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CAZyme Information: QRC96192.1

You are here: Home > Sequence: QRC96192.1

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 QRC96192.1
CAZy Family CE4
CAZyme Description DUF1680-domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q0V4B2]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
620 68122.19 8.6444
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

No EC number prediction in QRC96192.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH146 41 556 5.3e-197 0.9960238568588469

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
400342 Glyco_hydro_127 4.71e-155 41 537 1 479
Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
226063 COG3533 3.83e-96 39 536 14 479
Uncharacterized conserved protein, DUF1680 family [Function unknown].
406713 DUF4986 0.004 565 612 26 84
Domain of unknown function. This family around 150 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Bacillus species. The function of this family remains unknown.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 620 1 620
0.0 28 616 43 633
7.64e-314 28 616 41 631
1.64e-313 16 614 22 621
4.77e-311 16 616 33 635

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.62e-97 37 612 28 648
Chain AAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]
1.16e-92 37 612 28 648
Beta-L-arabinofuranosidase [Bacteroides thetaiotaomicron]
1.06e-15 104 572 82 571
Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
1.31e-14 104 572 82 571
Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]

Swiss-Prot Hits      help

QRC96192.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000485 0.999515 CS pos: 19-20. Pr: 0.9672

TMHMM  Annotations      help

There is no transmembrane helices in QRC96192.1.