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CAZyme Information: KAG4304413.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Pneumocystis oryctolagi | |||||||||||
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| Lineage | Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis oryctolagi | |||||||||||
| CAZyme ID | KAG4304413.1 | |||||||||||
| CAZy Family | GH47 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT2 | 576 | 755 | 2.3e-27 | 0.9647058823529412 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 133031 | DPG_synthase | 6.15e-91 | 577 | 799 | 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. |
| 240336 | PTZ00260 | 3.69e-90 | 511 | 825 | 1 | 321 | dolichyl-phosphate beta-glucosyltransferase; Provisional |
| 270981 | STKc_AMPK_alpha | 1.23e-65 | 1 | 105 | 152 | 256 | Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| 270905 | STKc_AMPK-like | 1.19e-48 | 1 | 104 | 149 | 252 | Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. |
| 133022 | DPM_DPG-synthase_like | 1.32e-48 | 577 | 778 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1 | 830 | 176 | 978 | |
| 7.14e-89 | 526 | 825 | 16 | 313 | |
| 7.14e-89 | 526 | 825 | 16 | 313 | |
| 4.95e-85 | 518 | 825 | 10 | 312 | |
| 4.95e-85 | 518 | 825 | 10 | 312 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.29e-68 | 1 | 196 | 158 | 324 | crystal structure of pombe AMPK KDAID fragment [Schizosaccharomyces pombe],3H4J_B crystal structure of pombe AMPK KDAID fragment [Schizosaccharomyces pombe] |
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| 7.74e-55 | 1 | 362 | 164 | 430 | STRUCTURE OF FULL LENGTH HUMAN AMPK (NON-PHOSPHORYLATED AT T-LOOP) IN COMPLEX WITH A SMALL MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE (991) [Homo sapiens],5ISO_C STRUCTURE OF FULL LENGTH HUMAN AMPK (NON-PHOSPHORYLATED AT T-LOOP) IN COMPLEX WITH A SMALL MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE (991) [Homo sapiens] |
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| 7.22e-54 | 1 | 362 | 183 | 449 | Structure of full length human AMPK in complex with a small molecule activator, a benzimidazole derivative (991) [Homo sapiens],4CFE_C Structure of full length human AMPK in complex with a small molecule activator, a benzimidazole derivative (991) [Homo sapiens],4CFF_A Structure of full length human AMPK in complex with a small molecule activator, a thienopyridone derivative (A-769662) [Homo sapiens],4CFF_C Structure of full length human AMPK in complex with a small molecule activator, a thienopyridone derivative (A-769662) [Homo sapiens] |
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| 8.84e-54 | 1 | 362 | 177 | 443 | Novel binding site for allosteric activation of AMPK [Homo sapiens],4ZHX_C Novel binding site for allosteric activation of AMPK [Homo sapiens],6B1U_A Structure of full-length human AMPK (a2b1g1) in complex with a small molecule activator SC4 [Homo sapiens],6B1U_C Structure of full-length human AMPK (a2b1g1) in complex with a small molecule activator SC4 [Homo sapiens],6B2E_A Structure of full length human AMPK (a2b2g1) in complex with a small molecule activator SC4. [Homo sapiens] |
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| 1.50e-53 | 1 | 362 | 178 | 438 | X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid) [Homo sapiens],5EZV_C X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid) [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.27e-89 | 526 | 825 | 16 | 313 | Dolichyl-phosphate beta-glucosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg5 PE=3 SV=1 |
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| 1.35e-81 | 541 | 830 | 38 | 333 | Dolichyl-phosphate beta-glucosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG5 PE=1 SV=1 |
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| 8.35e-81 | 1 | 461 | 181 | 555 | SNF1-like protein kinase ssp2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ssp2 PE=1 SV=1 |
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| 3.85e-80 | 1 | 459 | 186 | 586 | Carbon catabolite-derepressing protein kinase OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=SNF1 PE=3 SV=2 |
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| 6.24e-79 | 1 | 459 | 202 | 607 | Carbon catabolite-derepressing protein kinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SNF1 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.999783 | 0.000239 |