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CAZyme Information: MGYG000001898_01857

You are here: Home > Sequence: MGYG000001898_01857

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 Parabacteroides sp900552415
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552415
CAZyme ID MGYG000001898_01857
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
682 MGYG000001898_70|CGC1 78954.59 5.0535
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001898 3107743 MAG Denmark Europe
Gene Location Start: 13718;  End: 15766  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001898_01857.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 48 250 2.9e-38 0.978021978021978

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09620 CBM9_like_3 6.96e-75 48 250 1 200
DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
cd09618 CBM9_like_2 1.85e-26 37 220 2 170
DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
COG1649 YddW 3.56e-17 393 631 113 339
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown].
pfam02638 GHL10 7.59e-09 393 636 68 299
Glycosyl hydrolase-like 10. This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.
pfam06452 CBM9_1 8.18e-08 48 146 1 94
Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CUA18365.1 0.0 20 677 27 684
CAH07622.1 0.0 20 677 27 684
QCT78438.1 0.0 20 677 27 684
QRP90424.1 0.0 20 677 27 684
AKA51642.1 0.0 20 677 27 684

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000770 0.997949 0.000640 0.000197 0.000213 0.000211

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001898_01857.