Species | Mucor circinelloides | |||||||||||
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Lineage | Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides | |||||||||||
CAZyme ID | HMPREF1544_09903-t46_1-p1 | |||||||||||
CAZy Family | GT31 | |||||||||||
CAZyme Description | ER degradation enhancer, mannosidase alpha-like 1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH47 | 1 | 435 | 3.1e-153 | 0.9932735426008968 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396217 | Glyco_hydro_47 | 2.10e-163 | 1 | 435 | 1 | 451 | 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 | 2.66e-77 | 1 | 440 | 79 | 521 | glycoside hydrolase family 47 protein; Provisional |
239041 | PA_EDEM3_like | 4.18e-12 | 657 | 760 | 5 | 121 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It 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. |
238300 | PA | 1.17e-11 | 680 | 755 | 39 | 115 | PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It 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. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2. |
239044 | PA_hSPPL_like | 1.70e-10 | 687 | 750 | 44 | 106 | PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.83e-278 | 1 | 569 | 1 | 559 | |
7.47e-172 | 1 | 437 | 77 | 526 | |
1.09e-171 | 1 | 441 | 103 | 556 | |
1.90e-171 | 1 | 440 | 19 | 471 | |
7.71e-171 | 2 | 439 | 1 | 451 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.46e-51 | 2 | 444 | 21 | 442 | Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 [Caulobacter sp. K31],4AYP_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with thiomannobioside [Caulobacter sp. K31],4AYQ_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole [Caulobacter sp. K31],4AYR_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin [Caulobacter sp. K31],5MEH_A Crystal structure of alpha-1,2-mannosidase from Caulobacter K31 strain in complex with 1-deoxymannojirimycin [Caulobacter sp. K31],5NE5_A Crystal structure of family 47 alpha-1,2-mannosidase from Caulobacter K31 strain in complex with kifunensine [Caulobacter sp. K31] |
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5.22e-50 | 1 | 435 | 12 | 449 | Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens] |
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5.94e-50 | 1 | 435 | 17 | 454 | Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens] |
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6.20e-50 | 1 | 435 | 17 | 454 | 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] |
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2.68e-49 | 1 | 435 | 12 | 449 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.38e-170 | 1 | 440 | 132 | 584 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1 |
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6.46e-170 | 1 | 437 | 137 | 586 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1 |
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3.81e-150 | 1 | 520 | 42 | 547 | ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2 |
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2.18e-129 | 1 | 478 | 44 | 532 | Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1 |
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2.77e-126 | 1 | 437 | 45 | 484 | ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000056 | 0.000000 |
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