CAZyme Information: MGYG000002168_01172

Basic Information

• Species: Prevotella sp900556825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556825
• CAZyme ID: MGYG000002168_01172
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
773	MGYG000002168_24|CGC1	87981.74	5.9403

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002168	3553249	MAG	Denmark	Europe

• Gene Location: Start: 13727; End: 16048 Strand: +

Full Sequence      

MKSKFFLYIFMLLFISCSSHEIEENNRWLALPSPSFSFDYLGGTQIQSAKITSEILPKSI
TYSYAGDGDKWCTVSINESTVTINVEHSYIEKDRSTQVTIAYEDKNPVILSVSQSAAPSA
EDTKIKVVNATATSEEVSGKDADGNPLTLPMSYDGNVKTYYNSKFGKVNYPFTITYELDG
LHTLSKIIYTPRTDAGNKWGSFDKFTVEGSTNEDPETFITLGEYSRGDNVQVPLEIPISH
PLKNAKYVRFTVHKAYQDRISCAEMEFYEASKNSFNIASIFKDPLCTCLKEGVTRKQIYQ
IPDSNLLQLGLALLDNTYNPAYRHASYRPYQNPSIMSKINKMSKYSMRDGVTGLYAKAGE
PLTAIVGSLYKGADVSLLIQDLNGGYNNYKIYTLQEGYNKIIPSVGGLIYVLNYTEDAVP
LLLKTSEGKELSSQKTVEIHFPMASVNGYFDIAKNSEADWSDMLKKATYQDIDVLGEYSH
LTWRVSDFRKYNTNIIQTVKNLDNLVYNEEDWTGLVKNNKMFPNRMHICIDYKAKSPNSS
DYRVVFNASDYYAQPFCEPDAFPSRCWGPAHEIGHSNQVRPGMKWAGMTEVTNNLMCLWE
QDFLGRPCKLLVDGAQDSYKNFYERAINYIVLGKRAHCLPGESNIIRELQLVPFWQLKLY
LVDVLGKKDFYRDLYEHFRITPDLDTSSKTQGILQLDFVRQVCNLAKINLIEFFKAWGFL
TPVNTTLNDYGSKKFVITQEEIDALELEIQAKKYPKAPSELWKITENNLEDFH

Enzyme Prediction     

No EC number prediction in MGYG000002168_01172.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	4.29e-27	446	718	3	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.
pfam00754	F5_F8_type_C	3.16e-08	129	267	1	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd14948	BACON	7.22e-06	29	115	2	83	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.
pfam13004	BACON	1.45e-04	61	115	1	61	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
cd00057	FA58C	0.002	129	268	13	142	Substituted updates: Jan 31, 2002

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUU06736.1	4.42e-317	16	772	31	800
QQT78470.1	1.27e-316	16	772	31	799
QRP59645.1	1.27e-316	16	772	31	799
QUU07870.1	8.07e-109	122	770	224	862
QRP57133.1	3.05e-108	122	770	224	862

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	7.56e-49	276	766	10	487	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	1.88e-43	277	742	31	485	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	2.50e-37	304	742	12	437	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	5.88e-20	352	768	46	409	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A	5.67e-19	352	768	46	409	Thecrystal structure of a functionally unknown conserved protein from Bacillus anthracis str. Ames. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000475	0.294461	0.704627	0.000143	0.000149	0.000137

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002168_01172.