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CAZyme Information: EPrPVT00000017371-p1

You are here: Home > Sequence: EPrPVT00000017371-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 Phytopythium vexans
Lineage Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
CAZyme ID EPrPVT00000017371-p1
CAZy Family GH17
CAZyme Description Endo-beta-1,6-galactanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
873 PvexDAOMBR484_SC0210|CGC1 96302.43 5.4772
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PvexansDAOMBR484 11991 1223560 34 11957
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.164:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH30 411 866 6e-128 0.9802631578947368

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
238121 WD40 7.16e-25 32 345 11 288
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
405300 Glyco_hydr_30_2 1.13e-24 417 740 18 357
O-Glycosyl hydrolase family 30.
225201 WD40 1.74e-20 33 340 68 349
WD40 repeat [General function prediction only].
227807 XynC 3.60e-15 506 872 88 432
O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
225201 WD40 2.29e-14 33 305 201 441
WD40 repeat [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.09e-176 370 872 4 500
3.10e-130 401 872 35 498
8.25e-127 378 872 10 499
8.25e-127 378 872 10 499
2.50e-125 380 872 12 499

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.37e-07 114 337 139 369
Structure of the human THO - UAP56 complex [Homo sapiens],7APK_K Structure of the human THO - UAP56 complex [Homo sapiens],7APK_c Structure of the human THO - UAP56 complex [Homo sapiens],7APK_k Structure of the human THO - UAP56 complex [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.70e-102 371 868 1 473
Endo-beta-1,6-galactanase OS=Hypocrea rufa OX=5547 GN=6GAL PE=1 SV=1
3.69e-57 8 345 3 307
WD repeat-containing protein 82 OS=Danio rerio OX=7955 GN=wdr82 PE=2 SV=1
5.08e-57 8 345 3 307
WD repeat-containing protein 82-A OS=Xenopus laevis OX=8355 GN=wdr82-a PE=2 SV=1
9.64e-57 8 345 3 307
WD repeat-containing protein 82-B OS=Xenopus laevis OX=8355 GN=wdr82-b PE=2 SV=1
9.64e-57 8 345 3 307
WD repeat-containing protein 82 OS=Gallus gallus OX=9031 GN=WDR82 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000063 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in EPrPVT00000017371-p1.