logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: QRC91067.1

You are here: Home > Sequence: QRC91067.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRC91067.1
CAZy Family AA3
CAZyme Description GH115_C domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2EQS3]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1028 113652.57 5.3921
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
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 43 698 5.9e-239 0.8464849354375896

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
406396 Glyco_hydro_115 0.0 222 561 1 333
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 2.73e-62 838 1013 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 0.005 122 188 62 119
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 1028 1 1028
0.0 1 1025 1 1021
0.0 1 1018 1 1015
0.0 29 1017 25 1022
0.0 24 1017 14 1036

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.55e-207 33 1018 6 937
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]
2.37e-132 43 715 19 667
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
6.60e-131 43 715 18 666
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
3.91e-130 124 1018 65 967
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]
7.52e-129 33 707 35 674
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]

Swiss-Prot Hits      help

QRC91067.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000480 0.999487 CS pos: 24-25. Pr: 0.9734

TMHMM  Annotations      help

There is no transmembrane helices in QRC91067.1.