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CAZyme Information: MGYG000001461_00112

You are here: Home > Sequence: MGYG000001461_00112

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 Bacteroides neonati
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides neonati
CAZyme ID MGYG000001461_00112
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
682 78583.11 6.1114
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001461 5024706 Isolate not provided not provided
Gene Location Start: 134480;  End: 136528  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001461_00112.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 48 249 2.3e-43 0.9725274725274725

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09620 CBM9_like_3 2.81e-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 4.40e-28 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 2.42e-14 393 631 113 339
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown].
pfam06452 CBM9_1 1.12e-12 48 249 1 177
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.
pfam02638 GHL10 2.73e-07 393 636 68 299
Glycosyl hydrolase-like 10. This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCQ37007.1 0.0 13 680 19 686
QTO24490.1 0.0 13 680 19 686
AUI46257.1 0.0 13 680 19 686
QCQ32632.1 0.0 13 680 19 686
CUA18365.1 0.0 15 680 22 687

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
0.057934 0.925357 0.015567 0.000418 0.000342 0.000356

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001461_00112.