproteinsequencing; Magnesium; Metal-binding; Nucleotidyltransferase; Referenceproteome; RNA-binding; Stressresponse; Transferase
Protein Sequence
 MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA KPGQDFFPLT 60
 VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR PLFPEGFVNE VQVIATVVSV 120
 NPQVNPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KESKLDLVVA 180
 GTEAAVLMVE SEAQLLSEDQ MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE 240
 ALNARVAALA EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI 300
 EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTAR 360
 DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE IGHGRLAKRG VLAVMPDMDK 420
 FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD 480
 ILGDEDHLGD MDFKVAGSRD GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA 540
 INAPRGDISE FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT 600
 DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE 660
 KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA APEAPAAEQG E 711
  GO:0005829   C:cytosol IDA:UniProtKB
  GO:0016020   C:membrane IDA:UniProtKB
  GO:0000175   F:3'-5'-exoribonuclease activity IDA:EcoCyc
  GO:0035438   F:cyclic-di-GMP binding IDA:EcoCyc
  GO:0042802   F:identical protein binding IPI:IntAct
  GO:0000287   F:magnesium ion binding IEA:UniProtKB-HAMAP
  GO:0004654   F:polyribonucleotide nucleotidyltransferase activity IDA:EcoCyc
  GO:0003723   F:RNA binding IEA:UniProtKB-HAMAP
  GO:0006402   P:mRNA catabolic process IEA:UniProtKB-HAMAP
  GO:0006950   P:response to stress IEA:UniProtKB-KW
  GO:0090503   P:RNA phosphodiester bond hydrolysis, exonucleolytic IDA:GOC
  GO:0006396   P:RNA processing IEA:InterPro
  IPR001247   ExoRNase_PH_dom1.
  IPR015847   ExoRNase_PH_dom2.
  IPR004087   KH_dom.
  IPR004088   KH_dom_type_1.
  IPR012340   NA-bd_OB-fold.
  IPR012162   PNPase.
  IPR027408   PNPase/RNase_PH_dom.
  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.
  PF00013   KH_1.
  PF03726   PNPase.
  PF01138   RNase_PH.
  PF03725   RNase_PH_C.
  PF00575   S1.
  SM00322   KH.
  SM00316   S1.
  PS50084   KH_TYPE_1.
  PS50126   S1.