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InterPro: IPR001352 Ribonuclease HII/HIII

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UniProtKB

Matches:

2294 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
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Accession

IPR001352 RNase_HII/HIII

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01351	RNase_HII	2294
PANTHER	PTHR10954	RNase_HII/HIII	1962
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012337 Polynucleotidyl transferase, ribonuclease H fold

Children

IPR004641 Ribonuclease HIII
IPR004649 Ribonuclease H2, subunit A

GO Term annotation Help

Function

GO:0003723 RNA binding
GO:0004523 ribonuclease H activity

InterPro annotation

Entry Details in BioMart

Abstract

Ribonuclease HII is involved in the degradation of the ribonucleotide moiety on RNA-DNA hybrid molecules carrying out endonucleolytic cleavage to 5'-phospo-monoester. Proteins which belong to this family have been found in bacteria, archaea, and yeasts. This family also includes Ribonuclease HIII.

Structural links Help

PDB - click here

SCOP: c.55.3.1

CATH: 1.10.10.460 , 3.30.420.10

Database links Help

Enzyme: EC:3.1.26.4

PANDIT: PF01351

Blocks: IPB001352

Pfam Clan: CL0219.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001352

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75792 Ribonuclease H2 subunit A

P53942 Ribonuclease H2 subunit A

Q9CWY8 Ribonuclease H2 subunit A

Q9U6P6 Ribonuclease H2 subunit A

Q9VPP5 Ribonuclease H2 subunit A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001352	Ribonuclease HII/HIII
IPR012337	Polynucleotidyl transferase, ribonuclease H fold
IPR004649	Ribonuclease H2, subunit A
	SWISS-MODEL
	ModBase

Publications Help

Additional Reading Open in usermanual
	Chapados BR, Chai Q, Hosfield DJ, Qiu J, Shen B, Tainer JA. Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication. J. Mol. Biol. 307 2001 541-56 [PubMed: 11254381] http://dx.doi.org/10.1006/jmbi.2001.4494
	Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S. Conformational contagion in a protein: structural properties of a chameleon sequence. Proteins 68 2007 617-25 [PubMed: 17510955] http://dx.doi.org/10.1002/prot.21451
	Takano K, Endo S, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S. Structure of amyloid beta fragments in aqueous environments. FEBS J. 273 2006 150-8 [PubMed: 16367755] http://dx.doi.org/10.1111/j.1742-4658.2005.05051.x
	Mian IS. Comparative sequence analysis of ribonucleases HII, III, II PH and D. Nucleic Acids Res. 25 1997 3187-95 [PubMed: 9241229] http://dx.doi.org/10.1093/nar/25.16.3187
	Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K. Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses. Protein Sci. 10 2001 707-14 [PubMed: 11274461] http://dx.doi.org/10.1110/ps.48001
	Lai L, Yokota H, Hung LW, Kim R, Kim SH. Crystal structure of archaeal RNase HII: a homologue of human major RNase H. Structure 8 2000 897-904 [PubMed: 10997908] http://dx.doi.org/10.1016/S0969-2126(00)00179-9

InterPro 23.1