glycoside hydrolase family 97 protein similar to Streptomyces bingchenggensis retaining alpha-galactosidase that catalyzes hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
298-557
1.03e-80
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.
The actual alignment was detected with superfamily member pfam10566:
Pssm-ID: 463149 Cd Length: 279 Bit Score: 259.10 E-value: 1.03e-80
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
29-293
1.78e-40
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: 148.48 E-value: 1.78e-40
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
560-662
5.38e-36
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: 130.65 E-value: 5.38e-36
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
298-557
1.03e-80
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: 259.10 E-value: 1.03e-80
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
29-293
1.78e-40
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: 148.48 E-value: 1.78e-40
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
560-662
5.38e-36
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: 130.65 E-value: 5.38e-36
Glycoside hydrolase 97; This domain is the catalytic region of the bacterial ...
298-557
1.03e-80
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: 259.10 E-value: 1.03e-80
Glycosyl-hydrolase 97 N-terminal; This N-terminal domain of glycosyl-hydrolase-97 contributes ...
29-293
1.78e-40
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: 148.48 E-value: 1.78e-40
Glycosyl-hydrolase 97 C-terminal, oligomerization; Glycosyl-hydrolase-97 is made up of three ...
560-662
5.38e-36
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: 130.65 E-value: 5.38e-36
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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