EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR001900 Ribonuclease II/R

Protein matches Help

UniProtKB

Matches:

2541 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001900 RNase_II/R

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00773	RNB	2540
PROSITE pattern	PS01175	RIBONUCLEASE_II	1772
Signatures in BioMart

InterPro Relationships Help

Found in

IPR004476 Ribonuclease II/ribonuclease R, bacteria
IPR011804 Ribonuclease II, bacterial
IPR011805 Ribonuclease R, bacterial

GO Term annotation Help

Function

GO:0003723 RNA binding
GO:0004540 ribonuclease activity

InterPro annotation

Entry Details in BioMart

Abstract

This group of bacterial and eukaryotic proteins represent both characterised and related sequences to exoribonuclease II (RNase II)and ribonuclease R; a bacterial 3' --> 5' exoribonuclease homologous to RNase II [1,2,3].

The size of these proteins range from 644 residues (rnb) to 1250 (SSD1). While their sequence is highly divergent they share a conserved domain in their C-terminal section [4]. It is possible that this domain plays a role in the exonuclease function.

Structural links Help

PDB - click here

SCOP: b.40.4.16

Database links Help

PDBe-motif: PS01175

Enzyme: EC:3.1

PROSITE doc: PDOC00904

PANDIT: PF00773

Blocks: IPB001900

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001900

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P73177 Uncharacterized ribonuclease sll1290

Q08162 Exosome complex exonuclease DIS3

Q09568 Uncharacterized ribonuclease F48E8.6

Q8C0S1 DIS3-like exonuclease 1

Q8IYB7 DIS3-like exonuclease 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013223	Ribonuclease B, N-terminal OB domain
IPR001900	Ribonuclease II/R
IPR003029	Ribosomal protein S1, RNA binding domain
IPR006596	Nucleotide binding protein, PINc
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Cheng ZF, Deutscher MP. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277 21624-9 2002 [PubMed: 11948193] http://dx.doi.org/10.1074/jbc.M202942200
2.	Kishine M, Takabayashi A, Munekage Y, Shikanai T, Endo T, Sato F. Ribosomal RNA processing and an RNase R family member in chloroplasts of Arabidopsis. Plant Mol. Biol. 55 595-606 2004 [PubMed: 15604703] http://dx.doi.org/10.1007/s11103-004-1507-1
3.	Dziembowski A, Malewicz M, Minczuk M, Golik P, Dmochowska A, Stepien PP. The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA. Mol. Gen. Genet. 260 108-14 1998 [PubMed: 9829834] http://dx.doi.org/10.1007/s004380050876
4.	Mian IS. Comparative sequence analysis of ribonucleases HII, III, II PH and D. Nucleic Acids Res. 25 3187-95 1997 [PubMed: 9241229] http://dx.doi.org/10.1093/nar/25.16.3187

Additional Reading Open in usermanual
	Amblar M, Barbas A, Fialho AM, Arraiano CM. Characterization of the functional domains of Escherichia coli RNase II. J. Mol. Biol. 360 2006 921-33 [PubMed: 16806266] http://dx.doi.org/10.1016/j.jmb.2006.05.043
	Noguchi E, Hayashi N, Azuma Y, Seki T, Nakamura M, Nakashima N, Yanagida M, He X, Mueller U, Sazer S, Nishimoto T. Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1. EMBO J. 15 1996 5595-605 [PubMed: 8896453] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8896453&action=stream&blobtype=pdf
	Frazao C, McVey CE, Amblar M, Barbas A, Vonrhein C, Arraiano CM, Carrondo MA. Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature 443 2006 110-4 [PubMed: 16957732] http://dx.doi.org/10.1038/nature05080
	Lorentzen E, Basquin J, Tomecki R, Dziembowski A, Conti E. Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol. Cell 29 2008 717-28 [PubMed: 18374646] http://dx.doi.org/10.1016/j.molcel.2008.02.018
	Zuo Y, Vincent HA, Zhang J, Wang Y, Deutscher MP, Malhotra A. Structural basis for processivity and single-strand specificity of RNase II. Mol. Cell 24 2006 149-56 [PubMed: 16996291] http://dx.doi.org/10.1016/j.molcel.2006.09.004
	Cheng ZF, Zuo Y, Li Z, Rudd KE, Deutscher MP. The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J. Biol. Chem. 273 1998 14077-80 [PubMed: 9603904] http://dx.doi.org/10.1074/jbc.273.23.14077
	Zilhao R, Camelo L, Arraiano CM. DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II. Mol. Microbiol. 8 1993 43-51 [PubMed: 8497196] http://dx.doi.org/10.1111/j.1365-2958.1993.tb01201.x
	Beuf L, Bedu S, Cami B, Joset F. A protein is involved in accessibility of the inhibitor acetazolamide to the carbonic anhydrase(s) in the cyanobacterium Synechocystis PCC 6803. Plant Mol. Biol. 27 1995 779-88 [PubMed: 7727754] http://dx.doi.org/10.1007/BF00020230
	McVey CE, Amblar M, Barbas A, Cairrao F, Coelho R, Romao C, Arraiano CM, Carrondo MA, Frazao C. Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 684-7 [PubMed: 16820694]

InterPro 23.1