Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein ...
77-441
0e+00
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins; The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily.
The actual alignment was detected with superfamily member cd11663:
Pssm-ID: 483946 Cd Length: 363 Bit Score: 587.69 E-value: 0e+00
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
974-1320
1.86e-28
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: 125.15 E-value: 1.86e-28
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
876-949
3.05e-14
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.
The actual alignment was detected with superfamily member smart01066:
Pssm-ID: 474061 [Multi-domain] Cd Length: 83 Bit Score: 69.31 E-value: 3.05e-14
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
1348-1416
4.84e-05
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
The actual alignment was detected with superfamily member cd12956:
Pssm-ID: 475118 Cd Length: 93 Bit Score: 43.50 E-value: 4.84e-05
putative catalytic domain of glycoside hydrolase family 119 (GH119); The prokaryotic subgroup ...
77-441
0e+00
putative catalytic domain of glycoside hydrolase family 119 (GH119); The prokaryotic subgroup is represented by IgtZ, an alpha-amylase from a Bacillus circulans strain. The GH119 family is related to GH57, a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
Pssm-ID: 212128 Cd Length: 363 Bit Score: 587.69 E-value: 0e+00
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
974-1320
1.86e-28
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: 125.15 E-value: 1.86e-28
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
785-1057
5.34e-10
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: 64.29 E-value: 5.34e-10
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
1145-1231
6.91e-07
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240566 Cd Length: 91 Bit Score: 48.44 E-value: 6.91e-07
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
831-1115
2.66e-06
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 52.31 E-value: 2.66e-06
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1240-1315
1.27e-05
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: 44.75 E-value: 1.27e-05
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
1348-1416
4.84e-05
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240562 Cd Length: 93 Bit Score: 43.50 E-value: 4.84e-05
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
985-1207
6.41e-03
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 41.14 E-value: 6.41e-03
putative catalytic domain of glycoside hydrolase family 119 (GH119); The prokaryotic subgroup ...
77-441
0e+00
putative catalytic domain of glycoside hydrolase family 119 (GH119); The prokaryotic subgroup is represented by IgtZ, an alpha-amylase from a Bacillus circulans strain. The GH119 family is related to GH57, a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
Pssm-ID: 212128 Cd Length: 363 Bit Score: 587.69 E-value: 0e+00
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57; Glycoside ...
83-425
4.10e-44
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57; Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
Pssm-ID: 212096 [Multi-domain] Cd Length: 313 Bit Score: 162.99 E-value: 4.10e-44
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
974-1320
1.86e-28
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: 125.15 E-value: 1.86e-28
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
785-1057
5.34e-10
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: 64.29 E-value: 5.34e-10
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
1145-1231
6.91e-07
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240566 Cd Length: 91 Bit Score: 48.44 E-value: 6.91e-07
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
831-1115
2.66e-06
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 52.31 E-value: 2.66e-06
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1240-1315
1.27e-05
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: 44.75 E-value: 1.27e-05
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
1348-1416
4.84e-05
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240562 Cd Length: 93 Bit Score: 43.50 E-value: 4.84e-05
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
1250-1316
2.67e-04
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: 40.94 E-value: 2.67e-04
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
980-1052
7.78e-04
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: 39.79 E-value: 7.78e-04
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
1149-1231
1.04e-03
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240562 Cd Length: 93 Bit Score: 39.65 E-value: 1.04e-03
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
978-1052
1.16e-03
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: 38.97 E-value: 1.16e-03
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
1330-1415
1.27e-03
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.
Pssm-ID: 240566 Cd Length: 91 Bit Score: 39.20 E-value: 1.27e-03
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan ...
1253-1320
2.15e-03
Dystroglycan-type cadherin-like domains; Cadherin-homologous domains present in metazoan dystroglycans and alpha/epsilon sarcoglycans, yeast Axl2p and in a very large protein from magnetotactic bacteria. Likely to bind calcium ions.
Pssm-ID: 214795 [Multi-domain] Cd Length: 97 Bit Score: 38.86 E-value: 2.15e-03
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
1059-1124
3.93e-03
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: 37.82 E-value: 3.93e-03
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
985-1207
6.41e-03
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.
Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 41.14 E-value: 6.41e-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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