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ProRule PRU00886


General rule information [?]

PURL https://purl.expasy.org/prosite/rule/PRU00886
Accession PRU00886
Dates 4-JAN-2012 (Created)
19-NOV-2022 (Last updated, Version 6)
Data class Domain;
Predictors PROSITE; PS51553; GMPS_ATP_PPASE
Name GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain
Function The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five- stranded parallel beta-sheet sandwiched between helical layers. It contains a glycine rich ATP-binding motif called the "P-loop motif" located after the first beta-strand
Scope(s) Bacteria
Archaea
Eukaryota
Example(s) Q8TYD7 (GUAAB_METKA);

Propagated annotation [?]

Keywords [?]

ATP-binding
GMP biosynthesis
Nucleotide-binding
Purine biosynthesis

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0006177; Biological process:GMP biosynthetic process
GO:0000166; Molecular function:nucleotide binding
GO:0006164; Biological process:purine nucleotide biosynthetic process

Features [?]

From: PS51553
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="GMPS ATP-PPase #"
BINDING 28 34 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
/ligand_label="#"

Additional information [?]

Size range 172-208 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.



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UniProtKB rule member sequences [?]