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O34275

- PNP_YEREN

UniProt

O34275 - PNP_YEREN

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Protein

Polyribonucleotide nucleotidyltransferase

Gene
pnp
Organism
Yersinia enterocolitica
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity.UniRule annotation

Catalytic activityi

RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi486 – 4861Magnesium By similarity
Metal bindingi492 – 4921Magnesium By similarity

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: InterPro
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB-HAMAP
  4. RNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. mRNA catabolic process Source: UniProtKB-HAMAP
  2. RNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyribonucleotide nucleotidyltransferase (EC:2.7.7.8)
Alternative name(s):
Polynucleotide phosphorylase
Short name:
PNPase
Gene namesi
Name:pnp
OrganismiYersinia enterocolitica
Taxonomic identifieri630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 706706Polyribonucleotide nucleotidyltransferaseUniRule annotationPRO_0000197918Add
BLAST

Proteomic databases

PRIDEiO34275.

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation By similarity.

Structurei

3D structure databases

ProteinModelPortaliO34275.
SMRiO34275. Positions 617-692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini553 – 61260KHAdd
BLAST
Domaini622 – 69069S1 motifAdd
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

Family and domain databases

Gene3Di1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
HAMAPiMF_01595. PNPase.
InterProiIPR001247. 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]
PANTHERiPTHR11252. PTHR11252. 1 hit.
PfamiPF00013. 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]
PIRSFiPIRSF005499. PNPase. 1 hit.
SMARTiSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34275-1 [UniParc]FASTAAdd to Basket

« Hide

MLTPIIRKFQ YGQHTVTIET GMMARQATAA VMVSMDDTAV FVTVVGQKKA    50
KPGQSFFPLT VNYQERTYAA GRIPGSFFRR EGRPSEGETL TSRLIDRPIR 100
PLFPDSFLNE VQVIATVVSV NPQINPDIVA LIGASAALSL SGIPFNGPIG 150
AARVGFINDQ YVLNPTTDEL KESRLDLVVA GTAGAVLMVE SEADILSEDQ 200
MLGAVVFGHE QQQVVIENIN ALVAEAGKPK WDWHAEPVNE ALHARVAELA 250
AARLGDAYRI TEKQERYTQV DAIKADVTEA LLAQDDTLDA AEIQDILGSV 300
EKDVVRSRVL RGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA 350
LVTATLGTAR DAQNIDELMG ERTDSFLLHY NFPPYSVGET GMVGSPKRRE 400
IGHGRLAKRG VLAVMPSPSE FPYTVRVVSE ITESNGSSSM ASVCGASLAL 450
MDAGVPIKAA VAGIAMGLVK EDENFVVLSD ILGDEDHLGD MDFKVAGSRD 500
GITALQMDIK IEGITREIMQ VALNQAKGAR LHILGVMEQA ISTPRGDISE 550
FAPRIYTMKI NPEKIKDVIG KGGSVIRALT DETGTTIDIE ADGTIKIAAT 600
DGDKAKHAIR RIEEITAEIE VNRIYAGKVT RIVDFGAFVA IGGGKEGLVH 650
ISQIADKRVD KVTDYLQMGQ EVPVKVIEVD RQGRIRLSMK EATTPDAEAP 700
APEAAE 706
Length:706
Mass (Da):76,284
Last modified:December 1, 2000 - v2
Checksum:i9CD82CD348C3AD4A
GO

Sequence cautioni

The sequence CAA71697.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti588 – 5881D → E in AAQ11418. 1 Publication
Sequence conflicti591 – 5911A → D in AAQ11418. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10692 Genomic DNA. Translation: CAA71697.1. Different initiation.
AF542976 Genomic DNA. Translation: AAQ11418.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10692 Genomic DNA. Translation: CAA71697.1 . Different initiation.
AF542976 Genomic DNA. Translation: AAQ11418.1 .

3D structure databases

ProteinModelPortali O34275.
SMRi O34275. Positions 617-692.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O34275.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
HAMAPi MF_01595. PNPase.
InterProi 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.
[Graphical view ]
PANTHERi PTHR11252. PTHR11252. 1 hit.
Pfami 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 ]
PIRSFi PIRSF005499. PNPase. 1 hit.
SMARTi SM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The psychrotrophic bacterium Yersinia enterocolitica requires expression of pnp, the gene for polynucleotide phosphorylase, for growth at low temperature (5 degrees C)."
    Goverde R.L.J., Huis in't Veld J.H.J., Kusters H.G., Mooi F.R.
    Mol. Microbiol. 28:555-569(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of cold shock inducible dead gene for RNA helicase in Yersinia enterocolitica."
    Anastasov N., Scherer S.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCTC 10460.

Entry informationi

Entry nameiPNP_YEREN
AccessioniPrimary (citable) accession number: O34275
Secondary accession number(s): Q718F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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