CAZyme Information: EEU46969.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU46969.1
• CAZy Family: GT31
• CAZyme Description: glycoside hydrolase family 16

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
461		51674.77	6.9076

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698897:2185584-2187022(+)

Full Sequence      

MSVDSNAHSAHPEPPNSGLRHSIEPVRGPGSAGNAGMFSIPEFSRPPSDYESSNGSGTHF
EDRNRHFHSRRVKPGEIEKPWLEKTNPKEKWVTILPILAIFIGLVGSGFLVWDGIRSVVK
NTYCPVLDEDFSGGLDSKIWTKEVEVGGYGNGQFEQTTNTDENVYVDNGNLIIKATLQDA
KLMEKNNVINLFKDGSCTSKVWSNCIASTNLTAGNNSVVPPVRSGRINTKKGATIKYGRI
EVTAKLPEGDWLWPAIWMLPVKSTYGPWPRSGEIDIIESRGNNWTYAQGGNDIVGSALHW
GPNSANDGWWKTNNKRKALHTTYSAGFNMFGLEWSQKYLFTYVNTRLLQVTYTNFKKSMW
KRGGFPDVDQNGTRLTDPWSASGELNAPFDQEFYLILNLAVGATNGWFEDGKSGKPWYDN
SPTAKRDFWEARGEWYPTWKQPQMEVSRVVITQQCNGDEEL

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	130	449	9.6e-115	0.9841772151898734

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	4.79e-137	126	453	2	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.
185688	GH16_beta_GRP	1.13e-57	126	446	2	314	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.
185693	GH16_laminarinase_like	1.11e-54	128	416	3	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.
225182	BglS	2.95e-12	134	454	53	342	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
185683	Glyco_hydrolase_16	4.38e-11	129	360	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK91160.1|GH16_4	0.0	1	461	25	485
QKD55969.1|GH16_4	1.10e-293	1	461	21	481
QPC58385.1|GH16_4	1.01e-291	2	459	25	476
QPC69776.1|GH16_4	1.44e-291	2	459	25	476
QGI65880.1|GH16_4	2.18e-291	1	461	1	463

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	5.82e-19	126	402	21	237	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]
3ILN_A	5.98e-19	130	406	14	225	Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
3AZX_A	6.33e-19	126	402	13	229	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]
2HYK_A	9.90e-17	136	416	24	231	The crystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
5WUT_A	9.58e-16	126	406	8	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.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	3.07e-66	124	447	31	346	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q9NHB0|GNBP1_DROME	5.15e-31	161	451	208	489	Gram-negative bacteria-binding protein 1 OS=Drosophila melanogaster OX=7227 GN=GNBP1 PE=1 SV=2
sp|Q9NJ98|BGBP1_MANSE	1.47e-27	136	443	185	474	Beta-1,3-glucan-binding protein 1 OS=Manduca sexta OX=7130 PE=1 SV=1
sp|P23903|E13B_NIACI	1.29e-26	126	413	426	661	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
sp|Q76DI2|BGBP_TENMO	5.44e-26	126	452	169	479	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000038	0.000001

TMHMM  Annotations     

Start	End
91	113