CAZyme Information: MGYG000001535_04966

Basic Information

• Species: Paenibacillus_A phocaensis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A phocaensis
• CAZyme ID: MGYG000001535_04966
• CAZy Family: SLH
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1560	MGYG000001535_39|CGC1	170985.96	4.4516

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001535	5515101	Isolate	not provided	not provided

• Gene Location: Start: 64828; End: 69510 Strand: -

Full Sequence      

MKRLMTIGLILSMMFSSFMIPGYASPTDQTEGSDIRGHWAEASLRQWSDSGILTGYLDGT
LRPDEPVTRAEFSALLQRVFGVSGTGRTAFTDVSANAWYASSLAAALQAGYITGYEDGTF
KPNRPITRAETAVMLSKAFQLSEIVGGATADVIGTFKDKSAIRTYSLNAVNELVMTGATQ
GYPDGTFRPEQFVTRSEAVTLLDRLAGKLYNSAATDERKETLTNMVINSDGVILRNKELT
GNLYFAPGIGDGDVTVENMAVAGVTFINGGGPNSIHIKNTKLANVVLARQDSPIRVVVDG
HTVIQRLILHSPATIQTAEGASIQNLELQIGSSGSIIAGNGSINRITAWEGGIKVNGQEL
EQGKALAWSPTLGTLVPVDEKKVPERTPASVTITPSPSTDGTAPPRPSEPGSSLAAQGSL
PGTTKVTTTVSSGNHLAVLVSNKVISPPQAGSPLLKSHLLTNPYTSGTDISGVDPKINKY
LGVYEVDGTDKVVKFQQIALTEANIKPEAWNMVWNDEFEDAQIDPAKWNFIQGGGGYGNE
ELQNYTNRSENARIENGHLVIEALKEKYQGNDYTSAKLTTQGKGDWTYGKFEVRAQMPRG
KGIWPAIWMMPSDEGLYSSWPASGEIDIMELLGHEPNKIYGTLHYGQPHEQSQGSYTLAD
GASFADGFHTFGVEWEPGEFRYYVDGVLYAKLNNWFSQNPLEGGEYTYPAPFDRDFFLQL
NLAVGGKWPGNPDDTTEFSQKMLVDYVRVYEREGLAYRQPVLPAAKSGVVREPGEDGNYV
ENGSFEKGLNNWVFQPFAPPANLYGGEGTVEVDNGSLKTTISQEGTVNYAIQLVQSGLPV
IKGATYRLSFDAWSTGNRTMMASLSGPDRSYTRYMEDKSVSLTDAQKTYSYEFTMNSDTD
ANARLEFNMGLAGTLPVWVDNVQLMKIKDPDPNAPREPLPSGNLIYNGTFDQGVNRLGFW
QMEGPGSADADYYVGSAINDRKLYVKPAATGQPDALLLTQDRLNLAGGKTYILSFSAKAD
TPVSIATQIGNKEQPNAYADKTYTIGTELQNYSLIFTMDSTDPSVKLHFGLGALTARLEL
DNVSLKEMSPPVEVKASKRIEAENYSDMQGVQKGDDGLSVGWIDPGDWMQYIIDVKQAGD
FKINYFVASGYDGGGSLTLRGKQGSVFTHNLPVGEIREDEADFNFTMDVANTGDWGIFKL
VEQTPTVHLGEGIYTLQLYAPHVNVDYFTLTDVNYRANTGNLIRNGTFDAGVTEWQTYQA
GDFPEKLSISAADGALRIHLPGIEENTWEQQVYQEGLTLEQGKMYTVTFDVYSTVERPIQ
LAVGTVGSPPDYEYTDFLNGNKPVIWLTDTMKQHQFSFVMTHPTNTNAKLEFDLGQMTVD
GAVYKEPGDIFFDNIRLNSSLLENGAFDESTDHWSLKLGDQWNGMASASLTSTNGELVIR
IDTFDEKAIANELNWIPQVSQTGLRLEKGKTYLFSFDARASVARKIDFGFGKSLPDEPYY
DSYFGDRASLTTEMQRYTYTFTMGKETEENAQLDLNVGMIEGIGANTEVILDNVVWIELD

Enzyme Prediction     

EC	3.2.1.73	3.2.1.6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	514	750	9.5e-89	0.9956521739130435
CBM4	778	910	9e-38	0.9920634920634921
CBM54	201	313	5.1e-32	0.9824561403508771
CBM4	1241	1375	3.8e-30	0.9920634920634921
CBM4	1401	1538	1.5e-28	0.9841269841269841

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08023	GH16_laminarinase_like	1.56e-105	514	750	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	1.51e-53	512	750	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	1.98e-44	510	751	2	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	1.27e-38	516	750	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.
COG2273	BglS	3.19e-38	508	761	39	276	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZK46087.1	0.0	2	1353	14	1373
AGK07609.1	0.0	28	1403	44	1413
AFK65343.1	0.0	20	1544	33	1581
AFH60159.2	0.0	34	1544	2	1540
AFC28172.1	0.0	20	1542	30	1589

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	3.75e-69	506	751	14	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	1.51e-68	506	751	6	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]
3ILN_A	2.44e-63	510	750	5	247	ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
2HYK_A	3.74e-63	512	751	9	243	Thecrystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
3ATG_A	3.47e-60	511	751	4	239	endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45798	1.87e-61	506	750	36	282	Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903	2.10e-49	511	753	424	682	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
C1IE32	5.94e-49	509	737	19	250	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q27082	4.34e-40	510	751	25	253	Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
Q9ZG90	7.74e-30	500	751	46	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
0.000273	0.998959	0.000247	0.000186	0.000164	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001535_04966.