Summary: STAS domain
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The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function .
Kovacs H, Comfort D, Lord M, Campbell ID, Yudkin MD; , Proc Natl Acad Sci U S A 1998;95:5067-5071.: Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis. PUBMED:9560229 EPMC:9560229
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This tab holds annotation information from the InterPro database.
InterPro entry IPR002645
The STAS (Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C-terminal region of sulphate transporters and bacterial anti-sigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.
Malfunctions in members of the SLC26A family of anion transporters are involved in three human diseases: diastrophic dysplasia/achondrogenesis type 1B (DTDST), Pendred's syndrome (PDS) and congenital chloride diarrhea (CLD). These proteins contain 12 transmembrane helices followed by a cytoplasmic STAS domain at the C terminus. The importance of the STAS domain in these transporters is illustrated by the fact that a number of mutations in PDS and DTDST map to it [PUBMED:10662676].
The activity of bacterial sigma transcription factors is controlled by a regulatory cascade involving an antisigma-factor, the antisigma-factor antagonist (ASA) and a phosphatase. The antisigma-factor binds to sigma and holds it in an inactive complex. The ASA can also interact with the anti-sigma-factor, allowing the release of the active sigma factor. As the antisigma-factor is a protein kinase, it can phosphorylate the antisigma antagonist on a conserved serine residue of the STAS domain. This phosphorylation inactivates the ASA that can be reactivated through dephosphorylation by a phosphatase [PUBMED:10662676, PUBMED:10476035]. The STAS domain of the ASA SpoIIAA binds GTP and ATP and possesses a weak NTPase activity. Strong sequence conservation suggests that the STAS domain could possess general NTP-binding activity, and it has been proposed that the NTPs are likely to elicit specific conformational changes in the STAS domain through binding and/or hydrolysis [PUBMED:10662676].
Resolution of the solution structure of the ASA SpoIIAA from Bacillus subtilis has shown that the STAS domain consists of a four-stranded beta-sheet and four alpha helices. The STAS domain forms a characteristic alpha-helical handle-like structure [PUBMED:10662676, PUBMED:9560229].
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Curation and family details
|Number in seed:||68|
|Number in full:||10190|
|Average length of the domain:||111.40 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||25.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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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 STAS domain has been found. There are 44 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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