logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003363_02352

You are here: Home > Sequence: MGYG000003363_02352

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 sp900766195
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900766195
CAZyme ID MGYG000003363_02352
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
741 MGYG000003363_116|CGC1 84738.5 6.3891
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003363 4177575 MAG United States North America
Gene Location Start: 44471;  End: 46696  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003363_02352.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13402 Peptidase_M60 2.52e-48 424 683 1 265
Peptidase M60, enhancin and enhancin-like. This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonisation of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
cd14948 BACON 2.83e-09 33 113 1 82
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam00754 F5_F8_type_C 1.33e-04 151 260 19 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCT79445.1 1.25e-180 34 741 118 860
QRP89238.1 1.25e-180 34 741 118 860
QUU03487.1 1.77e-180 34 741 118 860
QRM71921.1 3.90e-179 34 741 118 860
QTO25368.1 3.90e-179 34 741 118 860

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7SCI_A 1.78e-70 269 734 10 487
ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A 2.98e-61 266 740 27 513
BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A 3.16e-56 314 740 28 465
BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
5EV7_A 4.05e-30 345 734 45 407
Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A 1.80e-28 345 734 45 407
Thecrystal structure of a functionally unknown conserved protein from Bacillus anthracis str. Ames. [Bacillus anthracis str. Ames]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000439 0.061251 0.938077 0.000079 0.000085 0.000063

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003363_02352.