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InterPro: IPR002466 Adenosine deaminase/editase

Protein matchesHelp
UniProtKB
Matches:
275 proteins
AccessionHelp IPR002466 A_deamin
SecondaryHelp IPR001365
TypeHelp Domain
SignaturesHelp
GO Term annotationHelp
Process GO:0006396 RNA processing
Function GO:0003723 RNA binding
GO:0004000 adenosine deaminase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Editase (EC:3.5) are enzymes that alter mRNA by catalyzing the site-selective deamination of adenosine residue into inosine residue. The editase domain contains the active site and binds three Zn atoms [1]. Several editases share a common global arrangement of domains, from N to C terminus: two 'double-stranded RNA-specific adenosine deaminase' (DRADA) repeat domains (IPR000607), followed by three 'double-stranded RNA binding' (DsRBD) domains (IPR001159), followed by the editase domain. Other editases have a simplified domains structure with no DRADA_REP and possibly fewer DSRBD domains. Editase that deaminate cytidine are not detected by this signature.

Database linksHelp
PROSITE doc: PDOC50141
PANDIT: PF02137
Blocks: IPB002466

Taxonomic coverageHelp

Example proteinsHelp
P53065 tRNA-specific adenosine deaminase 1

P55265 Double-stranded RNA-specific adenosine deaminase

Q22618 Probable double-stranded RNA-specific adenosine deaminase

Q5SUE7 Adenosine deaminase domain-containing protein 1

Q9NII1 Double-stranded RNA-specific editase Adar

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011991 Winged helix repressor DNA-binding
IPR002466 Adenosine deaminase/editase
IPR000607 Double-stranded RNA-specific adenosine deaminase (DRADA)
IPR001159 Double-stranded RNA binding
IPR014720 Double-stranded RNA-binding-like
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Maas S, Melcher T, Seeburg PH.
Mammalian RNA-dependent deaminases and edited mRNAs.
Curr. Opin. Cell Biol. 9 343-9 1997 [PubMed: 9159072]
http://dx.doi.org/10.1016/S0955-0674(97)80006-3

Additional ReadingHelp
Slavov D, Crnogorac-Jurcevic T, Clark M, Gardiner K.
Comparative analysis of the DRADA A-to-I RNA editing gene from mammals, pufferfish and zebrafish.
Gene 250 2000 53-60 [PubMed: 10854778]
http://dx.doi.org/10.1016/S0378-1119(00)00175-X
Keegan LP, Leroy A, Sproul D, O'Connell MA.
Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes.
Genome Biol. 5 2004 209 [PubMed: 14759252]
http://dx.doi.org/10.1186/gb-2004-5-2-209
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InterPro 23.1