Species | Albugo candida | |||||||||||
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Lineage | Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida | |||||||||||
CAZyme ID | evm.model.AC2VRR_s00227g209-p1 | |||||||||||
CAZy Family | GT48 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.113:20 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH47 | 181 | 607 | 1.9e-129 | 0.9977578475336323 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396217 | Glyco_hydro_47 | 2.27e-134 | 181 | 607 | 1 | 453 | Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). |
240427 | PTZ00470 | 1.45e-91 | 168 | 607 | 66 | 518 | glycoside hydrolase family 47 protein; Provisional |
239047 | PA_GO-like | 7.55e-09 | 824 | 933 | 42 | 139 | PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. |
400321 | PRKCSH | 2.36e-07 | 30 | 104 | 3 | 72 | Glucosidase II beta subunit-like protein. The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain. |
396691 | PA | 8.18e-06 | 823 | 919 | 2 | 89 | PA domain. The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor and members of the RZF family. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 341 | 997 | 1 | 656 | |
6.11e-201 | 96 | 993 | 4 | 1021 | |
3.08e-193 | 7 | 942 | 10 | 902 | |
4.59e-191 | 30 | 934 | 48 | 918 | |
9.48e-107 | 178 | 640 | 45 | 513 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.48e-48 | 178 | 607 | 9 | 451 | Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens] |
|
2.82e-48 | 178 | 607 | 14 | 456 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens] |
|
2.94e-48 | 178 | 607 | 14 | 456 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens] |
|
1.21e-47 | 178 | 607 | 9 | 451 | Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens] |
|
1.33e-47 | 178 | 607 | 92 | 534 | Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.17e-104 | 142 | 615 | 3 | 482 | Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1 |
|
1.80e-97 | 152 | 607 | 12 | 478 | Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1 |
|
4.02e-91 | 178 | 604 | 39 | 479 | ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2 |
|
7.55e-91 | 178 | 604 | 39 | 479 | ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1 |
|
8.18e-90 | 144 | 611 | 7 | 481 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000033 | 0.000013 |
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