Species | Ascosphaera apis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis | |||||||||||
CAZyme ID | KZZ97822.1 | |||||||||||
CAZy Family | GT50 | |||||||||||
CAZyme Description | Beta-N-acetylhexosaminidase [Source:UniProtKB/TrEMBL;Acc:A0A162ISH2] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.52:13 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 2185 | 2500 | 2.7e-58 | 0.8160237388724035 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
406558 | DOCK_N | 4.61e-105 | 188 | 582 | 1 | 377 | DOCK N-terminus. This family is found near to the N-terminus of dedicator of cytokinesis (DOCK) proteins, between the variant SH3 domain (pfam07653) and the C2 domain (pfam14429). |
212566 | DHR2_DOCK | 1.67e-98 | 1421 | 1816 | 1 | 392 | Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins. DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42. |
119332 | GH20_HexA_HexB-like | 4.89e-95 | 2184 | 2528 | 48 | 348 | Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. |
395590 | Glyco_hydro_20 | 3.49e-79 | 2185 | 2500 | 49 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
212569 | DHR2_DOCK_B | 1.50e-50 | 1421 | 1814 | 1 | 386 | Dock Homology Region 2, a GEF domain, of Class B Dedicator of Cytokinesis proteins. DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate small GTPases by exchanging bound GDP for free GTP. They are divided into four classes (A-D) based on sequence similarity and domain architecture; class B includes Dock3 and 4. Dock3 is a specific GEF for Rac and it regulates N-cadherin dependent cell-cell adhesion, cell polarity, and neuronal morphology. It promotes axonal growth by stimulating actin polymerization and microtubule assembly. Dock4 activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. It plays a role in regulating dendritic growth and branching in hippocampal neurons, where it is highly expressed. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate. This alignment model represents the DHR-2 domain of class B DOCKs, which contains the catalytic GEF activity for Rac and/or Cdc42. Class B DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.10e-173 | 2078 | 2555 | 15 | 599 | |
1.10e-173 | 2078 | 2555 | 15 | 599 | |
1.10e-173 | 2078 | 2555 | 15 | 599 | |
3.89e-173 | 2078 | 2555 | 15 | 599 | |
3.89e-173 | 2078 | 2555 | 15 | 599 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.59e-159 | 2188 | 2555 | 132 | 498 | Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae],5OAR_D Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae [Aspergillus oryzae] |
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1.32e-93 | 203 | 1730 | 92 | 1562 | Chain A, Dedicator of cytokinesis protein 5 [Homo sapiens],7DPA_D Chain D, Dedicator of cytokinesis protein 5 [Homo sapiens] |
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1.27e-54 | 1145 | 1730 | 964 | 1536 | CryoEM structure of the binary DOCK2-ELMO1 complex [Homo sapiens],6TGB_D CryoEM structure of the binary DOCK2-ELMO1 complex [Homo sapiens],6TGC_A CryoEM structure of the ternary DOCK2-ELMO1-RAC1 complex [Homo sapiens],6TGC_D CryoEM structure of the ternary DOCK2-ELMO1-RAC1 complex [Homo sapiens] |
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1.05e-39 | 1407 | 1730 | 13 | 345 | Crystal structure of the DHR-2 domain of DOCK2 in complex with Rac1 (T17N mutant) [Homo sapiens],3B13_C Crystal structure of the DHR-2 domain of DOCK2 in complex with Rac1 (T17N mutant) [Homo sapiens] |
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1.16e-39 | 1407 | 1730 | 18 | 350 | STRUCTURE OF THE COMPLEX BETWEEN Dock2 AND Rac1. [Homo sapiens],2YIN_B STRUCTURE OF THE COMPLEX BETWEEN Dock2 AND Rac1. [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.91e-174 | 2078 | 2555 | 15 | 599 | Beta-hexosaminidase OS=Aspergillus oryzae OX=5062 GN=nagA PE=1 SV=1 |
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1.16e-159 | 2074 | 2555 | 12 | 602 | Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1 |
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2.73e-146 | 2059 | 2555 | 1 | 594 | Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1 |
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5.71e-140 | 2054 | 2548 | 2 | 607 | Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1 |
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7.00e-112 | 2185 | 2554 | 214 | 561 | Beta-hexosaminidase OS=Candida albicans OX=5476 GN=HEX1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.603702 | 0.396305 |
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