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CAZyme Information: ASPVEDRAFT_712718-t33_1-p1

You are here: Home > Sequence: ASPVEDRAFT_712718-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 versicolor
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
CAZyme ID ASPVEDRAFT_712718-t33_1-p1
CAZy Family GH95|GH1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
975 KV878130|CGC9 108261.58 4.5398
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AversicolorCBS583.65 13364 1036611 142 13222
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131:6

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 35 653 7.8e-212 0.8278335724533716

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
406396 Glyco_hydro_115 1.72e-178 187 525 2 333
Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
407695 GH115_C 5.71e-57 799 970 1 172
Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
397627 Glyco_hydro_67N 0.001 44 151 26 119
Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 974 5 989
0.0 1 974 5 989
0.0 1 974 5 989
0.0 1 974 5 989
5.75e-305 1 974 5 999

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.91e-173 41 971 25 933
Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
6.39e-134 38 971 25 834
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
5.20e-131 38 971 24 833
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
3.31e-118 7 646 26 647
Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
1.12e-116 79 974 53 966
Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]

Swiss-Prot Hits      help

ASPVEDRAFT_712718-t33_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.486851 0.513140 CS pos: 18-19. Pr: 0.2865

TMHMM  Annotations      help

There is no transmembrane helices in ASPVEDRAFT_712718-t33_1-p1.