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A4W401

- PNP_STRS2

UniProt

A4W401 - PNP_STRS2

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Protein
Polyribonucleotide nucleotidyltransferase
Gene
pnp, SSU98_1932
Organism
Streptococcus suis (strain 98HAH33)
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 bindingi489 – 4891Magnesium By similarity
Metal bindingi495 – 4951Magnesium By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciSSUI391296:GI2E-1988-MONOMER.

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
Ordered Locus Names:SSU98_1932
OrganismiStreptococcus suis (strain 98HAH33)
Taxonomic identifieri391296 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000244: Chromosome

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 – 739739Polyribonucleotide nucleotidyltransferaseUniRule annotation
PRO_0000329883Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi391296.SSU98_1932.

Structurei

3D structure databases

ProteinModelPortaliA4W401.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini556 – 61560KH
Add
BLAST
Domaini625 – 69369S1 motif
Add
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1185.
HOGENOMiHOG000218326.
KOiK00962.
OrthoDBiEOG6WT8CC.

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.

A4W401-1 [UniParc]FASTAAdd to Basket

« Hide

MSKQVFETVF AGKKLVVETG QVAKQANGAV VVRYGDSTVL TAAVMSKKMA    50
TGDFFPLQVN YEEKMYAAGK FPGGWMKREG RPSTDATLTA RLIDRPIRPM 100
FAEGFRNEVQ VINTVLSYDP DASAPMAAMF GSSLALAISD IPFNGPIAGV 150
QVGYVNGELI INPDQAQQEA SLLELTVAGN KDAINMVESG AKELSEEVML 200
EALLKGHAAI QELLDFQNQI VAAVGKEKAD VELLQVDPEL QAEIVAAYND 250
DLKKAVQVEE KLAREDATNA VRETVIATYE EKYAEHEEFD RIMRDVHEIL 300
ELMEHTEVRR LITEDKVRPD GRRVDEIRPL DAEVDFLPNV HGSGLFTRGQ 350
TQALSVLTLA PMGETQIIDG LDDEYKKRFL HHYNFPQYSV GSTGRYGAPG 400
RREIGHGALG ERALEQVLPS LEDFPYAIRL VAEVLESNGS SSQASITAGT 450
LALMAGGVPI KAPVAGIAMG LISDGTNYTV LTDIQGLEDH FGDMDFKVAG 500
TRDGITALQM DIKIDGITPQ ILEEALAQAK KARFEILDVI EATIPEVRPD 550
LAPTAPKIDT IKIDVDKIKI VIGKGGETID KIIAETGVKI DIDEDGLVAI 600
FSPDRAAIER TKEIIAGLVR EAKVDEVFQA KVVRLEKFGA FVNLFDKTDA 650
LVHVSEMAWT RVNKPEDLVE VGDVVDVKVI KIDDKGRIDA SMKALLPKPE 700
GYVEPEKRER SEKPRRHKEH KEKKDNNFGE FKFHKVDKK 739
Length:739
Mass (Da):81,297
Last modified:April 29, 2008 - v2
Checksum:i989C5675C2AA01A3
GO

Sequence cautioni

The sequence ABP93090.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000408 Genomic DNA. Translation: ABP93090.1. Different initiation.
RefSeqiYP_001201490.1. NC_009443.1.

Genome annotation databases

EnsemblBacteriaiABP93090; ABP93090; SSU98_1932.
GeneIDi5102835.
KEGGissv:SSU98_1932.
PATRICi19780078. VBIStrSui72275_1896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000408 Genomic DNA. Translation: ABP93090.1 . Different initiation.
RefSeqi YP_001201490.1. NC_009443.1.

3D structure databases

ProteinModelPortali A4W401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391296.SSU98_1932.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP93090 ; ABP93090 ; SSU98_1932 .
GeneIDi 5102835.
KEGGi ssv:SSU98_1932.
PATRICi 19780078. VBIStrSui72275_1896.

Phylogenomic databases

eggNOGi COG1185.
HOGENOMi HOG000218326.
KOi K00962.
OrthoDBi EOG6WT8CC.

Enzyme and pathway databases

BioCyci SSUI391296:GI2E-1988-MONOMER.

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. "A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
    Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y.
    , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
    PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 98HAH33.

Entry informationi

Entry nameiPNP_STRS2
AccessioniPrimary (citable) accession number: A4W401
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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