CAZyme Information: MGYG000003192_01039

Basic Information

• Species: UBA5416 sp900539175
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA5416; UBA5416 sp900539175
• CAZyme ID: MGYG000003192_01039
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1155	MGYG000003192_15|CGC1	127459.31	4.2883

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003192	4033193	MAG	United States	North America

• Gene Location: Start: 49069; End: 52536 Strand: -

Full Sequence      

MLKKSRMAAGMLVAFLCAALAAAPVSAAENPVQEPNISVTTDKSVYSEKENITETVTIET
PDGCSLTDVEIRAQIPEKYVTEDGKEAPKEWISSIPEVAGGSASETKIVFIRKNNDPNGK
PNGDQNGKPNGDQNGKPNGVQNGNKGNSSATGNHTAPKTGDSSHVMLWMCMILVSAVLIV
LLVKKKKGKEICSLLLSVVLLGGLVQNRGLFVYAAESETEQKTVTLNREITVDGKQVILS
VKVTYKVSPVKTPDEEENRLSYEGYNLKWQDEFDGTVLNREDWNVELHAPGWVNAELQEY
VDSEENIYLKDGKLVLKPIKTVNEDGEVSYTSGRINTQNKHNFKYGIFEARVKVPEGKGY
LPAFWLMAADENQYGQWPRCGEIDIMEIHGSDTSKNYGTIHYGNPHKESQGSYQLNEGEG
TYADDYHTFAVEWLPGRINWYMDGKMFHTENNWYSRTEGQGEITYPAPFDQEFYMILNLA
VGGSWVGYPDETTDFENAAYEVDYVRVYQKDSYDENVSKPETPKPVLRDPDEEGNYIING
DFTVAEDLEDGKDWEFLTALGGEATAEIKDGRILIKTGNAGTADYSVQLVQPNLPIQKGG
TYQVSFDAWADEARTMSVALTAPDNSYVRYLPDTTVGLTSEKQTYTYEFTMTQNDDANGR
MEFNLGNTASTANVYITNVTLKKTAQADVSTEDKKTVRSDGNYVYNGSFQEGANRLEYWE
IASDNAEVAVTGLEDGRRLKVTAPEGTTPEHPVVISQSELAMIAGAEYAMSFEAQGDAGK
SIQATVAGQSFDAAVSGEKASYLYKFAMPAVGEGNNNLVFTISQPGTYYLDEIRIVEDVL
IKNGSFNAGFAGYEPYVDGTAKASYTVDSLTEENAASYTIENTGDADWKIQLKQNNVELE
QGQWYRLTLDAKSNIERKLMFAIQRDGSRHNDDWTPYTQVTVDLTNDYQTFKSEFQMKEP
TDPESVLSISMGAVGGTQITNQHQIVIDNINLEKIDAPAIEEKPAGENILKNPDFSARAD
GWENAVTAPGEAAVSFEENKAVYNIANVGTADWNVQLKQNGITLEQGSTYKVAFKAHSTL
GRTIKLAFLTASYDWYGGADISLTENETKEVELEFAVDKDTDTNMTMVVSMGVIEGQETP
TSTVTLSDFSLVKIS

Enzyme Prediction     

No EC number prediction in MGYG000003192_01039.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	269	508	7.8e-78	0.9956521739130435
CBM4	535	666	3.2e-36	0.9920634920634921
CBM4	840	972	2.2e-30	0.9841269841269841
CBM4	1008	1132	1.8e-26	0.9920634920634921

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	4.42e-91	269	508	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.
cd02182	GH16_Strep_laminarinase_like	2.55e-51	264	509	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.
cd08024	GH16_CCF	1.80e-50	269	509	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.
cd00413	Glyco_hydrolase_16	3.42e-36	271	508	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	5.44e-31	271	508	5	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	27	1153	24	1220
QWT52878.1	0.0	1	1154	1	1135
QQQ91210.1	0.0	28	1153	27	1152
ASU30685.1	0.0	28	1153	27	1152
ANU77877.1	0.0	28	1153	27	1152

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	3.31e-58	256	509	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]
3AZX_A	1.33e-57	255	509	2	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	6.96e-55	265	508	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	8.84e-54	266	525	4	255	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2HYK_A	1.21e-51	267	509	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	1.03e-52	264	510	422	681	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	6.80e-44	267	506	22	265	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
P45798	2.63e-37	265	509	40	283	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
Q27082	3.45e-34	265	509	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90	8.11e-28	265	509	56	288	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000291	0.998977	0.000178	0.000186	0.000169	0.000150

TMHMM  Annotations     

start	end
7	29
164	183
190	212