Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, ...
662-730
2.18e-12
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function; The SulP family is a large and diverse family of anion transporters, with members from eubacteria, plants, fungi, and mammals. They contain 10 to 14 transmembrane helices which form the catalytic core of the protein and a C-terminal extension, the STAS (Sulphate Transporter and AntiSigma factor antagonist) domain which plays a role in the function and regulation of the transport activity. The STAS 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.
:
Pssm-ID: 132913 [Multi-domain] Cd Length: 107 Bit Score: 64.19 E-value: 2.18e-12
high affinity sulphate transporter 1; The SulP family is a large and ubiquitous family with ...
57-561
4.00e-100
high affinity sulphate transporter 1; The SulP family is a large and ubiquitous family with over 30 sequenced members derived from bacteria, fungi, plants and animals. Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues. Many of these proteins are functionally characterized, and all are sulfate uptake transporters. Some transport their substrate with high affinities, while others transport it with relatively low affinities. Most function by SO42- :H+symport, but SO42- :HCO3- antiport has been reported for the rat protein (spP45380). The bacterial proteins vary in size from 434 residues to 566 residues with one exception, a Mycobacterium tuberculosis protein with 784 residues. The eukaryotic proteins vary in size from 611 residues to 893 residues with one exception, a protein designated "early nodulin 70 protein" from Glycine max which is reported to be of 485 residues. Thus, the eukaryotic proteins are almost without exception larger than the prokaryotic proteins. These proteins exhibit 10-13 putative transmembrane a-helical spanners (TMSs) depending on the protein. The phylogenetic tree for the SulP family reveals five principal branches. Three of these are bacterial specific as follows: one bears a single protein from M. tuberculosis; a second bears two proteins, one from M. tuberculosis, the other from Synechocystis sp, and the third bears all remaining prokaryotic proteins. The remaining two clusters bear only eukaryotic proteins with the animal proteins all localized to one branch and the plant and fungal proteins localized to the other. The generalized transport reactions catalyzed by SulP family proteins are: (1) SO42- (out) + nH+ (out) --> SO42- (in) + nH+ (in). (2) SO42- (out) + nHCO3- (in) SO42- (in) + nHCO3- (out). [Transport and binding proteins, Anions]
Pssm-ID: 273284 [Multi-domain] Cd Length: 552 Bit Score: 320.43 E-value: 4.00e-100
Sulfate permease family; This family of integral membrane proteins are known as the Sulfate ...
74-468
2.36e-98
Sulfate permease family; This family of integral membrane proteins are known as the Sulfate Permease (SulP) family. SulP is a large family found in all domains of life. Although sulfate is a commonly transported ion there are many other activities in this family. See the TCDB description for a comprehensive summary.
Pssm-ID: 459995 [Multi-domain] Cd Length: 379 Bit Score: 309.95 E-value: 2.36e-98
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, ...
662-730
2.18e-12
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function; The SulP family is a large and diverse family of anion transporters, with members from eubacteria, plants, fungi, and mammals. They contain 10 to 14 transmembrane helices which form the catalytic core of the protein and a C-terminal extension, the STAS (Sulphate Transporter and AntiSigma factor antagonist) domain which plays a role in the function and regulation of the transport activity. The STAS 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.
Pssm-ID: 132913 [Multi-domain] Cd Length: 107 Bit Score: 64.19 E-value: 2.18e-12
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
663-733
1.15e-11
STAS domain; 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.
Pssm-ID: 426404 [Multi-domain] Cd Length: 106 Bit Score: 61.86 E-value: 1.15e-11
high affinity sulphate transporter 1; The SulP family is a large and ubiquitous family with ...
57-561
4.00e-100
high affinity sulphate transporter 1; The SulP family is a large and ubiquitous family with over 30 sequenced members derived from bacteria, fungi, plants and animals. Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues. Many of these proteins are functionally characterized, and all are sulfate uptake transporters. Some transport their substrate with high affinities, while others transport it with relatively low affinities. Most function by SO42- :H+symport, but SO42- :HCO3- antiport has been reported for the rat protein (spP45380). The bacterial proteins vary in size from 434 residues to 566 residues with one exception, a Mycobacterium tuberculosis protein with 784 residues. The eukaryotic proteins vary in size from 611 residues to 893 residues with one exception, a protein designated "early nodulin 70 protein" from Glycine max which is reported to be of 485 residues. Thus, the eukaryotic proteins are almost without exception larger than the prokaryotic proteins. These proteins exhibit 10-13 putative transmembrane a-helical spanners (TMSs) depending on the protein. The phylogenetic tree for the SulP family reveals five principal branches. Three of these are bacterial specific as follows: one bears a single protein from M. tuberculosis; a second bears two proteins, one from M. tuberculosis, the other from Synechocystis sp, and the third bears all remaining prokaryotic proteins. The remaining two clusters bear only eukaryotic proteins with the animal proteins all localized to one branch and the plant and fungal proteins localized to the other. The generalized transport reactions catalyzed by SulP family proteins are: (1) SO42- (out) + nH+ (out) --> SO42- (in) + nH+ (in). (2) SO42- (out) + nHCO3- (in) SO42- (in) + nHCO3- (out). [Transport and binding proteins, Anions]
Pssm-ID: 273284 [Multi-domain] Cd Length: 552 Bit Score: 320.43 E-value: 4.00e-100
Sulfate permease family; This family of integral membrane proteins are known as the Sulfate ...
74-468
2.36e-98
Sulfate permease family; This family of integral membrane proteins are known as the Sulfate Permease (SulP) family. SulP is a large family found in all domains of life. Although sulfate is a commonly transported ion there are many other activities in this family. See the TCDB description for a comprehensive summary.
Pssm-ID: 459995 [Multi-domain] Cd Length: 379 Bit Score: 309.95 E-value: 2.36e-98
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, ...
662-730
2.18e-12
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function; The SulP family is a large and diverse family of anion transporters, with members from eubacteria, plants, fungi, and mammals. They contain 10 to 14 transmembrane helices which form the catalytic core of the protein and a C-terminal extension, the STAS (Sulphate Transporter and AntiSigma factor antagonist) domain which plays a role in the function and regulation of the transport activity. The STAS 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.
Pssm-ID: 132913 [Multi-domain] Cd Length: 107 Bit Score: 64.19 E-value: 2.18e-12
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
663-733
1.15e-11
STAS domain; 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.
Pssm-ID: 426404 [Multi-domain] Cd Length: 106 Bit Score: 61.86 E-value: 1.15e-11
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
662-706
2.33e-05
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.
Pssm-ID: 132914 [Multi-domain] Cd Length: 99 Bit Score: 43.66 E-value: 2.33e-05
Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex ...
663-706
3.58e-03
Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex proteins RsbS and RsbR, regulators of the bacterial stress activated alternative sigma factor sigma-B by phosphorylation; The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain of proteins related to RsbS and RsbR which are part of the "stressosome" complex that plays an important role in the regulation of the bacterial stress activated alternative sigma factor sigma-B. During stress conditions RsbS and RsbR are phosphorylated which leads to the release of RsbT, an activator of of the RsbU phosphatase, which in turn activates RsbV which leads to the release and activation of sigma factor B. RsbS is a single domain protein (STAS domain), while RsbR-like proteins have a well-conserved C-terminal STATS domain and a variable N-terminal domain. The STAS domain is also found in the C- terminal region of sulphate transporters and anti-anti-sigma factors.
Pssm-ID: 132912 Cd Length: 109 Bit Score: 37.82 E-value: 3.58e-03
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.
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