guanylate cyclase soluble subunit alpha heterodimerizes with the beta subunit to form the active guanylate cyclase that catalyzes the synthesis of 3',5'-cyclic GMP via the condensation of 2 GTP molecules; contains a HNOB (Heme NO Binding) domain and a HNOBA domain N-terminal to the catalytic domain
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
316-503
5.19e-70
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.
:
Pssm-ID: 462234 Cd Length: 214 Bit Score: 228.61 E-value: 5.19e-70
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
159-270
6.24e-18
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.
The actual alignment was detected with superfamily member pfam07700:
Pssm-ID: 462233 Cd Length: 162 Bit Score: 81.78 E-value: 6.24e-18
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
316-503
5.19e-70
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.
Pssm-ID: 462234 Cd Length: 214 Bit Score: 228.61 E-value: 5.19e-70
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
485-705
6.01e-69
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
Pssm-ID: 214485 Cd Length: 194 Bit Score: 224.83 E-value: 6.01e-69
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
519-728
8.78e-49
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.
Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 169.68 E-value: 8.78e-49
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
159-270
6.24e-18
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.
Pssm-ID: 462233 Cd Length: 162 Bit Score: 81.78 E-value: 6.24e-18
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
316-503
5.19e-70
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.
Pssm-ID: 462234 Cd Length: 214 Bit Score: 228.61 E-value: 5.19e-70
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
485-705
6.01e-69
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
Pssm-ID: 214485 Cd Length: 194 Bit Score: 224.83 E-value: 6.01e-69
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
519-728
8.78e-49
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.
Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 169.68 E-value: 8.78e-49
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
520-687
1.81e-23
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 96.66 E-value: 1.81e-23
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
159-270
6.24e-18
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.
Pssm-ID: 462233 Cd Length: 162 Bit Score: 81.78 E-value: 6.24e-18
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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