glycoside hydrolase family 97 protein such as Bacteroides thetaiotaomicron glucan 1,4-alpha-glucosidase SusB and retaining alpha-galactosidase, which hydrolyze terminal, non-reducing (1->4)-linked alpha-D-glucose and alpha-D-galactose, respectively
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
265-525
1.12e-128
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
:
Pssm-ID: 463149 Cd Length: 279 Bit Score: 379.67 E-value: 1.12e-128
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
3-260
5.96e-60
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
:
Pssm-ID: 464192 Cd Length: 234 Bit Score: 200.10 E-value: 5.96e-60
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
528-626
3.56e-44
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
:
Pssm-ID: 464193 Cd Length: 97 Bit Score: 152.61 E-value: 3.56e-44
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
265-525
1.12e-128
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
Pssm-ID: 463149 Cd Length: 279 Bit Score: 379.67 E-value: 1.12e-128
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
3-260
5.96e-60
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
Pssm-ID: 464192 Cd Length: 234 Bit Score: 200.10 E-value: 5.96e-60
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
528-626
3.56e-44
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
Pssm-ID: 464193 Cd Length: 97 Bit Score: 152.61 E-value: 3.56e-44
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
278-404
2.49e-05
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
Pssm-ID: 269891 [Multi-domain] Cd Length: 253 Bit Score: 46.08 E-value: 2.49e-05
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
265-525
1.12e-128
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
Pssm-ID: 463149 Cd Length: 279 Bit Score: 379.67 E-value: 1.12e-128
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
3-260
5.96e-60
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
Pssm-ID: 464192 Cd Length: 234 Bit Score: 200.10 E-value: 5.96e-60
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
528-626
3.56e-44
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
Pssm-ID: 464193 Cd Length: 97 Bit Score: 152.61 E-value: 3.56e-44
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
278-404
2.49e-05
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
Pssm-ID: 269891 [Multi-domain] Cd Length: 253 Bit Score: 46.08 E-value: 2.49e-05
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
304-509
1.45e-03
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
Pssm-ID: 269892 [Multi-domain] Cd Length: 299 Bit Score: 41.06 E-value: 1.45e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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