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CAZyme Information: MGYG000004003_00468

You are here: Home > Sequence: MGYG000004003_00468

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004003_00468
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
936 MGYG000004003_5|CGC2 104023.35 4.9054
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004003 5653807 MAG United Kingdom Europe
Gene Location Start: 34640;  End: 37450  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004003_00468.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13402 Peptidase_M60 4.39e-50 532 808 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.
cd14948 BACON 4.08e-11 30 112 2 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.
pfam17291 M60-like_N 4.44e-07 426 528 3 107
N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
NF037974 SslE_AcfD_Zn_LP 7.07e-06 640 849 1152 1381
SslE/AcfD family lipoprotein zinc metalloprotease. Members of this family are surface lipoprotein zinc metalloproteases, from the family that includes accessory colonization factor AcfD from Vibrio cholerae, SslE (YghJ ) from E. coli (Secreted and Surface-associated Lipoprotein from E. coli), and VPA1376 from Vibrio parahaemolyticus. Each is about 1500 amino acids long, and SslE is a known substrate of a type II secretion system (T2SS). SslE is known to have mucinase activity.
cd14948 BACON 7.11e-06 119 205 2 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTO25368.1 1.39e-259 2 936 3 939
QRM71921.1 1.96e-259 2 936 3 939
QCT79445.1 3.14e-258 10 936 14 939
QRP89238.1 3.14e-258 10 936 14 939
QUU03487.1 4.44e-258 10 936 14 939

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5KD2_A 1.73e-52 375 929 32 602
BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7SCI_A 9.85e-50 366 857 2 487
ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD5_A 8.79e-47 409 929 20 554
BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
7BLG_A 2.09e-30 213 367 12 162
ChainA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLH_AAAA Chain AAAA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLJ_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLK_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5EV7_A 1.22e-26 448 808 45 379
Thecrystal structure of a functionally unknown conserved protein mutant 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
0.000089 0.064630 0.935224 0.000026 0.000030 0.000024

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004003_00468.