CAZyme Information: MGYG000000414_01951

Basic Information

• Species: Alistipes sp900546065
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900546065
• CAZyme ID: MGYG000000414_01951
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
959	MGYG000000414_15|CGC1	106307.2	4.8189

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000414	2648727	MAG	Sweden	Europe

• Gene Location: Start: 53072; End: 55951 Strand: +

Full Sequence      

MKRSATRFFAAAATILLAAGITCSCHKSGTDVYNGPATLEVDVSTVNFTEENASNRTIMV
KSNVAWDYTVSDGWLHAEKQPDRLIISAEDNDQKNIRRATVTITVPDLPAHTVEVQQLGW
GKAILLSQSTTTVSAAGGDITVEVTTNVEVEASVGSDCTWIYETPIDTRSAAHPVVTSTR
AFSVSGNTADGTRSATITFSDKQTPSDVEAATLTVTQRGLDAYAPESTESLKDDIKLIIA
RGEASSYQSGGEIELSFDGDMNTIYHSNWNNAGDGYFPITLTYYLEQESDIDYMVYYPRT
TGWNGRFKEVEIEALSAITQNASTAPAATPQWQHVMTHDFGGNASAAKVEFPEPLIGVTA
IRLTVKSGAGDGQGFASCAEMEFYRRNPEAFDYTTLFTDASCSELRAGVTPQDIAACPYA
FFKNIAYFMYHDRYAKEFRINTFKAYPNPDTEATRNKTSQYSLLDNPTGIEVAAGQQLIV
MADLKGQSVSLRVQNLDRPNGDGFGGDSYPISTGVNKIDITNKGLVYVMYHTDNFASAPA
VRLHFATGTVNGYYDSQRADHEGRASELLGAATGKYFDVVGAYAHLIFPTERFRNHTHDL
KALIDAYDALVYREQEFIGLEKYGKMFHNRMCFTVMYTSYMYSTSYHTAYHDDTLAELCD
ENRLTTSACWGPAHEVGHSNQTRPGLKWLGTTEVTNNILSQHIQTSVYGQDSRVQTENMG
DAANPNRYTKAWSNILVKDAPHATEGDVFCKLIPFWQLELYFGKVLGRTPMQQSDHGGFY
ADCFEWVRTHDNLSTAGEQQLEFVYIASACARMNLLDFFDKWGFLTPVDATIDDYGTGQL
TVTQQMIDRIRSRVEALGYDAPTAAIEYITDNNYETFKQQKSVVKGTAERSDRKLTMSGW
QNVIVYEVRDGGPDGTLIHVSDGMLRPSTTASFDVPAAWQPSWKVYAVQYDNRRIEVTF

Enzyme Prediction     

No EC number prediction in MGYG000000414_01951.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	9.58e-51	574	823	27	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	2.95e-11	123	217	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	5.24e-11	38	117	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.
pfam00754	F5_F8_type_C	4.26e-10	245	381	6	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam13004	BACON	1.06e-05	150	217	1	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
QCT79445.1	0.0	38	959	33	939
QRP89238.1	0.0	38	959	33	939
QUU03487.1	0.0	38	959	33	939
QTO25368.1	0.0	38	959	33	939
QRM71921.1	0.0	38	959	33	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	1.28e-67	396	871	14	487	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	1.99e-66	395	955	33	605	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	1.12e-61	429	955	21	557	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	1.28e-40	232	386	20	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]

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	0.000012	1.000033	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000414_01951.