Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ...
33-250
3.19e-98
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
:
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 310.33 E-value: 3.19e-98
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-865
1.69e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
The actual alignment was detected with superfamily member NF038112:
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 49.27 E-value: 1.69e-05
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.
The actual alignment was detected with superfamily member cd04084:
Pssm-ID: 449372 Cd Length: 123 Bit Score: 45.31 E-value: 1.96e-05
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ...
33-250
3.19e-98
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 310.33 E-value: 3.19e-98
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
721-803
1.98e-13
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 66.75 E-value: 1.98e-13
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
723-804
3.72e-13
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 65.94 E-value: 3.72e-13
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
877-955
3.09e-07
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 49.46 E-value: 3.09e-07
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
723-811
1.19e-06
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 53.16 E-value: 1.19e-06
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-865
1.69e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 49.27 E-value: 1.69e-05
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
1045-1132
1.96e-05
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold.
Pssm-ID: 271150 Cd Length: 123 Bit Score: 45.31 E-value: 1.96e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-810
1.14e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 46.57 E-value: 1.14e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
671-825
3.11e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 45.07 E-value: 3.11e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-840
4.08e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 44.65 E-value: 4.08e-04
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA ...
33-250
3.19e-98
Trehalose utilization; This family consists of several bacterial ThuA-like proteins. ThuA appears to be involved in utilization of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium. ThuA is involved in the conversion of of disaccharides to their respective 3-keto derivatives.
Pssm-ID: 461867 [Multi-domain] Cd Length: 213 Bit Score: 310.33 E-value: 3.19e-98
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
721-803
1.98e-13
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 66.75 E-value: 1.98e-13
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
723-804
3.72e-13
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.
Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 65.94 E-value: 3.72e-13
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
877-955
3.09e-07
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 49.46 E-value: 3.09e-07
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
723-811
1.19e-06
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 53.16 E-value: 1.19e-06
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-865
1.69e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 49.27 E-value: 1.69e-05
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 ...
1045-1132
1.96e-05
Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains; This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold.
Pssm-ID: 271150 Cd Length: 123 Bit Score: 45.31 E-value: 1.96e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-810
1.14e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 46.57 E-value: 1.14e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
701-823
1.41e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 46.23 E-value: 1.41e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
745-841
2.84e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 45.46 E-value: 2.84e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
671-825
3.11e-04
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.
Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 45.07 E-value: 3.11e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
718-840
4.08e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 44.65 E-value: 4.08e-04
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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