CAZyme Information: CCG81819.1

Basic Information

• Species: Taphrina deformans
• Lineage: Ascomycota; Taphrinomycetes; ; Taphrinaceae; Taphrina; Taphrina deformans
• CAZyme ID: CCG81819.1
• CAZy Family: GH13
• CAZyme Description: GH16 domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
393		44799.16	6.1726

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TdeformansPYCC5710	4680	1097556	17	4663

• Gene Location: location=HE965059:33713-34894(+)

Full Sequence      

MLLGFVALFLSAYWGYSEVPKHKFREIWYEDFTSGLDLVNDWNHEIALGGYGAGTFDWTT
SNDNNSFVRDGKLYIYPTLTTWPPNIEGNSVNLTADGTCTLNTKLDCYASHNDSSFQVIN
PVQSARLTTKGKHTIRFGKVEIRVKMPRGRYLWPALWMMPQDSVYGIWPASGELDIFEGR
GNDPTKLTIQASQCMQSSAHWGPDYSQDPERQVQLSKKQTKISCWPRRSLTQDYHTYTLE
WTPQRLLFYIDSPLYVMQSITFRKGPFDGGIDSVLDSLGTPVPNPWSSSPLKAAPFDQHF
YLILNVAVGSYNGWFPEDNSDNPAYSTAHGTGGQPYEAVHDFWKSQHQWYPTWPTDLTRG
MAVDWIRMSELVDTAYWENLASARMNGRKGESK

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	32	368	7.4e-91	0.9873417721518988

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	7.40e-120	27	368	2	328	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	4.44e-50	28	325	1	226	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	6.78e-49	27	367	2	318	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.
225182	BglS	2.48e-15	33	251	26	211	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].
395585	Glyco_hydro_16	3.63e-15	132	251	28	121	Glycosyl hydrolases family 16.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFZ32377.1|GH16_4	2.58e-91	2	375	122	484
QFZ43729.1|GH16_4	2.58e-91	2	375	122	484
QFZ49406.1|GH16_4	2.58e-91	2	375	122	484
QFZ38046.1|GH16_4	2.58e-91	2	375	122	484
QFZ26709.1|GH16_4	2.58e-91	2	375	122	484

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	8.92e-29	16	323	7	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	3.66e-28	17	323	3	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]
2HYK_A	3.91e-21	27	323	10	231	The crystal structure of an endo-beta-1,3-glucanase from alkaliphilic Nocardiopsis sp.strain F96 [Nocardiopsis sp. F96]
3ATG_A	1.71e-20	27	323	6	227	endo-1,3-beta-glucanase from Cellulosimicrobium cellulans [Cellulosimicrobium cellulans]
2VY0_A	2.70e-20	18	324	7	249	The X-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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	6.63e-59	29	374	34	364	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|C1IE32|E13B_CRYAT	1.34e-30	28	326	24	255	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
sp|Q0E666|BGBP1_GALME	4.01e-28	30	371	183	490	Beta-1,3-glucan-binding protein 1 OS=Galleria mellonella OX=7137 GN=bgrp1 PE=1 SV=1
sp|P23903|E13B_NIACI	8.29e-27	27	324	426	669	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
sp|Q9NL89|BGBP_BOMMO	4.35e-26	56	368	213	492	Beta-1,3-glucan-binding protein OS=Bombyx mori OX=7091 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.351963	0.648032	CS pos: 17-18. Pr: 0.4226

TMHMM  Annotations     

There is no transmembrane helices in CCG81819.1.