CAZyme Information: MGYG000002549_03321

Basic Information

• Species: Bacteroides caccae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides caccae
• CAZyme ID: MGYG000002549_03321
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
922	MGYG000002549_16|CGC6	103709.28	5.2728

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002549	5479119	Isolate	United States	North America

• Gene Location: Start: 151385; End: 154153 Strand: +

Full Sequence      

MKKKIIIFFMLFFLCTVISACSDEDGKGTNTATLEITEQFVDFKENGESQTLVITTNQAE
WSATVESNGKSWCSILPDINPGNHKLTISVTPNTGKEQRSTIITVKAAELSEKITVRQLG
TDKGILISPMMKTFTAEGGKIEFTVTANVEFEIIPTVDWITLPVTTRTAEYVTTDHTYFI
QRNKGEKRTGTITVKDKASDLFSELIMSQEALGEYESGESGIQGDLLVPVSTGSAFNSLG
KVSQLGSSGFHRTYDGSKETGYHSNTSDDFPNNWPLTLTFEFAEQPRIDYCVCHSTGSDK
LKKAKIFVSTETEPEYTKLMDVDLSGSTTALIKFSSPVINPKGIKFEVTESSGKYLVIKE
MEFYRQNSDNYDPLNLFTDITCSELKPGITEKDIDACPDPLFRNVAFYLSINKYPREFRI
QEYKAYPHPELFRKANKTSAEHNLLDNPTGIFVNKGKEVVVLVGDSHGYQLSARILNLNV
SGGDGFNYNYSYPLVEGINRFIAETDGLIYIYYHTPEYRDALPIKIHIPSGQVNGYFDSG
KHQPSDWSRLLHAAVGPHLDVLGEKAHLIFPVDKFKANTPDGKALIDAYDRLVLLEQQFM
GLEKYDRMDPNRVCFSVMYNDSYMYSAGNHTGYVVGTMNELCNLEKFSTTSIWGPAHEVG
HSYQTKPGLCWLGMTEVTNNIHSLYVQTSFGNQSRLLDKQGDYTSIYEKSMCMYFVRKRA
HIITDSDVNVFNQLVPFWQLYLYTKAIGQEDFYKDLYELIRINTDQDTPGKSQLEFTFLA
SKASGLDLTEFFVKWGFFEPIDIEKSDYSKGQFVVTESMIDETKQRITDLGLPKPKGIIE
YICDSNVDCYKTFNSIIKGTAQREGQKIVMTNWRNVAVYEVYSNGKLCFVSPASSFTVNG
NLGTKVQVFAVSATGEKVEVTF

Enzyme Prediction     

No EC number prediction in MGYG000002549_03321.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	8.36e-46	531	796	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	8.47e-20	33	118	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	1.31e-09	125	195	2	70	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	2.29e-09	448	527	22	107	N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
pfam13004	BACON	2.53e-09	62	118	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
QUU06838.1	0.0	1	922	1	922
QRM71921.1	2.97e-249	1	922	1	939
QTO25368.1	8.39e-249	1	922	1	939
QCT79445.1	1.34e-247	1	922	1	939
QRP89238.1	1.34e-247	1	922	1	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	1.70e-77	374	836	12	479	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	1.85e-66	374	918	32	605	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	2.33e-59	408	918	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	4.43e-38	448	846	45	409	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A	6.72e-36	448	846	45	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
0.000000	0.000000	1.000055	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002549_03321.