Species | Albugo laibachii | |||||||||||
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Lineage | Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii | |||||||||||
CAZyme ID | ALNC14_006910:RNA-p1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | proline iminopeptidase putative | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 99 | 272 | 5.2e-26 | 0.9411764705882353 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
130316 | pro_imino_pep_1 | 1.08e-159 | 447 | 752 | 1 | 305 | proline iminopeptidase, Neisseria-type subfamily. This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members. |
240336 | PTZ00260 | 4.88e-105 | 21 | 351 | 6 | 326 | dolichyl-phosphate beta-glucosyltransferase; Provisional |
133031 | DPG_synthase | 1.39e-97 | 100 | 320 | 1 | 211 | DPG_synthase is involved in protein N-linked glycosylation. UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. |
133022 | DPM_DPG-synthase_like | 2.23e-51 | 100 | 299 | 1 | 185 | DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily. |
395444 | Abhydrolase_1 | 2.32e-33 | 474 | 740 | 1 | 244 | alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 762 | 1 | 762 | |
1.81e-76 | 85 | 349 | 54 | 317 | |
9.68e-76 | 97 | 350 | 66 | 319 | |
1.43e-74 | 97 | 346 | 44 | 293 | |
1.45e-74 | 97 | 350 | 66 | 319 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.25e-127 | 443 | 752 | 4 | 312 | Proline Iminopeptidase From Xanthomonas Campestris Pv. Citri [Xanthomonas citri],1AZW_B Proline Iminopeptidase From Xanthomonas Campestris Pv. Citri [Xanthomonas citri] |
|
4.49e-116 | 443 | 752 | 7 | 314 | Crystal Structure Analysis Of The Prolyl Aminopeptidase From Serratia Marcescens [Serratia marcescens],1WM1_A Crystal Structure of Prolyl Aminopeptidase, Complex with Pro-TBODA [Serratia marcescens],1X2B_A The crystal structure of prolyl aminopeptidase complexed with Sar-TBODA [Serratia marcescens],1X2E_A The crystal structure of prolyl aminopeptidase complexed with Ala-TBODA [Serratia marcescens] |
|
4.78e-107 | 443 | 752 | 40 | 351 | Proline iminopeptidase from Psychrophilic yeast glaciozyma antarctica [Glaciozyma antarctica],5YHP_B Proline iminopeptidase from Psychrophilic yeast glaciozyma antarctica [Glaciozyma antarctica] |
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5.36e-10 | 91 | 280 | 21 | 192 | Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa] |
|
5.36e-10 | 91 | 280 | 21 | 192 | Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.17e-130 | 430 | 754 | 48 | 377 | Proline iminopeptidase OS=Arabidopsis thaliana OX=3702 GN=PIP PE=2 SV=3 |
|
4.74e-126 | 442 | 758 | 3 | 318 | Probable proline iminopeptidase OS=Leptolyngbya boryana OX=1184 GN=pip PE=3 SV=1 |
|
1.59e-124 | 443 | 752 | 4 | 312 | Proline iminopeptidase OS=Xylella fastidiosa (strain 9a5c) OX=160492 GN=pip PE=3 SV=1 |
|
6.28e-124 | 443 | 752 | 4 | 312 | Proline iminopeptidase OS=Xylella fastidiosa (strain Temecula1 / ATCC 700964) OX=183190 GN=pip PE=3 SV=1 |
|
4.33e-121 | 443 | 752 | 4 | 312 | Proline iminopeptidase OS=Xanthomonas citri OX=346 GN=pip PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000089 | 0.000001 |
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