Summary
CYTH domain
These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Six distinct non-homologous classes of AC have been identified. The structure of three classes of adenylyl cyclases have been solved [3].
Literature references
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Sismeiro O, Trotot P, Biville F, Vivares C, Danchin A; , J Bacteriol 1998;180:3339-3344.: Aeromonas hydrophila adenylyl cyclase 2: a new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic archaebacteria. PUBMED:9642185
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Iyer LM, Aravind L; , BMC Genomics 2002;3:33-33.: The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates. PUBMED:12456267
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Gallagher DT, Smith NN, Kim SK, Heroux A, Robinson H, Reddy PT; , J Mol Biol. 2006;362:114-122.: Structure of the class IV adenylyl cyclase reveals a novel fold. PUBMED:16905149
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Smith N, Kim SK, Reddy PT, Gallagher DT; , Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006;62:200-204.: Crystallization of the class IV adenylyl cyclase from Yersinia pestis. PUBMED:16511301
InterPro entry IPR008172
These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate.
The protein CyaB from Aeromonas hydrophila is a second adenylyl cyclase from that species, as demonstrated by complementation in Escherichia coli and by assay of the enzymatic properties of purified recombinant protein PUBMED:9642185. It has no detectable homology to any other protein of known function, and has several unusual properties, including an optimal temperature of 65 degrees and an optimal pH of 9.5. A cluster of uncharacterised archaeal homologs may be orthologous and serve (under certain circumstances) to produce the regulatory metabolite cyclic AMP (cAMP).
Clan
This family is a member of clan CYTH (CL0273), which contains the following 2 members:
CYTH mRNA_triPaseGene Ontology
| Molecular function | adenylate cyclase activity (GO:0004016) |
| Biological process | cAMP biosynthetic process (GO:0006171) |
External database links
| PANDIT: | PF01928 |
| SYSTERS: | CYTH |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Aravind L |
| Previous IDs: | Adenylate_cyc_2; |
| Type: | Domain |
| Author: | Aravind L |
| Number in seed: | 56 |
| Number in full: | 1351 |
| Average length of the domain: | 181.70 aa |
| Average identity of full alignment: | 20 % |
| Average coverage of the sequence by the domain: | 64.75 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 187 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
CYTHStructures
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 CYTH domain has been found.
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