The domain within your query sequence starts at position 142 and ends at position 177; the E-value for the ADK_lid domain shown below is 4.2e-17.

RLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSD

ADK_lid

ADK_lid
PFAM accession number:PF05191
Interpro abstract (IPR007862):

Adenylate kinases (ADK; EC 2.7.4.3) are phosphotransferases that catalyse the Mg-dependent reversible conversion of ATP and AMP to two molecules of ADP, an essential reaction for many processes in living cells. In large variants of adenylate kinase, the AMP and ATP substrates are buried in a domain that undergoes conformational changes from an open to a closed state when bound to substrate; the ligand is then contained within a highly specific environment required for catalysis. Adenylate kinase is a 3-domain protein consisting of a large central CORE domain flanked by a LID domain on one side and the AMP-binding NMPbind domain on the other [(PUBMED:17299745)]. The LID domain binds ATP and covers the phosphates at the active site. The substrates first bind the CORE domain, followed by closure of the active site by the LID and NMPbind domains.

Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organisms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues (two CX(n)C motifs) are responsible for the binding of a zinc ion. The bound zinc ion in the lid domain is clearly structurally homologous to Zinc-finger domains. However, it is unclear whether the adenylate kinase lid is a novel zinc-finger DNA/RNA binding domain, or that the lid bound zinc serves a purely structural function [(PUBMED:9715904)].

GO function:adenylate kinase activity (GO:0004017)

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