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CAZyme Information: PWY86944.1

You are here: Home > Sequence: PWY86944.1

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 heteromorphus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
CAZyme ID PWY86944.1
CAZy Family GH71
CAZyme Description bacterial alpha-L-rhamnosidase domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
657 MSFL01000007|CGC4 71193.26 4.8938
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55 11436 1448321 306 11130
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.40:5

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 240 621 2.3e-70 0.7301587301587301

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
407469 Bac_rhamnosid6H 2.90e-08 238 510 27 302
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
273702 oligosac_amyl 8.47e-04 319 422 366 465
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 654 1 653
0.0 1 654 1 653
0.0 1 654 1 653
0.0 1 656 1 655
0.0 1 656 1 655

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.34e-09 245 557 237 541
Chain A, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]
4.03e-09 67 621 194 708
Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      help

PWY86944.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000378 0.999613 CS pos: 18-19. Pr: 0.9796

TMHMM  Annotations      help

There is no transmembrane helices in PWY86944.1.