CAZyme Information: MGYG000002622_00669

Basic Information

• Species: Phocaeicola sp900546095
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900546095
• CAZyme ID: MGYG000002622_00669
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
943	MGYG000002622_4|CGC1	105606.26	4.4276

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002622	3429958	MAG	China	Asia

• Gene Location: Start: 30658; End: 33489 Strand: -

Full Sequence      

MNNFLKTKAAALFAAAALLGGLSGCWDENEWESIPNGAFLQVAETSLNFDSPATTYQLEV
KCNEEYVVGYGNGLENWCTATKDELGDLTLNITENTEKDVRRGELYIKALSQTDTISVAQ
LGWGKAILVSETVVNMSETGGEFDIDVTANVPYNFDFAGSDWVQETASASSRAYETVTKT
HHFSVLPNKGEARNASITVDDVEGSEDIGAATFTVSQKGLGSYEPGAPETGNDIKVTVSS
VTGMDGDWRPNRDYSKMIDGVAVAGEDEGWLSNWQDPKYPKWFEFTFDEPQDIDYVNYIA
SYKGHFKKVKIEVYTDVNVQRTAGYTTVFDGELVKNNSGSTRIDFNQPQAGVTKVKFTLE
DSWDTGECRCCEMEFYKKDPNTFDWTTLFANPACTELKSGVTEQDILSCEHSFYKNMAWY
MYNDRYPREFRIADYKAYPHPDVQAKENKTTTYSLLDNPTGIQVAADENLVVMADLKGQE
SVKIRVQNLDTPGEDGFGGNEYAVKEGINTIKMKEKGLVYVMYHTADYETAPEITLHFAS
GKVNGYFDSQNPAHEGRWNELLSAAVDKHFDVVGKYAHLTFPTLNFVNNTRDGKELIDTY
DELVYNEQVFLGLEKYGRMFKNRMYFNVMYSDSYMYSTSYRTSYSAGTIDALTDPDKLRT
TDCWGPAHEVGHSNQTRPGLKWLGTTEVTNNITALYIQTTIFGNDSRLELQDFYNKAWNS
LMVPGIAHAQETDVFRKLVPFWQLELYYGKVLGRTPTQQADKGGFYPDVYEYVRTNEDLE
TAGEQQLEFVYNCCVNAKANLLDFFGKWGFLTPVDTEIDDYGKGRLTVTQQQIDNLKARV
EGLGYAKPDVALEYITDYMVDSYKNKDNVVAGSASRSGNTITLANWQHVAAFEVKDASGK
LVYVSEGIAPGSSSREFTLPTDWASGFTVYAVSAAGNRMPVNF

Enzyme Prediction     

No EC number prediction in MGYG000002622_00669.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	9.17e-50	541	809	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	1.00e-10	39	120	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.
cd14948	BACON	5.58e-07	126	218	1	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.
pfam17291	M60-like_N	4.11e-05	459	537	22	107	N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
pfam18630	Peptidase_M60_C	1.26e-04	873	938	3	63	Peptidase M60 C-terminal domain. This is C-terminal domain (CTD) of M60-peptidases pfam13402. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerize through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUU07039.1	0.0	2	939	3	938
QQT78256.1	0.0	2	939	3	938
QRP56500.1	0.0	2	939	3	938
QCT79445.1	6.45e-295	40	943	34	939
QRP89238.1	6.45e-295	40	943	34	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	6.04e-77	388	857	14	487	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	1.90e-49	387	939	33	605	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	1.22e-46	420	939	20	557	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	3.35e-33	459	809	45	379	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A	2.60e-32	459	809	45	379	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
0.000000	0.000035	1.000013	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002622_00669.