logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: ASPACDRAFT_14258-t33_1-p1

You are here: Home > Sequence: ASPACDRAFT_14258-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 aculeatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus aculeatus
CAZyme ID ASPACDRAFT_14258-t33_1-p1
CAZy Family AA7
CAZyme Description glycoside hydrolase family 16 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
425 KV878985|CGC1 43623.61 4.0675
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AaculeatusATCC16872 11165 690307 322 10843
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39:3 3.2.1.-:1 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 63 298 5.2e-86 0.9868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
185690 GH16_fungal_Lam16A_glucanase 5.83e-153 23 319 1 293
fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).
185693 GH16_laminarinase_like 1.30e-14 93 274 66 215
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
185691 GH16_Strep_laminarinase_like 2.58e-08 120 211 106 181
Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
185694 GH16_CCF 1.18e-05 122 219 130 222
Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
185683 Glyco_hydrolase_16 2.71e-05 66 318 32 210
glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.99e-179 1 326 1 328
3.01e-178 1 326 1 328
3.01e-178 1 326 1 328
8.85e-161 5 326 8 335
1.01e-159 5 326 8 335

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.83e-120 23 318 2 297
Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'],5JVV_B Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila']
2.88e-81 24 318 2 295
The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_B The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_C The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_D The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila']
2.98e-81 24 318 3 296
The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_B The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_C The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_D The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDV_A The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_B The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_C The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_D The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila']
2.22e-80 24 318 1 294
The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_B The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_C The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_D The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila']
2.36e-80 24 318 3 296
The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDW_B The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDX_A The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'],3WDX_B The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila']

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.53e-180 1 326 1 328
Probable endo-1,3(4)-beta-glucanase An02g00850 OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=An02g00850 PE=3 SV=1
1.57e-161 5 326 8 335
Probable endo-1,3(4)-beta-glucanase AO090023000083 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=AO090023000083 PE=3 SV=1
1.79e-160 5 326 8 335
Probable endo-1,3(4)-beta-glucanase AFLA_105200 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=AFLA_105200 PE=3 SV=1
6.53e-154 2 325 3 334
Probable endo-1,3(4)-beta-glucanase ACLA_073210 OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=ACLA_073210 PE=3 SV=1
4.03e-150 2 326 3 334
Probable endo-1,3(4)-beta-glucanase AFUB_029980 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=AFUB_029980 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000234 0.999749 CS pos: 21-22. Pr: 0.9804

TMHMM  Annotations      help

There is no transmembrane helices in ASPACDRAFT_14258-t33_1-p1.