Species | Aspergillus sydowii | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii | |||||||||||
CAZyme ID | ASPSYDRAFT_194404-t33_1-p1 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA3 | 728 | 1287 | 5.3e-167 | 0.9947183098591549 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
235000 | PRK02106 | 4.27e-89 | 728 | 1286 | 4 | 531 | choline dehydrogenase; Validated |
225186 | BetA | 8.35e-81 | 729 | 1295 | 7 | 542 | Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]. |
239322 | DsbA_FrnE | 1.20e-47 | 6 | 214 | 1 | 200 | DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins. |
271038 | STKc_SRPK | 3.06e-43 | 325 | 709 | 1 | 320 | Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK 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. |
270688 | STKc_CMGC | 7.36e-41 | 337 | 709 | 1 | 249 | Catalytic domain of CMGC family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1302 | 1 | 1303 | |
0.0 | 716 | 1302 | 4 | 600 | |
9.22e-238 | 729 | 1286 | 41 | 611 | |
4.31e-233 | 729 | 1287 | 42 | 613 | |
1.87e-227 | 729 | 1274 | 42 | 600 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.11e-48 | 729 | 1293 | 5 | 571 | Crystal structure of Aspergillus flavus FAD glucose dehydrogenase [Aspergillus flavus NRRL3357],4YNU_A Crystal structure of Aspergillus flavus FADGDH in complex with D-glucono-1,5-lactone [Aspergillus flavus NRRL3357] |
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1.40e-47 | 724 | 1297 | 8 | 536 | Crystal structure of choline oxidase reveals insights into the catalytic mechanism [Arthrobacter globiformis],2JBV_B Crystal structure of choline oxidase reveals insights into the catalytic mechanism [Arthrobacter globiformis],4MJW_A Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine [Arthrobacter globiformis],4MJW_B Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine [Arthrobacter globiformis] |
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1.40e-47 | 724 | 1297 | 8 | 536 | Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_B Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_C Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_D Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_E Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_F Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_G Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_H Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis] |
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2.55e-47 | 724 | 1297 | 8 | 536 | Chain A, Choline oxidase [Arthrobacter globiformis],3LJP_B Chain B, Choline oxidase [Arthrobacter globiformis] |
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1.91e-46 | 730 | 1286 | 7 | 569 | Crystal structure analysis of formate oxidase [Aspergillus oryzae RIB40],3Q9T_B Crystal structure analysis of formate oxidase [Aspergillus oryzae RIB40],3Q9T_C Crystal structure analysis of formate oxidase [Aspergillus oryzae RIB40] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.06e-161 | 728 | 1286 | 49 | 624 | Patulin synthase OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patE PE=1 SV=1 |
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2.22e-160 | 728 | 1286 | 50 | 624 | Patulin synthase OS=Penicillium expansum OX=27334 GN=patE PE=1 SV=1 |
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3.16e-143 | 730 | 1290 | 36 | 611 | Oxidoreductase cicC OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cicC PE=1 SV=1 |
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6.44e-142 | 729 | 1284 | 40 | 605 | Dehydrogenase pkfF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=pkfF PE=2 SV=1 |
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4.38e-129 | 715 | 1287 | 34 | 594 | Cyclase atC OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=atC PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000063 | 0.000001 |
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