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CAZyme Information: MGYG000004513_03144

You are here: Home > Sequence: MGYG000004513_03144

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 sp900550905
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900550905
CAZyme ID MGYG000004513_03144
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1002 113127.23 8.2289
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004513 4294613 MAG Israel Asia
Gene Location Start: 497;  End: 3505  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004513_03144.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 338 603 8.8e-21 0.6589327146171694

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09621 CBM9_like_5 1.48e-54 813 1002 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 1.27e-12 830 971 4 146
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 3.80e-12 838 973 30 161
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
AHF94342.1 1.12e-141 77 1002 100 1032
AHF90198.1 1.49e-122 51 1002 52 1005
AVM46276.1 3.56e-82 264 1002 410 1136
AVM44759.1 6.82e-79 66 988 55 951
AVM47149.1 4.99e-75 219 1002 526 1306

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
0.000323 0.999022 0.000175 0.000167 0.000150 0.000145

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004513_03144.