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CAZyme Information: MGYG000004499_02530

You are here: Home > Sequence: MGYG000004499_02530

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 Victivallis sp900551245
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900551245
CAZyme ID MGYG000004499_02530
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
983 110359.51 8.346
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004499 4071424 MAG Israel Asia
Gene Location Start: 28119;  End: 31070  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004499_02530.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 389 597 1.4e-17 0.5498839907192575

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09621 CBM9_like_5 1.15e-60 795 981 1 188
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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd00241 DOMON_like 5.15e-11 820 961 12 156
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.
cd09619 CBM9_like_4 8.11e-07 819 957 29 165
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM46276.1 2.49e-163 168 982 306 1137
AHF94342.1 4.59e-150 55 982 83 1033
AVM47149.1 1.29e-149 193 982 494 1307
AHF90198.1 6.22e-137 58 981 60 1005
AVM44759.1 3.57e-135 193 982 160 965

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
0.000462 0.998806 0.000195 0.000196 0.000175 0.000159

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004499_02530.