logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004798_00241

You are here: Home > Sequence: MGYG000004798_00241

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 Enterococcus_B hirae
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B hirae
CAZyme ID MGYG000004798_00241
CAZy Family CBM5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
508 MGYG000004798_8|CGC1 58740.77 5.326
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004798 2841576 Isolate United States North America
Gene Location Start: 48944;  End: 50470  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004798_00241.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13402 Peptidase_M60 5.34e-45 158 415 1 268
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.
cd12215 ChiC_BD 5.96e-11 467 505 2 41
Chitin-binding domain of chitinase C. Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.
smart00495 ChtBD3 2.53e-08 467 501 3 37
Chitin-binding domain type 3.
cd12204 CBD_like 5.22e-06 468 505 9 45
Cellulose-binding domain, chitinase and related proteins. This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18.
cd00036 ChtBD3 3.08e-05 468 504 2 38
Chitin/cellulose binding domains of chitinase and related enzymes. This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEE77531.1 0.0 1 508 1 508
QNG06678.1 0.0 67 508 1 442
ASV82974.1 0.0 67 508 1 442
QIV91132.1 0.0 67 508 1 442
QXJ62437.1 9.00e-282 137 508 1 372

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EV7_A 8.03e-62 37 437 4 403
Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A 1.18e-59 37 437 4 403
Thecrystal structure of a functionally unknown conserved protein from Bacillus anthracis str. Ames. [Bacillus anthracis str. Ames]
7SCI_A 5.86e-18 171 414 189 438
ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q6QR59 7.44e-15 123 430 590 895
TRPM8 channel-associated factor 3 OS=Mus musculus OX=10090 GN=Tcaf3 PE=1 SV=1
Q6P6V7 1.30e-14 123 430 590 895
TRPM8 channel-associated factor 3 OS=Rattus norvegicus OX=10116 GN=Tcaf3 PE=2 SV=1
A5PJN5 3.49e-12 78 438 546 912
TRPM8 channel-associated factor 1 OS=Bos taurus OX=9913 GN=TCAF1 PE=2 SV=1
Q5R8R3 6.10e-12 78 438 546 912
TRPM8 channel-associated factor 1 OS=Pongo abelii OX=9601 GN=TCAF1 PE=2 SV=2
Q9Y4C2 6.10e-12 78 438 546 912
TRPM8 channel-associated factor 1 OS=Homo sapiens OX=9606 GN=TCAF1 PE=1 SV=3

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
0.000256 0.999118 0.000170 0.000165 0.000141 0.000132

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004798_00241.