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Q5HTK8 (PNP_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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

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:CJE1390
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in mRNA degradation. Catalyzes the phosphorolysis of 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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01595

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01595.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719Polyribonucleotide nucleotidyltransferase HAMAP-Rule MF_01595
PRO_0000329572

Regions

Domain573 – 63361KH
Domain658 – 71962S1 motif

Sites

Metal binding5071Magnesium By similarity
Metal binding5131Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HTK8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: E9EA95891AAE6FEB

FASTA71979,018
        10         20         30         40         50         60 
MQYSIEINKN TEIFNIDKVA KQAAGAVLMR QGKSVVLATV AREEKQVEED FLPLTVQYIE 

        70         80         90        100        110        120 
KAYAAGKIPG GYVKRETKPS DAETLTARII DRSLRPLFPK GYAYPTQIVV MVLSADPKVD 

       130        140        150        160        170        180 
LQVMSLNAAS VALYLSDIPM KAPVCGVRIG KIDGNFILNP NNEELQNSTL DLYVAGVKDE 

       190        200        210        220        230        240 
LLMIEMRALP DQKENEIFIE APYADVLTQT TSQNMNELSE DEILEALNLA QKAILNGSNA 

       250        260        270        280        290        300 
YEEAFSKHKK NSQIELKNEI EYPEILAFIE NNFQKQIKEA INQMAKSERA SELNKIAKEI 

       310        320        330        340        350        360 
SNLEIAKEWS EESVLNTLAK VKRKLIRGQI LNEGKRADGR SLNEVRPISI ETNILPNAHG 

       370        380        390        400        410        420 
SCLFTRGQTQ ALVVATLGGE NDAQMIDLLT EKNPISERFM VNYNFPGFSV GEASPIKAPG 

       430        440        450        460        470        480 
RRELGHGNLA KRALYPSVDE NYPYVIRLVS EILESNGSSS MATVCGGSLA LKAAGVPSLK 

       490        500        510        520        530        540 
LVAGVAMGLI FEDNKYAVLT DIMGLEDHDG DMDFKVAGSK DGVTALQMDI KLGGIDQETL 

       550        560        570        580        590        600 
KQALYQAKEG RIHILNIMEE AAKEIIVNEE VLPKLELFSV DPSKIVDIIG QAGKTIKEIV 

       610        620        630        640        650        660 
EKFGVSIDLD REKGEVKIAG SQNEQIKAAK DYIINITSSQ KGTKKGSKDK DISGFELGQE 

       670        680        690        700        710 
FQGIVKKIAP FGAFVELKNG VDGLLHSSKS KHLNLSENQS LKVKISEIKN GKISVDLCE 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35710.1.
RefSeqYP_179377.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HTK8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35710; AAW35710; CJE1390.
GeneID3231896.
KEGGcjr:CJE1390.
PATRIC20044580. VBICamJej134361_1407.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1185.
HOGENOMHOG000218326.
KOK00962.
OMAHGNFKSN.
OrthoDBEOG6WT8CC.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1417-MONOMER.

Family and domain databases

Gene3D1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
HAMAPMF_01595. PNPase.
InterProIPR001247. 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.
[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]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNP_CAMJR
AccessionPrimary (citable) accession number: Q5HTK8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 64 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