logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: VBB84839.1

You are here: Home > Sequence: VBB84839.1

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 Podospora comata
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata
CAZyme ID VBB84839.1
CAZy Family GT2
CAZyme Description Putative Glycoside Hydrolase Family 55
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
800 86573.03 4.5228
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcomataTmat 13100 N/A 2652 10448
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 16 787 8.5e-257 0.9837837837837838

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
403800 Pectate_lyase_3 1.25e-88 41 265 1 213
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 8.89e-05 43 102 84 132
Polygalacturonase [Carbohydrate transport and metabolism].
215120 PLN02188 3.20e-04 43 97 38 83
polygalacturonase/glycoside hydrolase family protein
403800 Pectate_lyase_3 4.99e-04 388 502 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.
314993 End_N_terminal 0.003 49 66 1 18
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 1 800 1 800
0.0 1 800 1 761
0.0 1 800 1 761
0.0 7 788 8 782
0.0 15 759 15 760

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.23e-217 19 788 6 754
Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila],5M60_A Chain A, Beta-1,3-glucanase [Thermochaetoides thermophila]
7.49e-193 19 770 26 738
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]
3.26e-06 43 99 76 128
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
6.15e-219 11 785 40 782
Glucan 1,3-beta-glucosidase OS=Cochliobolus carbonum OX=5017 GN=EXG1 PE=1 SV=1
5.33e-185 17 787 41 873
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
2.76e-44 16 719 33 700
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 OTHER

Other SP_Sec_SPI CS Position
0.907854 0.092154

TMHMM  Annotations      help

There is no transmembrane helices in VBB84839.1.