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InterPro: IPR003156 Phosphoesterase, DHHA1

Protein matchesHelp
UniProtKB
Matches:
5287 proteins
AccessionHelp IPR003156 Pesterase_DHHA1
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR002318 Alanyl-tRNA synthetase, class IIc
IPR004610 Bacterial RecJ exonuclease
IPR014528 Signal transduction phosphoesterase predicted, YybT type
GO Term annotationHelp
Function GO:0003676 nucleic acid binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is often found adjacent to the DHH domain, found in the RecJ-like phosphoesterase family IPR001667, and is called DHHA1 for DHH associated domain. DHHA1 is diagnostic of DHH subfamily 1 members [1]. This domain is also found in alanyl tRNA synthetase e.g. P00957, suggesting that it may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif.

Structural linksHelp
SCOP: c.107.1.2
Database linksHelp
Enzyme: EC:6.1.1.7
PANDIT: PF02272
Blocks: IPB003156

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003156 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P36428 Alanyl-tRNA synthetase, mitochondrial

P40825 Alanyl-tRNA synthetase, cytoplasmic

P49588 Alanyl-tRNA synthetase, cytoplasmic

P74423 Alanyl-tRNA synthetase

Q8BGQ7 Alanyl-tRNA synthetase, cytoplasmic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012947 Threonyl/alanyl tRNA synthetase, SAD
IPR002318 Alanyl-tRNA synthetase, class IIc
IPR018165 Alanyl-tRNA synthetase, class IIc, core domain
IPR003156 Phosphoesterase, DHHA1
IPR018162 Alanyl-tRNA synthetase, class IIc, anti-codon-binding domain
IPR018163 Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain
IPR018164 Alanyl-tRNA synthetase, class IIc, N-terminal
SWISS-MODEL
ModBase

PublicationsHelp
1. Aravind L, Koonin EV.
A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease.
Trends Biochem. Sci. 23 17-9 1998 [PubMed: 9478130]
http://dx.doi.org/10.1016/S0968-0004(97)01162-6

Additional ReadingHelp
Yamagata A, Kakuta Y, Masui R, Fukuyama K.
The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity.
Proc. Natl. Acad. Sci. U.S.A. 99 2002 5908-12 [PubMed: 11972066]
http://dx.doi.org/10.1073/pnas.092547099
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InterPro 23.1