The domain within your query sequence starts at position 160 and ends at position 339; the E-value for the ATP-grasp_3 domain shown below is 8.1e-9.

STSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSERE
FQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQ
KIIEEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVE

ATP-grasp_3

ATP-grasp_3
PFAM accession number:PF02655
Interpro abstract (IPR003806):

The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyze the formation of amide bonds, catalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule [(PUBMED:9416615)]. This fold is found in many different enzyme families, including various peptide synthetases, biotin carboxylase, synapsin, succinyl-CoA synthetase, pyruvate phosphate dikinase, and glutathione synthetase, amongst others [(PUBMED:12392708)]. These enzymes contribute predominantly to macromolecular synthesis, using ATP-hydrolysis to activate their substrates.

The ATP-grasp fold shares functional and structural similarities with the PIPK (phosphatidylinositol phosphate kinase) and protein kinase superfamilies. The ATP-grasp domain consists of two subdomains with different alpha+beta folds, which grasp the ATP molecule between them. Each subdomain provides a variable loop that forms part of the active site, with regions from other domains also contributing to the active site, even though these other domains are not conserved between the various ATP-grasp enzymes [(PUBMED:7862655)].

This entry describes a type of ATP-grasp fold that is found in a set of proteins of unknown function.

GO function:metal ion binding (GO:0046872), ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-grasp_3