Species | Stachybotrys chartarum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum | |||||||||||
CAZyme ID | KFA50871.1 | |||||||||||
CAZy Family | GH135 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH64 | 62 | 431 | 7e-86 | 0.989100817438692 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
185759 | GH64-GluB-like | 1.47e-154 | 62 | 431 | 1 | 369 | glycoside hydrolase family 64: beta-1,3-glucanase B (GluB)-like. This subfamily is represented by GluB, beta-1,3-glucanase B , from Lysobacter enzymogenes Strain N4-7 and related bacterial and ascomycete proteins. GluB is a member of the glycoside hydrolase family 64 (GH64) involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. GluB possesses the conserved Glu and Asp residues required to cleave substrate beta-1,3-glucans. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Based on the structure of laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis, which belongs to the same family as GluB but to a different subfamily, this cd is a two-domain model. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. |
406796 | Glyco_hydro_64 | 3.15e-150 | 60 | 430 | 1 | 370 | Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity. |
185755 | GH64-LPHase-like | 3.28e-72 | 71 | 428 | 12 | 350 | glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain. |
185753 | GH64-like | 6.29e-35 | 77 | 431 | 19 | 319 | glycosyl hydrolase 64 family. This family is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain, and in the Salinispora tropica CNB-440, coagulation factor 5/8 C-terminal domain (FA58C) protein, they are positioned C-terminal of two FA58C domains which are proposed to function as cell surface-attached, carbohydrate-binding domain. This FA58C-containing protein has an internal peptide deletion (of approx. 44 residues) in the LPHase domain II. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.15e-161 | 13 | 434 | 27 | 450 | |
1.47e-160 | 14 | 434 | 28 | 447 | |
3.28e-157 | 14 | 433 | 28 | 447 | |
1.37e-156 | 2 | 433 | 17 | 448 | |
1.33e-155 | 5 | 433 | 22 | 443 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.97e-27 | 84 | 407 | 32 | 344 | Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis],3GD9_A Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis] |
|
3.80e-07 | 74 | 431 | 164 | 443 | Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii] |
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2.06e-06 | 74 | 431 | 164 | 443 | Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose. [Paenibacillus barengoltzii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.31e-20 | 77 | 407 | 55 | 375 | Glucan endo-1,3-beta-glucosidase OS=Cellulosimicrobium cellulans OX=1710 PE=1 SV=1 |
|
1.67e-19 | 77 | 407 | 55 | 375 | Glucan endo-1,3-beta-glucosidase OS=Arthrobacter sp. (strain YCWD3) OX=79671 GN=glcI PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999672 | 0.000370 |
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