CAZyme Information: MGYG000003252_03444

Basic Information

• Species: Bacteroides sp900761785
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785
• CAZyme ID: MGYG000003252_03444
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
884	MGYG000003252_327|CGC1	100399.84	5.6477

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003252	8296673	MAG	United States	North America

• Gene Location: Start: 14916; End: 17570 Strand: -

Full Sequence      

MKNIAKSLLIILCTSLFGTLPASCTKDNHPLVENIFNIAQDELEVGFLKTSSSTLVPVNT
NLSPDQWKVTATDRWCTVEQSGIGNETAIKISVTANNDKKIRKTTITAQSTLKTYTISVS
QHGTETTLETIADIRILPTGGRASEAQPGSEIKYTWDGIIGSGQCYHSIWNQKANFPVTL
EYYFNANKNEEIDYFIYHSRNGNGNFGKFNLYVSTNDHPHYVLYGSYDFKMKNTPQRVDF
EGGLKGVRNIKLEVHSGLNDFVSCDEMEFLKKAASQEDKNQLHTLLLNVFSDLSCSELNT
ETNDRKIALLPAFYADLAMQLKNGTYPTTEKKFRTATYQPYSIVEDWADKLMTKKYSNLD
NPTGICVEEGDELNVLVSDTHGQSISLQCIGEEDAGGYVQVAGSGDNYFIEKGANKLTMR
SSGQLFVMYNTDLTLPEAKPIRIHFTPGSGKVTGFFDLKTDKTDEAYAELLAKATHKYFC
VRGEKIIFYFHTTKMREHVNNEIRSAIHLWDDIISWQQELMGIDDVRPSQVNNHLFAFSP
EGSYMWASDYRIAFADWKLGDILLKDNVMAAEDNAWGPAHEIGHIHQSAINWAGSTESSN
NLFSNYVIYKLGKYKSRGKGLNQLAKARFEQGRSWLGMLNPPQPDEERGGEDTELHMRMN
WQLWNWYHRCEAKTDFWPTLFKLMRNLHIGEGEDCGRKQLEFAKMASKAANENLTDFFET
WGFFEPVQDKVYQYGTYDYIVTEQQIEDAKAYMAQFPAPKRAIQYIEDRKTEQFSSGDYR
YKEVGDVGYYTQFKDNMKITQNPTYTLNVSTQDKTILIRNGEEAVAFEVRKQEKQAGSQT
VSMGKLVYFANSFEFKVPSNIDISDCGIYAVQADGERKLMAPIN

Enzyme Prediction     

No EC number prediction in MGYG000003252_03444.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	1.23e-26	450	722	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.
pfam18630	Peptidase_M60_C	2.17e-16	804	877	1	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.
cd14948	BACON	1.66e-13	36	121	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.
pfam19190	BACON_2	1.95e-06	36	124	2	91	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.
pfam13004	BACON	5.91e-06	67	121	3	60	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAO79349.1	0.0	19	880	18	857
QQA07622.1	0.0	19	880	18	857
QUT42145.1	0.0	19	880	18	857
QUT69943.1	0.0	19	880	18	857
QUU10001.1	3.17e-312	16	878	20	949

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KD2_A	7.24e-269	286	880	31	607	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	2.86e-258	330	880	27	559	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
7SCI_A	2.68e-36	287	763	12	482	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5EV7_A	2.20e-18	362	722	45	379	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A	2.47e-15	362	722	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
0.000375	0.111071	0.888340	0.000077	0.000074	0.000060

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003252_03444.