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Q6D9A1 (PNP_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyribonucleotide nucleotidyltransferase
EC=2.7.7.8
Alternative name(s):
Polynucleotide phosphorylase
Short name=PNPase
Gene names
Name:pnp
Ordered Locus Names:ECA0716
OrganismErwinia carotovora subsp. atroseptica (strain SCRI 1043 / ATCC BAA-672) (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium ›

Protein attributes

Sequence length706 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity. HAMAP-Rule MF_01595

Catalytic activity

RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. HAMAP-Rule 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.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandRNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processRNA processing

Inferred from electronic annotation. Source: InterPro

mRNA catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3'-5'-exoribonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: HAMAP

polyribonucleotide nucleotidyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 706706Polyribonucleotide nucleotidyltransferase HAMAP-Rule MF_01595
PRO_0000329637

Regions

Domain553 – 61260KH
Domain622 – 69069S1 motif

Sequences

Sequence LengthMass (Da)Tools
Q6D9A1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 01D440A633E7849C

FASTA70676,485
        10         20         30         40         50         60 
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGAKNA KPGQSFFPLT 

        70         80         90        100        110        120 
VNYQERTYAA GRFPGGFFRR EGRPSEGETL TSRLIDRPIR PLFPEGFLNE VQVIATVVSV 

       130        140        150        160        170        180 
NPQVSPDIVA MIGASAALSL SGIPFSGPIG VARVGYLNDQ YVLNPTTDEL KESRLDLVVA 

       190        200        210        220        230        240 
GTQGAVLMVE SEAELLSEDQ MLGAVVFGHE QQQIVIENIN SLVAEAGKPK WEWHAPAVNV 

       250        260        270        280        290        300 
SLEQRVQALS EARLGDAYRI TEKQERYAQV NVIKTDVVAA LQAEDETLNA GEIQEILGNI 

       310        320        330        340        350        360 
EKNVVRGRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTER 

       370        380        390        400        410        420 
DAQNIDELTG ERTDRFLLHY NFPPYCVGET GMVGSPKRRE IGHGRLAKRG VLAVMPKANE 

       430        440        450        460        470        480 
FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKSA VAGIAMGLVK EGDNFVVLSD 

       490        500        510        520        530        540 
ILGDEDHLGD MDFKVAGSRE GITALQMDIK IEGITREIMQ VALNQAKGAR LHILGVMEQA 

       550        560        570        580        590        600 
ISTPRGDISE FAPRIHTIKI STDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVRIAST 

       610        620        630        640        650        660 
DGEKAKHAIR RIEEITAEIE VGRVYQGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE 

       670        680        690        700 
KVTDYLQMGQ EVPVKVLEVD RQGRVRLSIK EANPQTQEAA APSSEE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX950851 Genomic DNA. Translation: CAG73631.1.
RefSeqYP_048830.1. NC_004547.2.

3D structure databases

HSSPHSSP built from PDB template 1SRO based on UniProtKB P05055.
ProteinModelPortalQ6D9A1.
SMRQ6D9A1. Positions 617-692.
ModBaseSearch...

Protein-protein interaction databases

STRING218491.ECA0716.

Proteomic databases

PRIDEQ6D9A1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG73631; CAG73631; ECA0716.
GeneID2883240.
KEGGeca:ECA0716.
PATRIC20476612. VBIPecAtr54885_0714.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1185.
HOGENOMHOG000218326.
KOK00962.
OMAYTMRVVS.
ProtClustDBPRK11824.

Enzyme and pathway databases

BioCycPATR218491:GJNB-738-MONOMER.

Family and domain databases

Gene3D1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
HAMAPMF_01595. PNPase.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR009019. KH_prok-type.
IPR012340. NA-bd_OB-fold.
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]
PANTHERPTHR11252. PTHR11252. 1 hit.
PfamPF00013. 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]
PIRSFPIRSF005499. PNPase. 1 hit.
SMARTSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF46915. 3_ExoRNase. 1 hit.
SSF55666. 3_ExoRNase. 2 hits.
SSF54814. KH_prok. 1 hit.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
TIGRFAMsTIGR03591. polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNP_ERWCT
AccessionPrimary (citable) accession number: Q6D9A1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 16, 2004
Last modified: May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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