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CAZyme Information: ASPGLDRAFT_45840-t33_1-p1

You are here: Home > Sequence: ASPGLDRAFT_45840-t33_1-p1

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 Aspergillus glaucus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus
CAZyme ID ASPGLDRAFT_45840-t33_1-p1
CAZy Family GH65
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
579 64466.23 5.8469
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AglaucusCBS516.65 11429 1160497 175 11254
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ASPGLDRAFT_45840-t33_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA3 8 573 1.7e-147 0.9947183098591549

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
225186 BetA 4.79e-86 8 575 8 538
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
235000 PRK02106 3.39e-80 8 569 6 530
choline dehydrogenase; Validated
398739 GMC_oxred_C 1.54e-40 427 566 1 143
GMC oxidoreductase. This domain found associated with pfam00732.
366272 GMC_oxred_N 2.07e-21 87 309 23 217
GMC oxidoreductase. This family of proteins bind FAD as a cofactor.
215420 PLN02785 1.77e-18 8 563 56 569
Protein HOTHEAD

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 579 1 579
0.0 1 578 1 578
0.0 1 578 1 578
0.0 1 578 1 578
0.0 1 578 1 571

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 4 578 3 577
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]
0.0 4 578 3 577
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]
0.0 4 578 3 577
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]
1.25e-67 8 573 2 564
Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid [Pleurotus eryngii]
6.72e-67 8 573 3 565
Crystal structure of aryl-alcohol-oxidase from Pleurotus eryingii [Pleurotus eryngii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.31e-59 8 570 7 533
4-pyridoxate dehydrogenase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=padh1 PE=1 SV=1
2.34e-54 8 572 14 528
Choline oxidase OS=Arthrobacter globiformis OX=1665 GN=codA PE=1 SV=1
1.62e-53 8 570 41 595
Pyranose dehydrogenase 3 OS=Leucoagaricus meleagris OX=201219 GN=pdh3 PE=2 SV=1
3.74e-52 8 571 36 612
Dehydrogenase str4 OS=Strobilurus tenacellus OX=41251 GN=str4 PE=1 SV=1
7.44e-52 4 570 43 615
GMC oxidoreductase family protein Mala s 12.0101 OS=Malassezia sympodialis OX=76777 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000030 0.000005

TMHMM  Annotations      help

There is no transmembrane helices in ASPGLDRAFT_45840-t33_1-p1.