The domain within your query sequence starts at position 285 and ends at position 442; the E-value for the Guanylate_cyc domain shown below is 2.3e-12.

YLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVHITSVLKVFRGQINKVFMFDKGCSF
LCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTVRHEY
TVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFF

Guanylate_cyc

Guanylate_cyc
PFAM accession number:PF00211
Interpro abstract (IPR001054):

Guanylate cyclases (EC 4.6.1.2) catalyse the formation of cyclic GMP (cGMP) from GTP. cGMP acts as an intracellular messenger, activating cGMP-dependent kinases and regulating cGMP-sensitive ion channels. The role of cGMP as a second messenger in vascular smooth muscle relaxation and retinal photo-transduction is well established. Guanylate cyclase is found both in the soluble and particulate fractions of eukaryotic cells. The soluble and plasma membrane-bound forms differ in structure, regulation and other properties [(PUBMED:1349465), (PUBMED:1356629), (PUBMED:1680765), (PUBMED:1982420)]. Most currently known plasma membrane-bound forms are receptors for small polypeptides. The soluble forms of guanylate cyclase are cytoplasmic heterodimers having alpha and beta subunits.

In all characterised eukaryote guanylyl- and adenylyl cyclases, cyclic nucleotide synthesis is carried out by the conserved class III cyclase domain.

GO process:cyclic nucleotide biosynthetic process (GO:0009190), intracellular signal transduction (GO:0035556)
GO function:phosphorus-oxygen lyase activity (GO:0016849)

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