CAZyme Information: MGYG000001707_00896

Basic Information

• Species: Coprococcus sp000154245
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp000154245
• CAZyme ID: MGYG000001707_00896
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1157	MGYG000001707_7|CGC1	128366.6	5.515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001707	2954116	Isolate	not provided	not provided

• Gene Location: Start: 46116; End: 49589 Strand: +

Full Sequence      

MKNAKKIIAFLMALTLLVSTIQMPVMAATTKKATIKMVSIVKPETKTLVLKAKKSYQLKT
KVTVNGKISKKVTYESSNKKVATVSKTGKIKALKKGKATITVRSKVNKKKKTTLKVIVGT
PVKSVKLNKSKVKTQVGKKVKLKATVSPKKTSVKGVKFTSSNKKVATVSKKGVVTCKKAG
TVTITATAKDGSGKKAKCKITIKKKTTKPSNKPETPNKPETPNKPETPNKPETPNKPETP
NKPETPNKPETPNKPDDKDNKLSYDGYNLKWEDDFDGDALNEDDWNYEEHAPGWVNSELQ
AYVKSDQNVYVKDGKLVIQPVKTKNEDGSYSITSGRINTQGKHDFTYGLFEVRAKVPSGK
GFLPAFWMMPTDENLYGQWPRCGEIDAMEVMGQETNKVYGTIHYGSPHAEKQGTYTLEDG
NFADEYHTFSCDWQPGKITWYVDGVKYHETSDWFTAVEGETEVAYPAPFDQPFYMILNLA
VGGSWVGYPDDDADYINTQSYSIDYVKVYQKDSYNEDVEKPVNEVIIRDPDANGNYVNNG
DFAKTEDLTDDIDWKFLTTLEGEGNAVINDKTIEIHTDNAGTVDYSIQLVQPSIPAEKGG
EYTVTFDAWADEARTMKVDVSAPDRSYKRYLNDTVVDLKTEKQTYTYTYTMMDKPDANAR
LEFNFGATDSTATVYITNVSIKKTAQKEIDNSKKPLSDGNYIYNGGFQEGKNRLGDWTVT
NNCQAVVSVTGLADGRRLMVKADTKNKADVILSQDGLPLNSETEYALSFDAQADTDMQLD
VVIAGETFTADVTTDKQTFNYVFKTPEELTDALKTITYFLGNKGTIYLDNVRVVENTLIK
NGSFKAGFSGYEVYAEGSTDVSYVVDSQTEDCAADFTIKDTGAQDWMIQLKQNNISLEEG
QWYRLSLKAKSDMNRKLMVALQRDGSSDDDWTPYSGSKTVDLTDEYQSIVVEFKMKNKSD
PRTILSISMGAVGGVQIKQQHRICIDDIILEKIDAPKVDETESDVNLIKNADFSEGDNGL
SNWEGGIMGDAVGTQTVDKGVITYELSDVGTADWNVQLKQTGLALENGKTYEASITLKST
EARTVLLNFMSNTYKWYGGETIVLPKNEEVVKTITFTMNEETDTDAGFFLSMGKIADVDT
PASTITVSNISLKKLAE

Enzyme Prediction     

No EC number prediction in MGYG000001707_00896.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	271	509	4e-81	0.9956521739130435
CBM4	535	666	3.8e-33	0.9920634920634921
CBM4	838	970	5.7e-27	0.9841269841269841
CBM4	1006	1133	1.3e-22	0.9920634920634921
CBM4	700	813	3e-16	0.9285714285714286

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	2.86e-99	271	509	1	235	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	4.93e-53	271	510	3	330	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	1.75e-44	266	510	1	259	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.
cd00413	Glyco_hydrolase_16	9.13e-41	273	509	1	210	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.
cd02179	GH16_beta_GRP	1.33e-33	272	509	4	320	beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16. Beta-GRP (beta-1,3-glucan recognition protein) is one of several 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. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAA34888.1	0.0	261	1154	331	1220
QWT52878.1	0.0	260	1155	242	1135
BCN29267.1	0.0	41	1154	129	1201
QQQ91210.1	1.94e-314	262	1154	257	1152
ASU30685.1	1.94e-314	262	1154	257	1152

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	6.65e-54	267	510	18	263	Structureof the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
3AZX_A	1.05e-53	267	510	10	255	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]
2VY0_A	8.50e-52	267	509	13	259	TheX-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus],2VY0_B The X-ray structure of endo-beta-1,3-glucanase from Pyrococcus furiosus [Pyrococcus furiosus]
3ATG_A	5.04e-50	269	513	5	242	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	1.47e-48	269	510	9	243	Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	5.60e-48	266	511	422	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	3.17e-43	269	507	22	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	4.22e-40	267	510	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082	7.22e-30	267	510	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	3.18e-28	271	490	34	309	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 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
0.000248	0.999092	0.000192	0.000155	0.000150	0.000141

TMHMM  Annotations     

start	end
7	29