Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0SM46 (PNP_BORAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BAPKO_0858
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length722 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 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 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: InterPro

   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: UniProtKB-KW

polyribonucleotide nucleotidyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Polyribonucleotide nucleotidyltransferase HAMAP MF_01595
PRO_0000329539

Regions

Domain553 – 61260KH
Domain622 – 71796S1 motif

Sequences

Sequence LengthMass (Da)Tools
Q0SM46 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 9BCAB9C88DC5E0FB

FASTA72280,376
        10         20         30         40         50         60 
MRKILKLKIG RDELVFETGF MAKQANGSVL ATYGGSSVLA TVCCSNNVRE DLDFVPLSVE 

        70         80         90        100        110        120 
YNEKYYAAGK IPGGFIKREG KPKDKEILVS RLIDRPMRPL FDKRFGREIQ VIPTTLATDQ 

       130        140        150        160        170        180 
LNPPDIVGMN AAFTAVFLSD IPFNGPIAAV RMVYLNGKFI VNPSFEEIHD SDLDIVVAGS 

       190        200        210        220        230        240 
LNGITMVEGG ANEVSEDILL SAIDSAHEYI KQICNAQKEF LDIVGEKEKL PLAFEEKIFE 

       250        260        270        280        290        300 
FKEELRDFIY ADLKEACFVK GKLNRDKAIT LLRNKSYEHF SSLEKLDDSN ESLFYKAFDD 

       310        320        330        340        350        360 
FEKEIVRNSI LNDKIRTDGR TPNEIRDILA EVDILSRTHG SSLFTRGETQ ALAVTTLGTS 

       370        380        390        400        410        420 
IDEQIMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE IGHGHLAQRA LESMIPGKND 

       430        440        450        460        470        480 
FPYTIRVVSE ILESNGSSSM ATVCAGSMSL MSAGVPVKRQ VAGIAMGLIS EGDKYVVLSD 

       490        500        510        520        530        540 
ILGEEDHLGD MDFKVAGTEN GITGFQMDIK IENVTKQLMR DALEQARVGR IHILSIMNSV 

       550        560        570        580        590        600 
ISNSRVGISK YAPKIIQLQI DIDKISLVIG STGKTVKAIT DEFEVKVQIE QNGKIILFGD 

       610        620        630        640        650        660 
DDFKMQKAKE KIESIVREPK VGEIYEGTVK KINSFGAFIE LTPTKEGFLS TRLKSRDSKY 

       670        680        690        700        710        720 
GSGRFGHGNR YSRFGSGGDN IRGNAGLVRP PKLEEGQRIK VRIVDIDKFG KIDLEIVRDK 


DY

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed: 16914037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000395 Genomic DNA. Translation: ABH02082.1.
RefSeqYP_710258.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SM46.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0SM46.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000004330; EBBORP00000003948; EBBORG00000004330.
GeneID4227019.
GenomeReviewsGene locus BAPKO_0858 in contig CP000395_GR.
KEGGbaf:BAPKO_0858.
NMPDRfig|390236.5.peg.860.
PATRIC37189963. VBIBorAfz3878_0862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1185.
GeneTreeEBGT00050000007115.
HOGENOMHBG382411.
OMAYGETVVL.
ProtClustDBPRK11824.

Enzyme and pathway databases

BioCycBAFZ390236:BAPKO_0858-MONOMER.

Family and domain databases

HAMAPMF_01595. PNPase.
[Tree]
InterProIPR001247. 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]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.
KOK00962.
PANTHERPTHR11252. PNPase. 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.
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_BORAP
AccessionPrimary (citable) accession number: Q0SM46
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 42 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents