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 .
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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:||89|
|Number in full:||3458|
|Average length of the domain:||79.20 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||51.70 %|
|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:||1|
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