glycoside hydrolase family 99 protein similar to glycoprotein endo-alpha-1,2-mannosidase that catalyzes the hydrolysis of the terminal alpha-D-glucosyl- (1->3)-D-mannosyl unit from the GlcMan(9)(GlcNAc)(2) oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
105-446
0e+00
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.
:
Pssm-ID: 211415 Cd Length: 338 Bit Score: 576.57 E-value: 0e+00
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
105-446
0e+00
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.
Pssm-ID: 211415 Cd Length: 338 Bit Score: 576.57 E-value: 0e+00
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
105-450
0e+00
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.
Pssm-ID: 435273 Cd Length: 341 Bit Score: 511.36 E-value: 0e+00
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
105-446
0e+00
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.
Pssm-ID: 211415 Cd Length: 338 Bit Score: 576.57 E-value: 0e+00
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
105-450
0e+00
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.
Pssm-ID: 435273 Cd Length: 341 Bit Score: 511.36 E-value: 0e+00
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
163-445
1.98e-45
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.
Pssm-ID: 211414 Cd Length: 284 Bit Score: 159.58 E-value: 1.98e-45
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
107-414
5.97e-18
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.
Pssm-ID: 211419 Cd Length: 313 Bit Score: 84.38 E-value: 5.97e-18
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
101-414
3.64e-15
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.
Pssm-ID: 211416 Cd Length: 376 Bit Score: 76.61 E-value: 3.64e-15
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
337-441
5.24e-04
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism. The domain may co-occur with other domains involved in the binding/processing of glycans.
Pssm-ID: 211417 Cd Length: 378 Bit Score: 42.24 E-value: 5.24e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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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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