glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may be a member of glycosyl hydrolase families GH47, GH76, GH88, or GH127
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
57-337
4.77e-19
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.
The actual alignment was detected with superfamily member pfam07470:
Pssm-ID: 471159 Cd Length: 345 Bit Score: 87.43 E-value: 4.77e-19
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
57-337
4.77e-19
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
Pssm-ID: 429478 Cd Length: 345 Bit Score: 87.43 E-value: 4.77e-19
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
174-361
3.01e-04
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.
Pssm-ID: 238153 Cd Length: 384 Bit Score: 42.73 E-value: 3.01e-04
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
57-337
4.77e-19
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
Pssm-ID: 429478 Cd Length: 345 Bit Score: 87.43 E-value: 4.77e-19
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
174-361
3.01e-04
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.
Pssm-ID: 238153 Cd Length: 384 Bit Score: 42.73 E-value: 3.01e-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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Functional characterization of the conserved domain architecture found on the query.
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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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