CAZyme Information: MGYG000004188_01454

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004188_01454
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
942	MGYG000004188_8|CGC5	106828.75	4.7912

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004188	3351981	MAG	United Kingdom	Europe

• Gene Location: Start: 133041; End: 135869 Strand: -

Full Sequence      

MYLLFVISVCSCGNKDTLMDVTNPFLEVNTSTLNFGEEYSEKVVEIKCNTKWTCEVEGEN
SSWCHLDPRNGELVISVDNNEDKDIRQARVIVTASQMKKTIEVVQLGWGKAILLTTNSAT
IPVTGGKVELEVTTNIEYQYKLPQDCEWVHDTQTRAADHPLVSKVFVFHVDASKTDGERQ
AVITFSDVDLESDLKPATFTIVQKGLGQYDPLNPEELEEDILVKVTGATASSEQPGYGIA
NSYDGNKETQYHSSWNNSDDHYYPIILEYTFAEGTDMDYMIYYPRADGHWNGHFKLVDIE
VRSNANTRGVDEWQYVMTYDFGGTSSARRVDFPHSLIGVSALRFTIHSGSGDGQGFAVCS
EMEFYKKNPESFEYTTLFTDPSCSELKTGITEKDILSCTHSFFKNIAYYMYHGRYKTDFR
INTFQAYPHPDVQALENKTSPYSLLDNPTGIALESGETLVAMVGDLQGQQISLRVQNLNK
PGGDGFGGMEYPLSTGINKLKIEQGGLAYIMYHTPDFEDAPKIKMHFATGKVNGYFDSQD
PEHEGRWKELLNQACDDYFDVLGKYAHLTFPTNRFRNHTTDLKALIDTYDLLVYGEQQLM
GLEKYGRMFRNRMYFNVMYHSYMYATSYHTAYHDETLSELCNEKSLKTTACWGPAHEVGH
CNQTRPGLKWVGTTEVTNNIFSEYVQTTLFGQPSRIQTESMGSQESPNRYSWAWNSILVG
KISHALEPDVFCKLIPFWQLELYFGKVLGMTPLQQTDRGGFYPDVFEYIRTHEDLKTPGE
QQLEFVYIASKVAHTNLLDFFEKWGFLTPVDVLVEDYGSGQMTITQDQADEIRRRVEALG
YSKPDIALEYITDNTVDVFKNKKDIVVGTASRTEASLTMKNWKNVVVYEVRDGNEGGTLI
CVSDGMLEPSATASFSVKGGWKDTYKVYAVSYNNKRIEVKFL

Enzyme Prediction     

No EC number prediction in MGYG000004188_01454.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	5.53e-62	530	805	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	1.13e-15	25	105	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	6.39e-10	111	204	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	1.40e-06	448	526	22	107	N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
pfam13004	BACON	6.86e-05	53	105	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	10	941	21	939
QRP89238.1	0.0	10	941	21	939
QUU03487.1	0.0	10	941	21	939
QTO25368.1	0.0	11	941	20	939
QRM71921.1	0.0	11	941	20	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	1.70e-80	377	853	14	487	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	2.29e-60	376	937	33	605	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	2.56e-56	409	937	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	8.06e-33	424	805	19	379	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
7BLG_A	5.13e-32	220	367	22	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QLU7	2.42e-11	547	806	649	889	TRPM8 channel-associated factor 2 OS=Bos taurus OX=9913 GN=TCAF2 PE=2 SV=1
A6NFQ2	3.19e-11	547	816	650	898	TRPM8 channel-associated factor 2 OS=Homo sapiens OX=9606 GN=TCAF2 PE=1 SV=2
Q8BNE1	1.29e-08	505	806	611	893	TRPM8 channel-associated factor 1 OS=Mus musculus OX=10090 GN=Tcaf1 PE=2 SV=1
A5PJN5	1.69e-08	505	806	611	890	TRPM8 channel-associated factor 1 OS=Bos taurus OX=9913 GN=TCAF1 PE=2 SV=1
Q5XHI4	2.21e-08	547	806	632	872	TRPM8 channel-associated factor homolog OS=Xenopus laevis OX=8355 GN=tcaf PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.482002	0.515067	0.002258	0.000302	0.000179	0.000200

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004188_01454.