logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: OAG17857.1

You are here: Home > Sequence: OAG17857.1

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 Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG17857.1
CAZy Family GH10
CAZyme Description GH115_C domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A177DF62]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1023 KV441485|CGC1 112800.75 4.7967
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
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 42 696 2.2e-238 0.8493543758967002

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
406396 Glyco_hydro_115 0.0 219 558 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 1.01e-62 835 1011 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 4.66e-04 112 185 53 119
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 1022 1 1021
0.0 1 1017 1 1016
0.0 1 1022 1 1025
0.0 38 1015 27 1036
0.0 38 1015 27 1036

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.64e-195 40 1016 13 937
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]
4.51e-130 43 712 19 667
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
9.32e-128 43 712 18 666
Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7.24e-127 35 712 38 682
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]
8.49e-117 121 1016 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]

Swiss-Prot Hits      help

OAG17857.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000421 0.999558 CS pos: 24-25. Pr: 0.9738

TMHMM  Annotations      help

There is no transmembrane helices in OAG17857.1.