CAZyme Information: MGYG000000245_00123

Basic Information

• Species: Roseburia sp003470905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp003470905
• CAZyme ID: MGYG000000245_00123
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1853	MGYG000000245_1|CGC4	204051.2	4.9

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000245	4145433	Isolate	China	Asia

• Gene Location: Start: 135166; End: 140727 Strand: +

Full Sequence      

MKNRKLTRIIAITLTATVAATSVMPCGTVLGAQNDPVTEEAAQTTESVQESEVSESEISE
AETSENETESQTGTEAGTEKEINTEINTETGTETEIGMETENDAEIETEIETEQIELESS
DFPQIGSKVTKNTVDCETKETKSTDWELVWSDEFNEDSLDLTKWDYQSGDGSDYGVAGWG
NAEKEYYTKGENISFEDGHLVITARKENRGSSTYTSAKLWTKGNDYYNGIAKEPLYAKKY
GRIEAKMSLPEGTGYWPAFWMMPLDDAYGGWASSGEIDIMEARGRVTGSVDGTIHFGNSW
PNNKSRGGHYDTTIDPSFNFTQEHEYALEWTPGKISWFVDDQCYKTITNWYSIGSDNKEN
FTYPAPFDQEFYIMLNLAVGGNYDSGNLDDIDGGQMKVDYVRVYDLLDANGEIHDYSENE
KTVESEAAQAGGLEGGIVGKTNFLSGDLTKARKITEHAEGIEGWYLQNGTGGAANVTAAE
GGAKVSISSAGENGYSVQLMHQFPLTYGYEYELKFDAKADEARSITAQAGDFTYNFLGSW
TKYSDAFTVPLTTEWKTYTYKFDMKEFNDDYARLELNLGLTSTAGVYIRNASLVAIGLYQ
GITEDGDKEPTKGGEHIYNGTFDQGNNKDAGGAYTRLKFWNVKGNAAANVDTQRKLVLGS
GTDENAGIEQTGISLFGKDRYELTFDAAAFSGDSIRVQVKGANGTEYISETVDLTSDMQK
KKVSFTVPENVSDKTGSVSFIVGNDGKKIHIDNISLKRLTNYNVDYSQIKVYPIENGDFA
GCSGNDLKGWSTYGNPAVDVADGVCTVTAVPSGNVWDKMLIADAMQMEEGMTYELHFEQK
AERAGETYTAKIETTDGSYTVITEKQCKTTTDWTNEDITFTCNSSGVMEFKYLLAQVSGE
CKISFRNVKLNVSNAPILQMPFFYKNGVAKAEQDIVFQMHPASGTGDAWKAAEKTVTVDG
KQVEAVFDDTTMTIPAGTISEEGKYKIKISASGFDLCEWNLEVFPAGKNLVLNGNFSKGT
ASWADSYFNEGEGYPAGNLSVTESKEAKIEYKWAQNFWDLQLIQKNIPVKKGVEYKITFD
ARATVDRPVSLQIAGGLTTYKLGSRYHKYTRYFTAPENNAEIAFMLGNVAMGSLITPSDE
HTVYFDNICIEEMGAEDALTRIPEVESAGSVKLTQDAVLNLVGVNDAWNAAEKTVYVNGT
AVEKQNSKFDDDKITISGSVFHQTGNYEIVIKADGFSDTNLAFLQITSAGIQEYMTNGDF
SEGEKNWKFWAGGEPESASVRYVGGQAEINMLYPWKNQFGVYDSWGIQLSQNVLVSKDTE
YVLKFKAKSEINKKLDVDISGQKFSFDMTGDEQEFTCQFKANDEKATVGFFFGACDENTP
ENTKMWLKDVSLTKVGDETLDGVCSYQVEHYLQKNGSYVLYEKAHGAAKADTMVDAQKDG
LCRNYEGYTFAPEVNGSVVSGKASDKLVIKLFYKPNKYQIQYVMNLDADVKNPNPDAYTY
GKMVGLKAPSCDTNEFLGWYLDPEYTVLVENIEANMTGDVVLYAKWKDRENVDPEKPGDK
KPDENTPDIKKPDEKTPDTKIPDEKTPDTKKPDEKAPDSQDSGNAAVTAISLNKTKVTLN
KGKKFTLTAKITPENAANKKVVFCSGNKKVATVNAKGVIKAVGKGKTKITVKTPDGKKTA
VCTVTVKIPSKKVTMNVKEIYVVKGKKISLKATMNPIDSTDKIKWSSSKKSVVTVKNGKI
TAKKTGTAVITAKTTSGKKVTCKVHVVKKAKKSTSIKLNKKQLTMKTGGRYELKAKVKPF
NSTDIVKWKSSNKKIATVDQFGTVKAKKAGKVKITATTSSGKKVTCVIKVKKK

Enzyme Prediction     

EC	3.2.1.39	3.2.1.6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	150	404	1.8e-73	0.9956521739130435
CBM4	458	579	3.7e-28	0.9285714285714286
CBM4	1009	1127	3.1e-19	0.9920634920634921

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	8.50e-85	150	404	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	5.82e-44	148	404	1	329	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	6.42e-39	146	404	2	258	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	4.19e-37	152	404	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	2.87e-27	148	404	1	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
BBF45016.1	1.10e-239	146	1158	65	1083
ABX43741.1	2.49e-239	113	1359	36	1262
ABJ15796.1	1.14e-160	146	1311	537	1720
AGF58045.1	1.91e-157	146	1134	237	1226
AQR96735.1	2.35e-157	132	1134	221	1221

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VY0_A	6.13e-46	137	407	4	262	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]
4DFS_A	3.12e-45	137	405	9	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]
3ILN_A	3.62e-45	146	404	5	247	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
3AZX_A	9.05e-45	140	404	4	254	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]
6JH5_A	2.14e-43	146	408	4	235	Structureof Marine bacterial laminarinase [Aquimarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23903	1.60e-58	148	404	425	679	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
P45798	1.00e-43	142	404	36	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
C1IE32	2.55e-42	146	402	20	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	1.30e-34	146	417	25	265	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90	2.39e-24	143	412	53	296	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000900	0.282886	0.715670	0.000231	0.000170	0.000127

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000245_00123.