CAZyme Information: MGYG000000189_01126

Basic Information

• Species: Coprococcus sp900066115
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900066115
• CAZyme ID: MGYG000000189_01126
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1148	MGYG000000189_2|CGC1	127204.26	5.5935

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000189	2889110	Isolate	China	Asia

• Gene Location: Start: 258472; End: 261918 Strand: +

Full Sequence      

MKNAKKIIAFLMALTLLVSTIQMPVMAATTKKATIKTVSIVKPETKTLVLKAKKSYQLKT
KVTVNGKISKKVTYKSSNEKVATVSKNGKIKALKKGKTTITVRSKVNKKKKTTLKVIVGT
PVKAVKLNKSKVKTQVGKKVKLKATVSPKKSSVKGVKFTSSNKKVATVSKKGVVTCKKAG
KVTITATAKDGSAKKAKCTITIKKKKTEPSNKPGTPNKPGTPNKPVTPNKPVTPNKPDDK
DDQDNKGDEDNKLSYDGYNLKWEDDFDGDALNEDDWNYEEHAPGWVNSELQAYVKSDQNV
YVKDGKLVIQPVKTKNEDGSYSITSGRINTQGKHDFTYGLFEVRAKVPSGKGFLPAFWMM
PTDENLYGQWPRCGEIDAMEVMGQETDKVYGTIHYGSPHAEKQGTYTLENGNFADEYHTF
SCDWQPGKITWYVDGIKYHETSDWFTAVEGETEVAYPAPFDQPFYMILNLAVGGSWVGYP
DDDADYINTQSYSIDYVKVYQKDSYNEDVEKPVNEVIIRDPDANGNYVNNGDFAKTEDLT
DDIDWKFLTTLEGEGNAVIKNKAIEIHTDKAGTVDYSIQLVQPSIPAEKGGEYTVTFDAW
ADEARTMKVDVSAPDRSYKRYLNDTVVDLTTEKQTYTYTYTMTDKPDANARLEFNFGATD
STATVYITNVSIKKTAQKEIDNSKKPLSDGNYIYNGGFQEGKNRLGDWTVTNNCQAVVSV
TGLADGRRLMVKADTKNKADVILSQDGLPLNVETEYALSFDAQADTDMQLDVVIAGETFT
ADVTTDKQTFNYVFKTPEELTDAFKTITYFLGNKGTIYLDNVRVVENTLIKNGSFKAGFS
GYEVYAEGSTDVSYVVDSQTEDCAADFTIKDTGAQDWMIQLKQNNISLEEGQWYRLSLKA
KSDMNRKLMVALQRDGSSDDDWTPYSGSKTVDLTDEYQSIVVEFKMKNKSDPRTILSISM
GAVGGVQIKQQHRICIDDIILEKIDAPKVDETESDVNLIKNADFSEGDNGLSNWEGGIMG
DAVGTQTVDKGVITYELSDVGTADWNVQLKQTGLALENGKTYEASITLKSTEARTVLLNF
MSNTYKWYGGETIVLPKNEEVVKTITFTMNEETDTDAGFFLSMGKIADVDTPASTITVSN
ISLKKLAE

Enzyme Prediction     

No EC number prediction in MGYG000000189_01126.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	262	500	1.4e-80	0.9956521739130435
CBM4	526	657	6.1e-34	0.9920634920634921
CBM4	829	961	5.6e-27	0.9841269841269841
CBM4	997	1124	1.3e-22	0.9920634920634921

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	3.26e-99	262	500	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	1.59e-52	262	501	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	4.15e-44	257	501	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	1.55e-40	264	500	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	3.76e-34	263	500	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	253	1145	332	1220
QWT52878.1	0.0	253	1146	244	1135
BCN29267.1	0.0	41	1145	129	1201
QQQ91210.1	2.08e-311	253	1145	257	1152
ASU30685.1	2.08e-311	253	1145	257	1152

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	4.82e-54	258	501	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	7.61e-54	258	501	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	6.17e-52	258	500	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	1.98e-50	259	504	4	242	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	7.88e-49	260	501	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	3.06e-48	257	502	422	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	4.96e-44	260	498	22	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	1.43e-41	258	501	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082	5.57e-31	258	501	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q8N0N3	9.47e-29	263	481	35	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
0.000255	0.999087	0.000197	0.000157	0.000150	0.000140

TMHMM  Annotations     

start	end
7	29