CAZyme Information: APA09855.1

Basic Information

• Species: Sclerotinia sclerotiorum
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
• CAZyme ID: APA09855.1
• CAZy Family: GH2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
453		50500.95	6.8470

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70	11368	665079	238	11130

• Gene Location: location=CP017818:1965298-1966714(+)

Full Sequence      

MQRATSQVTVSKSTPQSEENSRAQTPVGTSNPFATPPYSRPASTIGARSGFQYAEVPGTG
YFRSRRVRKADAVPLPINKKSKKEALLWVFPLCGLVLGLGLTGLIIYLKIASITRHKYCP
VLSEDFSSGTLDPNIWTKEVQVGGFGNGQFEQTTTDAENLFIQDGQLYIKPTIQDASLIT
TNSIINLTADGTCTTMSNVFLNCVTSTNTTNGTIVQPAKSARINTKLGATIKYGRVEVKA
KLPKGDWLWPAIWMLPVEDTYGAWPQSGEIDIMESRGNNYTYSLGGNNFVFSSLHWGPDE
ASDAYKKTTNVRAALHSEFGDDFHLYGLEWTEKYVFAYIDNTLRQVMYWPFKKPLWQQGN
FPLSDANGTAIVDPWSQTGRKNTPFDQEFYLILNVGVGAQNGWFLDGADGKPWVDGSPSA
KLDFWKARNEWLPTWEKNGQMIVDQVQMWQQCD

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	125	449	2.6e-114	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	4.08e-141	121	450	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	2.61e-63	121	449	2	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.
185693	GH16_laminarinase_like	1.94e-54	123	415	2	230	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.
185683	Glyco_hydrolase_16	6.93e-15	200	343	39	164	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.
225182	BglS	4.59e-14	220	385	105	255	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA09855.1|GH16_4	0.0	1	453	1	453
CCD33799.1|GH16_4	0.0	1	453	1	453
ATZ49740.1|GH16_4	0.0	1	453	1	453
QSZ29479.1|GH16_4	6.18e-314	1	453	1	453
QSZ36651.1|GH16_4	1.98e-199	31	453	50	471

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	5.09e-27	121	398	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]
3AZX_A	5.65e-27	121	398	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]
3ILN_A	6.55e-20	220	398	72	221	Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A	4.23e-19	211	402	53	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.]
4BQ1_A	1.83e-17	121	402	14	235	Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans],4BQ1_B Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	8.80e-71	119	449	31	359	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q9NHB0|GNBP1_DROME	2.95e-30	162	448	213	489	Gram-negative bacteria-binding protein 1 OS=Drosophila melanogaster OX=7227 GN=GNBP1 PE=1 SV=2
sp|Q76DI2|BGBP_TENMO	4.79e-30	121	448	169	478	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1
sp|Q9NJ98|BGBP1_MANSE	6.97e-30	121	449	174	485	Beta-1,3-glucan-binding protein 1 OS=Manduca sexta OX=7130 PE=1 SV=1
sp|P23903|E13B_NIACI	3.78e-26	121	398	426	653	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000000

TMHMM  Annotations     

Start	End
86	108