CAZyme Information: EAQ90121.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ90121.1
• CAZy Family: GH5
• CAZyme Description: GH16 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q2H3M5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
481	CH408031|CGC2	53470.82	6.2605

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408031:4422467-4423967(+)

Full Sequence      

MDNGDYFGRPAANMPSMASTAAPTPQRPGTPSESLGRNPFGDGVESQASQRSGNNGNPFV
SPSVSRPASSFDSASALGRFDGGQRYFHSRRVRKGEVEKPWTKQVDPKEKWVTILPIIGI
IIGLGISGFLVWDGIRSVVKHNYCLVLEEDWSNGFNEKVWKKEVQVNGFGNGEFEQTTPG
NENVFIENGNLVIKATPRDDALMQKDTKIDLLKDGTCTSTSPTSCIAYTNITAGNSSIVP
PVLSGRINTSPGATIKYGRVEVTAKLPAGDWLWPAIWMMPLENKYGPWPASGEIDIVESR
GNNYTHPQGGNNIISSALHWGPTPGNDAWWRTNVKRQALHTTYASGFNTFGIEWSQKYLF
TYVNSRLLQVLYVNFDEPMWGRGNFPVQDSNGTRVEDIWGHTGRAQTPFDQPFFLILNLA
VGGTNGWFEDNVNGKPWLDASPNARKDFWQAKDRWLPTWTQPQLEVSKVMMWQQCDGNED
L

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	154	472	7.5e-112	0.9841772151898734

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	5.00e-136	145	473	1	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.
185693	GH16_laminarinase_like	1.54e-55	152	436	8	224	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.
185688	GH16_beta_GRP	2.63e-55	145	472	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.
185683	Glyco_hydrolase_16	2.38e-12	240	380	51	178	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.
185691	GH16_Strep_laminarinase_like	1.56e-11	168	444	32	249	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO61198.1|GH16_4	0.0	2	481	3	485
AEO64879.1|GH16_4	0.0	1	481	1	483
CAP65600.1|GH16_4	3.69e-265	5	479	6	479
CDP31594.1|GH16_4	3.69e-265	5	479	6	479
VBB84845.1|GH16_4	3.69e-265	5	479	6	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	1.90e-19	151	436	22	251	Structure of 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	2.07e-19	151	436	14	243	Crystal structure 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	1.66e-18	244	426	72	225	Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A	2.29e-18	244	426	69	213	Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
2HYK_A	1.73e-17	160	423	28	218	The crystal 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
sp|Q8N0N3|BGBP_PENMO	1.27e-57	144	468	31	347	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q9NHB0|GNBP1_DROME	8.78e-33	186	469	213	487	Gram-negative bacteria-binding protein 1 OS=Drosophila melanogaster OX=7227 GN=GNBP1 PE=1 SV=2
sp|Q9NL89|BGBP_BOMMO	5.98e-28	158	461	199	481	Beta-1,3-glucan-binding protein OS=Bombyx mori OX=7091 PE=1 SV=1
sp|Q76DI2|BGBP_TENMO	7.11e-28	146	469	169	476	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1
sp|Q9NJ98|BGBP1_MANSE	8.61e-27	158	471	187	478	Beta-1,3-glucan-binding protein 1 OS=Manduca sexta OX=7130 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000065	0.000000

TMHMM  Annotations     

Start	End
111	133