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CAZyme Information: EFQ32556.1

You are here: Home > Sequence: EFQ32556.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Colletotrichum graminicola
Lineage Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola
CAZyme ID EFQ32556.1
CAZy Family GH3
CAZyme Description GH16 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:E3QNW8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
477 GG697363|CGC4 53065.09 5.3205
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CgraminicolaM1-001 12400 645133 380 12020
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 145 468 4.9e-117 0.9936708860759493

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
185694 GH16_CCF 2.19e-145 141 469 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 4.14e-64 144 468 5 320
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 1.39e-54 144 432 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.
185683 Glyco_hydrolase_16 6.47e-15 144 376 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.
225182 BglS 5.29e-13 239 472 104 352
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.27e-313 1 477 1 493
1.77e-267 4 477 7 484
1.98e-266 1 477 1 483
7.39e-264 16 475 25 480
7.99e-255 4 477 2 476

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.50e-21 144 419 24 238
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]
2.74e-21 144 419 16 230
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]
4.09e-18 240 430 72 229
Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
3.55e-17 144 422 11 213
Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
1.83e-15 118 419 13 242
Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 [Bacteroides ovatus],5NBO_B Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 [Bacteroides ovatus],5NBP_A Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 in complex with G4G4G3G Product [Bacteroides ovatus],5NBP_B Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16 in complex with G4G4G3G Product [Bacteroides ovatus],6VHO_AAA Chain AAA, Glycosyl hydrolase family 16 [Bacteroides ovatus ATCC 8483],6VHO_BBB Chain BBB, Glycosyl hydrolase family 16 [Bacteroides ovatus ATCC 8483]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.36e-70 118 469 3 352
Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
8.84e-37 151 465 184 487
Gram-negative bacteria-binding protein 1 OS=Drosophila melanogaster OX=7227 GN=GNBP1 PE=1 SV=2
1.75e-34 141 462 173 477
Beta-1,3-glucan-binding protein 1 OS=Manduca sexta OX=7130 PE=1 SV=1
2.95e-28 141 462 179 480
Beta-1,3-glucan-binding protein 1 OS=Galleria mellonella OX=7137 GN=bgrp1 PE=1 SV=1
6.78e-28 130 466 155 479
Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000035 0.000020

TMHMM  Annotations      download full data without filtering help

Start End
106 128