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CAZyme Information: EAW16568.1

You are here: Home > Sequence: EAW16568.1

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 fischeri
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
CAZyme ID EAW16568.1
CAZy Family AA7
CAZyme Description exo-beta-1,3-glucanase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
804 84094.43 4.8293
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfischeriNRRL181 10668 331117 278 10390
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.58:16

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH55 61 803 9.9e-283 0.9918918918918919

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
403800 Pectate_lyase_3 4.64e-93 92 315 1 212
Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
403800 Pectate_lyase_3 5.34e-11 441 554 1 122
Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
227721 Pgu1 5.48e-04 434 489 75 130
Polygalacturonase [Carbohydrate transport and metabolism].
227721 Pgu1 0.002 94 222 84 254
Polygalacturonase [Carbohydrate transport and metabolism].
314993 End_N_terminal 0.002 100 118 1 19
N terminal extension of bacteriophage endosialidase. This domain family is found in bacteria and viruses, and is approximately 70 amino acids in length. This domain is found in the bacteriophage protein endosialidase. The two N-terminal domains (this domain and the beta propeller) assemble in the compact 'cap' whereas the C-terminal domain forms an extended tail-like structure. The very N-terminal part of the 'cap' region (residues 246 to 312) holds the only alpha-helix of the protein and is presumably the residual part of the deleted N-terminal head-binding domain. The endosialidase protein complexes to form homotrimeric molecules.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 66 803 76 816
0.0 66 803 75 815
0.0 66 804 43 782
0.0 42 803 43 805
0.0 64 802 46 786

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.44e-216 66 803 24 756
Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQN_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_A Chain A, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium],3EQO_B Chain B, Glucan 1,3-beta-glucosidase [Phanerodontia chrysosporium]
2.74e-208 69 802 6 753
Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
1.44e-06 94 171 76 150
Chain A, Putative pectin lyase [Geobacillus virus E2],7CHU_B Chain B, Putative pectin lyase [Geobacillus virus E2],7CHU_C Chain C, Putative pectin lyase [Geobacillus virus E2]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.33e-287 69 801 48 783
Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
5.15e-202 68 802 42 873
Probable glucan endo-1,3-beta-glucosidase ARB_02077 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02077 PE=1 SV=1
3.29e-61 134 778 97 732
Glucan endo-1,3-beta-glucosidase BGN13.1 OS=Trichoderma harzianum OX=5544 GN=bgn13.1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001485 0.998460 CS pos: 18-19. Pr: 0.9559

TMHMM  Annotations      help

There is no transmembrane helices in EAW16568.1.