CAZyme Information: MGYG000000048_01371

Basic Information

• Species: Clostridium_P ventriculi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P ventriculi
• CAZyme ID: MGYG000000048_01371
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
447	MGYG000000048_4|CGC4	51361.07	8.9776

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000048	2457227	Isolate	United Kingdom	Europe

• Gene Location: Start: 195191; End: 196534 Strand: +

Full Sequence      

MLKLKHYLKKLKTFKFTIFSNYLNKIKISENSYLLKYLRILRKHWEKVCICILILVLIIA
VYFSLSYNFTLNKYNSYIKNTQASQNISVTTLGNGSMVPIYSDLKKQDYTSFIYGFNLND
KTNTYKNGEYITINMNLSSNNDLDGKIINIYSYNTNTKTFECLGEAKVYNNTLTFKVNSL
GEHFITLGNAPTYDVNCGRLVYDEEFNSTSSVSNQWNYDIGNNDGWGNKEEEYYTDNIQN
SNIVNGTLNITALKQNLNGYNYTSARLVSKNSYLYGKIEVCAKLPKGKGTWPAIWMLPEN
NTYGNWPDSGEIDIMEATQKTPNYVHGSLQMNAYNFKTGDQKTASIKVNDLYSKYHVYGV
LWTPNKIELSIDGHVYLTYDRNIYNTGSDSWKTWPYNQPFKLILNIAIGGTYGGTIDNNA
FPQTMSIKYIKVYNLNLNDYNLNTITS

Enzyme Prediction     

No EC number prediction in MGYG000000048_01371.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	203	433	1.9e-72	0.991304347826087

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.46e-82	204	432	3	234	Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
cd08024	GH16_CCF	4.63e-39	200	413	1	279	Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
cd02182	GH16_Strep_laminarinase_like	4.75e-33	200	432	4	257	Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
COG2273	BglS	5.12e-32	205	432	48	262	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
cd00413	Glyco_hydrolase_16	3.40e-28	204	432	1	209	glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPJ86364.1	0.0	1	447	1	455
QPJ85097.1	4.42e-115	79	447	44	409
QPJ84815.1	1.94e-94	80	443	8	371
BAV13066.1	2.94e-86	145	443	160	461
ADL52413.1	2.94e-86	145	443	160	461

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ILN_A	1.69e-65	200	433	7	247	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A	7.25e-50	199	433	6	234	Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
6XOF_A	4.24e-47	188	433	14	266	ChainA, GH16 family protein [uncultured bacterium]
6XQF_A	2.28e-46	188	433	14	266	ChainA, GH16 family protein [uncultured bacterium],6XQG_A Chain A, GH16 family protein [uncultured bacterium],6XQH_A Chain A, GH16 family protein [uncultured bacterium],6XQL_A Chain A, GH16 family protein [uncultured bacterium],6XQM_A Chain A, GH16 family protein [uncultured bacterium]
3AZX_A	1.86e-45	199	446	11	263	Crystalstructure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	7.53e-64	200	433	42	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	7.99e-44	185	433	410	679	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	3.06e-40	200	436	22	270	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	2.00e-32	199	433	26	252	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90	2.09e-30	189	437	47	291	Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999974	0.000055	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
48	70