glycoside hydrolase family 3 protein similar to Schizosaccharomyces pombe beta-glucosidase that catalyzes the hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
483-621
6.21e-30
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.
:
Pssm-ID: 400161 [Multi-domain] Cd Length: 141 Bit Score: 115.54 E-value: 6.21e-30
Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be ...
388-779
1.02e-52
Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.
Pssm-ID: 396478 [Multi-domain] Cd Length: 216 Bit Score: 183.29 E-value: 1.02e-52
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
483-621
6.21e-30
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.
Pssm-ID: 400161 [Multi-domain] Cd Length: 141 Bit Score: 115.54 E-value: 6.21e-30
Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be ...
388-779
1.02e-52
Glycosyl hydrolase family 3 C-terminal domain; This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.
Pssm-ID: 396478 [Multi-domain] Cd Length: 216 Bit Score: 183.29 E-value: 1.02e-52
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
483-621
6.21e-30
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.
Pssm-ID: 400161 [Multi-domain] Cd Length: 141 Bit Score: 115.54 E-value: 6.21e-30
Fibronectin type III-like domain; This domain has a fibronectin type III-like structure. It is ...
817-887
3.35e-21
Fibronectin type III-like domain; This domain has a fibronectin type III-like structure. It is often found in association with pfam00933 and pfam01915. Its function is unknown.
Pssm-ID: 433860 [Multi-domain] Cd Length: 70 Bit Score: 87.91 E-value: 3.35e-21
GLEYA domain; The GLEYA domain is related to lectin-like binding domains found in the S. ...
537-601
5.20e-03
GLEYA domain; The GLEYA domain is related to lectin-like binding domains found in the S. cerevisiae Flo proteins and the C. glabrata Epa proteins. It is a carbohydrate-binding domain that is found in fungal adhesins (also referred to as agglutinins or flocculins). Adhesins with a GLEYA domain possess a typical N-terminal signal peptide and a domain of conserved sequence repeats, but lack glycosylphosphatidylinositol (GPI) anchor attachment signals. They contain a conserved motif G(M/L)(E/A/N/Q)YA, hence the name GLEYA. Based on sequence homology, it is suggested that the GLEYA domain would predominantly contain beta sheets. The GLEYA domain is also found in S. pombe protein Swiss:Q92344, thought to be a kinetochore portein (Sim4 complex subunit), however no direct evidence for kinetochore association has been found. Furthermore, a global protein localization study in S. pombe identified it as a secreted protein localized to the Golgi complex.
Pssm-ID: 463135 Cd Length: 91 Bit Score: 37.14 E-value: 5.20e-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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