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InterPro: IPR001568 Ribonuclease T2

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2174 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR001568 RNase_T2

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.730.10	RNase_T2	1960
Pfam	PF00445	Ribonuclease_T2	2008
PANTHER	PTHR11240	RNase_T2	1699
SuperFamily	SSF55895	RNase_T2	2165
Signatures in BioMart

InterPro Relationships Help

Contains

IPR018188 Ribonuclease T2, active site

GO Term annotation Help

Function

GO:0003723 RNA binding
GO:0033897 ribonuclease T2 activity

InterPro annotation

Entry Details in BioMart

Abstract

The fungal ribonucleases T2 from Aspergillus oryzae, M from Aspergillus saitoi and Rh from Rhizopus niveus are structurally and functionally related 30 Kd glycoproteins [1] that cleave the 3'-5' internucleotide linkage of RNA via a nucleotide 2',3'-cyclic phosphate intermediate (EC:3.1.27.1).

Two histidines residues have been shown [2, 3] to be involved in the catalytic mechanism of RNase T2 and Rh. These residues and the region around them are highly conserved in a number of other RNAses that have been found to be evolutionary related to these fungal enzymes.

Structural links Help

PDB - click here

SCOP: d.124.1.1

CATH: 3.90.730.10

Database links Help

PDBe-motif: PS00530 , PS00531

Enzyme: EC:3.1.27

PROSITE doc: PDOC00459

PANDIT: PF00445

Blocks: IPB001568

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001568

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00584 Ribonuclease T2

P21338 Ribonuclease I

P42813 Ribonuclease 1

Q02933 Ribonuclease T2-like

Q9CQ01 Ribonuclease T2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018188	Ribonuclease T2, active site
IPR001568	Ribonuclease T2
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Watanabe H, Naitoh A, Suyama Y, Inokuchi N, Shimada H, Koyama T, Ohgi K, Irie M. Primary structure of a base non-specific and adenylic acid preferential ribonuclease from Aspergillus saitoi. J. Biochem. 108 303-10 1990 [PubMed: 2229029] http://jb.oxfordjournals.org/cgi/content/abstract/108/2/303
2.	Kawata Y, Sakiyama F, Hayashi F, Kyogoku Y. Identification of two essential histidine residues of ribonuclease T2 from Aspergillus oryzae. Eur. J. Biochem. 187 255-62 1990 [PubMed: 2298207] http://dx.doi.org/10.1111/j.1432-1033.1990.tb15303.x
3.	Kurihara H, Mitsui Y, Ohgi K, Irie M, Mizuno H, Nakamura KT. Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus. FEBS Lett. 306 189-92 1992 [PubMed: 1633875] http://dx.doi.org/10.1016/0014-5793(92)80997-U

Additional Reading Open in usermanual
	Ida K, Norioka S, Yamamoto M, Kumasaka T, Yamashita E, Newbigin E, Clarke AE, Sakiyama F, Sato M. The 1.55 A resolution structure of Nicotiana alata S(F11)-RNase associated with gametophytic self-incompatibility. J. Mol. Biol. 314 2001 103-12 [PubMed: 11724536] http://dx.doi.org/10.1006/jmbi.2001.5127
	Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ. Structure of an RNase-related protein from Calystegia sepium. Acta Crystallogr. D Biol. Crystallogr. 58 2002 627-33 [PubMed: 11914487] http://dx.doi.org/10.1107/S090744490200255X
	Kimura K, Numata T, Kakuta Y, Kimura M. Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes. Biosci. Biotechnol. Biochem. 68 2004 1748-57 [PubMed: 15322360] http://dx.doi.org/10.1271/bbb.68.1748
	Kurihara H, Nonaka T, Mitsui Y, Ohgi K, Irie M, Nakamura KT. The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0 A resolution. J. Mol. Biol. 255 1996 310-20 [PubMed: 8551522] http://dx.doi.org/10.1006/jmbi.1996.0025
	Kawano S, Kakuta Y, Kimura M. Guanine binding site of the Nicotiana glutinosa ribonuclease NW revealed by X-ray crystallography. Biochemistry 41 2002 15195-202 [PubMed: 12484757] http://dx.doi.org/10.1021/bi026247l
	Numata T, Suzuki A, Kakuta Y, Kimura K, Yao M, Tanaka I, Yoshida Y, Ueda T, Kimura M. Crystal structures of the ribonuclease MC1 mutants N71T and N71S in complex with 5'-GMP: structural basis for alterations in substrate specificity. Biochemistry 42 2003 5270-8 [PubMed: 12731868] http://dx.doi.org/10.1021/bi034103g

InterPro 24.0