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IPR036523

Description

IPR036523 is a SurE-like phosphatase/nucleotidase superfamily.

<p>This entry represents a SurE-like structural domain superfamily with a 3-layer α/β/α topology that bears some topological similarity to the N-terminal domain of the glutaminase/asparaginase family. This domain is found in the stationary phase survival protein SurE, a metal ion-dependent phosphatase found in eubacteria, archaea and eukaryotes. In Escherichia coli, SurE also has activity as a nucleotidase and exopolyphosphatase, and may be involved in the stress response [[cite:PUB00042609]]. E. coli cells with mutations in the surE gene survive poorly in stationary phase [[cite:PUB00015315]]. The structure of SurE homologues have been determined from Thermotoga maritima [[cite:PUB00026311]] and the archaea Pyrobaculum aerophilum [[cite:PUB00017354]]. The T. maritima SurE homologue has phosphatase activity that is inhibited by vanadate or tungstate, both of which bind adjacent to the divalent metal ion.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function Hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.

Associated Lotus transcripts 1

Transcript Name Description Predicted domains Domain count
5'-nucleotidase surE; TAIR: AT1G72880.1 Survival protein SurE-like phosphatase/nucleotidase; Swiss-Prot: sp|A1VY14|SURE_CAMJJ 5'-nucleotidase SurE; TrEMBL-Plants: tr|C6TGC8|C6TGC8_SOYBN Putative uncharacterized protein; Found in the gene: LotjaGi3g1v0027600 10

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
mobidb-lite MobiDBLite 1 100.00