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CAZyme Information: MGYG000000538_02078

You are here: Home > Sequence: MGYG000000538_02078

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 sp900549045
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900549045
CAZyme ID MGYG000000538_02078
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1017 114717.72 9.2543
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000538 3384359 MAG Fiji Oceania
Gene Location Start: 146833;  End: 149886  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000538_02078.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 308 471 3.6e-22 0.39675174013921116

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09621 CBM9_like_5 8.08e-25 724 884 28 186
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 1.50e-05 717 868 11 158
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.
pfam01229 Glyco_hydro_39 4.29e-05 373 435 121 189
Glycosyl hydrolases family 39.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM45582.1 1.33e-136 154 1015 32 916
BBH24554.1 2.34e-92 22 884 257 1135
AVM45605.1 1.31e-86 27 886 230 1093
BBH20281.1 2.96e-83 154 901 223 991
AHF94113.1 1.25e-76 168 886 247 984

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZN2_A 1.49e-10 309 486 55 224
Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
5BX9_A 1.49e-10 309 486 55 224
Structureof PslG from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5BXA_A Structure of PslG from Pseudomonas aeruginosa in complex with mannose [Pseudomonas aeruginosa PAO1]

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
0.000240 0.998990 0.000204 0.000190 0.000172 0.000163

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000538_02078.