lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.
Pssm-ID: 410624 [Multi-domain] Cd Length: 180 Bit Score: 231.04 E-value: 4.90e-74
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
34-199
3.08e-62
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.
Pssm-ID: 460793 [Multi-domain] Cd Length: 184 Bit Score: 200.69 E-value: 3.08e-62
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.
Pssm-ID: 410624 [Multi-domain] Cd Length: 180 Bit Score: 231.04 E-value: 4.90e-74
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
34-199
3.08e-62
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.
Pssm-ID: 460793 [Multi-domain] Cd Length: 184 Bit Score: 200.69 E-value: 3.08e-62
N-acetylglucosamine binding protein domain 2; This domain can be found in N-acetylglucosamine ...
211-309
1.25e-36
N-acetylglucosamine binding protein domain 2; This domain can be found in N-acetylglucosamine binding protein (GbpA) from Vibrio cholerae, a bacterial pathogen that colonizes the chitinous exoskeleton of zooplankton as well as the human gastrointestinal tract. GbpA binds to GlcNAc oligosaccharides. Structural comparison show that there are distant structural similarities between domain 2 of GbpA and the beta-domain of the flagellin protein p5. It is suggested that this domain interacts with the bacterial surface, and functions to project an alginate binding domain of the protein from the cell surface.
Pssm-ID: 465759 Cd Length: 102 Bit Score: 130.54 E-value: 1.25e-36
lytic polysaccharide monooxygenase auxiliary activity protein; Many proteins in this ...
56-198
1.30e-10
lytic polysaccharide monooxygenase auxiliary activity protein; Many proteins in this superfamily are copper-dependent lytic polysaccharide monooxygenases (LPMOs) and include lytic polysaccharide monooxygenase auxiliary activity families 9 (AA9) and 10 (AA10). The substrate-binding surface of this family is a flat beta-sandwich fold.
Pssm-ID: 410621 Cd Length: 136 Bit Score: 59.17 E-value: 1.30e-10
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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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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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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(labeled illustration) Four types of hits can be shown, as available,
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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