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Haem-NO-binding Provide feedback
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.
Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J; , Proc Natl Acad Sci U S A 2004;101:12854-12859.: Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. PUBMED:15326296 EPMC:15326296
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011644
This ligand-binding domain is found in soluble guanylate cyclases. In soluble guanylate cyclases this domain binds heme via a covalent linkage to histidine [PUBMED:15326296]. Soluble guanylate cyclases are nitric oxide-responsive signaling proteins.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||heme binding (GO:0020037)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This clan contains families that bind small molecules and are predominantly involved in signalling. Members include the heme NO binding domain. This domain is related to soluble guanylate cyclases and is mainly alpha helical in structure. Other members of this clan include V4R, which is predicted to be a small molecule binding domain, and a domain often found adjacent to this that is found on activators of aromatic catabolism, and on signalling molecules.
The clan contains the following 3 members:HNOB V4R XylR_N
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
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Curation and family details
|Author:||Iyer LM, Anantharaman V, Aravind L, Studholme DJ|
|Number in seed:||184|
|Number in full:||1441|
|Average length of the domain:||152.90 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||34.22 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HNOB domain has been found. There are 73 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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