Species | Aspergillus cristatus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus cristatus | |||||||||||
CAZyme ID | ODM14866.1 | |||||||||||
CAZy Family | AA3 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA3 | 836 | 1391 | 4.1e-141 | 0.9823943661971831 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
235000 | PRK02106 | 1.12e-78 | 836 | 1389 | 13 | 532 | choline dehydrogenase; Validated |
225186 | BetA | 2.26e-78 | 836 | 1393 | 15 | 538 | Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]. |
260008 | Rnase_HI_RT_non_LTR | 4.38e-39 | 705 | 836 | 1 | 131 | non-LTR RNase HI domain of reverse transcriptases. Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. |
398739 | GMC_oxred_C | 1.95e-38 | 1250 | 1383 | 5 | 142 | GMC oxidoreductase. This domain found associated with pfam00732. |
238827 | RT_nLTR_like | 3.17e-36 | 333 | 546 | 2 | 214 | RT_nLTR: Non-LTR (long terminal repeat) retrotransposon and non-LTR retrovirus reverse transcriptase (RT). This subfamily contains both non-LTR retrotransposons and non-LTR retrovirus RTs. RTs catalyze the conversion of single-stranded RNA into double-stranded DNA for integration into host chromosomes. RT is a multifunctional enzyme with RNA-directed DNA polymerase, DNA directed DNA polymerase and ribonuclease hybrid (RNase H) activities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 835 | 1396 | 10 | 571 | |
5.56e-276 | 837 | 1396 | 19 | 579 | |
3.55e-271 | 837 | 1396 | 17 | 578 | |
3.55e-271 | 837 | 1396 | 17 | 578 | |
6.58e-271 | 837 | 1396 | 17 | 577 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.49e-235 | 837 | 1396 | 15 | 577 | 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] |
|
4.19e-235 | 837 | 1396 | 15 | 577 | Effect of mutation (R554K) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40],5ZU3_B Effect of mutation (R554K) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40],5ZU3_C Effect of mutation (R554K) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40] |
|
1.18e-234 | 837 | 1396 | 15 | 577 | Effect of mutation (R554A) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40],5ZU2_B Effect of mutation (R554A) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40],5ZU2_C Effect of mutation (R554A) on FAD modification in Aspergillus oryzae RIB40formate oxidase [Aspergillus oryzae RIB40] |
|
6.18e-64 | 836 | 1391 | 9 | 564 | Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid [Pleurotus eryngii] |
|
2.86e-63 | 836 | 1391 | 10 | 565 | Crystal structure of aryl-alcohol-oxidase from Pleurotus eryingii [Pleurotus eryngii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.36e-56 | 836 | 1388 | 14 | 533 | 4-pyridoxate dehydrogenase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=padh1 PE=1 SV=1 |
|
3.10e-55 | 836 | 1389 | 13 | 533 | Oxygen-dependent choline dehydrogenase OS=Burkholderia cenocepacia (strain HI2424) OX=331272 GN=betA PE=3 SV=1 |
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3.10e-55 | 836 | 1389 | 13 | 533 | Oxygen-dependent choline dehydrogenase OS=Burkholderia cenocepacia (strain AU 1054) OX=331271 GN=betA PE=3 SV=1 |
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3.10e-55 | 836 | 1389 | 13 | 533 | Oxygen-dependent choline dehydrogenase OS=Burkholderia cenocepacia (strain MC0-3) OX=406425 GN=betA PE=3 SV=1 |
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4.18e-55 | 836 | 1389 | 13 | 533 | Oxygen-dependent choline dehydrogenase OS=Burkholderia ambifaria (strain MC40-6) OX=398577 GN=betA PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000040 | 0.000000 |
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