SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A6Q4N2

- PNP_NITSB

UniProt

A6Q4N2 - PNP_NITSB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Polyribonucleotide nucleotidyltransferase
Gene
pnp, NIS_1333
Organism
Nitratiruptor sp. (strain SB155-2)
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 bindingi516 – 5161Magnesium By similarity
Metal bindingi522 – 5221Magnesium 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

BioCyciNSP387092:GHA5-1378-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:NIS_1333
OrganismiNitratiruptor sp. (strain SB155-2)
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
ProteomesiUP000001118: 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 – 732732Polyribonucleotide nucleotidyltransferaseUniRule annotation
PRO_0000329733Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi387092.NIS_1333.

Structurei

3D structure databases

ProteinModelPortaliA6Q4N2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini582 – 64261KH
Add
BLAST
Domaini659 – 72668S1 motif
Add
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1185.
HOGENOMiHOG000218326.
KOiK00962.
OMAiPRWDWVA.
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]
SUPFAMiSSF50249. 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.

A6Q4N2-1 [UniParc]FASTAAdd to Basket

« Hide

MKCRFEFEMN NLKEIYEFGE VAKQTNGSVL LKSGKTVMLA TVVMEKEMVD    50
EDFLPLTVQY IEKSYAAGKI PGGFVKREQK PGDFETLTAR IVDRALRPLF 100
PKGYLYPTVI TVMVLSADPE SDLQVLALNA ASAALFVSDI PVRKAVSGLR 150
VAKVDGEVLF NPPLSKLKES TLDLYLAGTK EELLMIEMAA IGSYKTEVVP 200
TTVDPLMDPT LAEEVITIKE PNAMKEEELA SIIAQGKDVI QIACNEYEKY 250
FIESAKEQLE LELLPQTIDE DIWTYVEEIY AADIKEAVQA MAKSERNELL 300
KEIAKKISED DVAKEQGWEY ETIYKVVEKY KRKIVREMIL NEGKRADGRG 350
LKDVRPIDIK TNILPSAHGS CLFTRGETQA LVVCTIGEKT DAQMYEMLTS 400
KGPEYEHFMV HYNFPPFSVG EAKPISAPGR RELGHGNLAR RALEPVVDVP 450
EDKTYRLVSE ILESNGSSSM ATVCGGALAL KAANIDLADL VAGVAMGLIV 500
EDDKYAILTD IMGLEDHDGD MDFKVAGTHD GVTAMQMDIK LGGVQQEILE 550
QALQQAREAR LHILKIMEEA AEKIEINEEN LPSSHTITVH PSKIVDIIGQ 600
AGKTIKEIIE KFEVSIDIDR DKGKVKVTGK NRPKVIAACD YIQEITNKPK 650
PEPVKFQEGD ILKGKIKRTT NFGAFVELPG GVDGLLHISK LSSGRVERVE 700
DVVNIGDEVE VEVLSQKGHK IELGLRQVLK KA 732
Length:732
Mass (Da):81,125
Last modified:August 21, 2007 - v1
Checksum:i15A5660875F92DF4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009178 Genomic DNA. Translation: BAF70441.1.
RefSeqiWP_012082704.1. NC_009662.1.
YP_001356798.1. NC_009662.1.

Genome annotation databases

EnsemblBacteriaiBAF70441; BAF70441; NIS_1333.
GeneIDi5361531.
KEGGinis:NIS_1333.
PATRICi22684810. VBINitSp82229_1402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009178 Genomic DNA. Translation: BAF70441.1 .
RefSeqi WP_012082704.1. NC_009662.1.
YP_001356798.1. NC_009662.1.

3D structure databases

ProteinModelPortali A6Q4N2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 387092.NIS_1333.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF70441 ; BAF70441 ; NIS_1333 .
GeneIDi 5361531.
KEGGi nis:NIS_1333.
PATRICi 22684810. VBINitSp82229_1402.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NSP387092:GHA5-1378-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 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. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB155-2.

Entry informationi

Entry nameiPNP_NITSB
AccessioniPrimary (citable) accession number: A6Q4N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 50 of the entry and version 1 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

Similar proteinsi