The domain within your query sequence starts at position 43 and ends at position 168; the E-value for the AdoHcyase domain shown below is 2e-59.

NFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIE
TLCALGAQCRWSACNIYSTQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQA
NMAVSA

AdoHcyase

AdoHcyase
PFAM accession number:PF05221
Interpro abstract (IPR000043):

Adenosylhomocysteinase (S-adenosyl-L-homocysteine hydrolase, EC 3.3.1.1 ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. This enzyme is ubiquitous, highly conserved, and may play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. AdoHcyase requires NAD + as a cofactor and contains a central glycine-rich region which is thought to be involved in NAD-binding. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+ [ (PUBMED:9586999) (PUBMED:16061414) (PUBMED:11325033) (PUBMED:15165742) ].

This family also includes S-adenosylhomocysteine hydrolase-like 1 (Ahcyl1), also known as IRBIT, and S-adenosylhomocysteine hydrolase-like protein 2 (Ahcyl2). Ahcyl1/IRBIT was shown to interact with inositol 1,4,5-trisphosphate receptors (IP3Rs), which function as intracellular Ca(2+) channels, and suppresses IP3 binding of IP3R [ (PUBMED:16793548) (PUBMED:16527252) ]. By competing with IP3, it modulates the threshold IP3 concentration required for the activation of the receptor [ (PUBMED:16793548) ]. Further studies indicate that Ahcyl1/IRBIT is in fact a multifunctional protein that regulates several ion channels and ion transporters [ (PUBMED:24518248) (PUBMED:21152975) ]. Despite its homology to S-adenosylhomocysteine hydrolases, Ahcyl1 has neither enzyme activity nor any effects on the enzyme activity of S-adenosylhomocysteine hydrolase [ (PUBMED:12525476) ]. Ahcyl2 lacks binding activity to IP3R [ (PUBMED:19220705) ]. Ahcyl2 upregulates NBCe1-B, which plays an important role in intracellular pH regulation [ (PUBMED:27382360) ].

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