Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
1-201
1.68e-43
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: 144.06 E-value: 1.68e-43
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
1-201
1.68e-43
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: 144.06 E-value: 1.68e-43
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: 138.59 E-value: 1.69e-41
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
1-201
1.68e-43
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: 144.06 E-value: 1.68e-43
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: 138.59 E-value: 1.69e-41
fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that ...
1-203
1.52e-09
fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that resembles the lytic polysaccharide monooxygenases of chitinovorous bacteria and may function to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. Thus, it is a component of the virus occlusion bodies (which are large proteinaceous polyhedra) that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.
Pssm-ID: 410625 Cd Length: 227 Bit Score: 55.80 E-value: 1.52e-09
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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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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specific hits meet or exceed a domain-specific e-value threshold
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