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CAZyme Information: MGYG000000360_00701

You are here: Home > Sequence: MGYG000000360_00701

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 UBA1829 sp900548385
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385
CAZyme ID MGYG000000360_00701
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
876 97971.45 8.8608
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000360 4492877 MAG Sweden Europe
Gene Location Start: 908577;  End: 911207  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000360_00701.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 673 874 5.2e-18 0.9945054945054945

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09619 CBM9_like_4 7.77e-24 670 870 1 187
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 are often located at the C-terminus of longer proteins and may co-occur with various other domains.
pfam06452 CBM9_1 1.18e-12 673 875 1 182
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.
cd00005 CBM9_like_1 2.10e-07 665 875 3 185
DOMON-like type 9 carbohydrate binding module of xylanases. 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. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
cd00241 DOMON_like 4.68e-07 690 851 1 154
Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
pfam10633 NPCBM_assoc 9.63e-05 538 611 1 75
NPCBM-associated, NEW3 domain of alpha-galactosidase. The English-language version of the first reference can be found on pages 388-399 of the above. This domain has been named NEW3 but its actual function is not known. It is found on proteins which are bacterial galactosidases. The domain is associated with the NPCBM family, pfam08305, a novel putative carbohydrate binding module found at the N-terminus of glycosyl hydrolases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SDU11835.1 5.87e-227 1 875 1 870
AHF92009.1 1.40e-212 43 875 8 867
AHF90983.1 6.04e-207 1 875 1 907
AZS14136.1 1.82e-17 129 486 416 786
QNK56522.1 4.46e-15 132 508 687 1079

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
0.000306 0.999001 0.000197 0.000163 0.000150 0.000136

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000360_00701.