CAZyme Information: KAF6516171.1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: KAF6516171.1
• CAZy Family: CE1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	CM024371|CGC1	42909.02	7.5042

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo5176	17912	660025	0	17912

• Gene Location: location=CM024371:2678683-2681401(-)

Full Sequence      

MSQTVGGTPAGTGDVAQSPTQSSLKKRFPPRPYFHSRRVKKGTVERPYLAVRDPRDIWIT
VIPALGVVVGLAAIALLSWSGYRSVDKHEYCKVFTDDFSNGFNSTIWNKQVEVGGYGNGE
FALTTDTDENVFVRDGQLIIKPTLQTDKFLSETTKINLTADGTCSSTTTQDCVQVANLTA
GEIVAPVKSGRITTKNFGVIRYGRVEIVAKLAAGDWLLSQLMMFPAKEYYGAWPASGEID
IGMVRGNNYTYDNGRGNQQVSSQLHWGLDTSTDRWQSTSGVRNALLTTFNRDFHTFGLEW
SDKYLFTWLDHRIAQVTYVKFNHPFYQHGGFHQALANGSQISDPWSGPGTSNATPFDRPF
YLIIALAVGGTSGWFPDDVHGSTSQVNSS

Enzyme Prediction     

EC	3.2.1.39:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	96	380	2.6e-91	0.8670886075949367

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185694	GH16_CCF	5.87e-100	93	389	2	295	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	2.89e-46	93	382	2	279	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	6.67e-35	94	378	1	219	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	2.64e-08	178	357	44	203	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	5.85e-07	189	356	105	255	Beta-glucanase, GH16 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD62180.1|GH16_4	1.76e-262	15	381	35	406
QGI99505.1|GH16_4	3.44e-261	15	381	35	401
CCT73009.1|GH16_4	3.44e-261	15	381	35	401
QGI68615.1|GH16_4	3.44e-261	15	381	35	401
QIX00326.1|GH16_4	2.78e-133	15	381	45	410

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DFS_A	3.80e-12	93	378	21	246	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	4.02e-12	93	378	13	238	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	1.05e-11	189	373	72	225	Chain A, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
4BQ1_A	2.22e-10	93	379	14	246	Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans],4BQ1_B Crystal structure of of LamAcat from Zobellia galactanivorans [Zobellia galactanivorans]
4BOW_A	9.83e-10	93	379	14	246	Crystal structure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BOW_B Crystal structure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose [Zobellia galactanivorans],4BPZ_A Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans],4BPZ_B Crystal structure of lamA_E269S from Zobellia galactanivorans in complex with a trisaccharide of 1,3-1,4-beta-D-glucan. [Zobellia galactanivorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8N0N3|BGBP_PENMO	3.37e-39	91	379	31	311	Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1
sp|Q0E666|BGBP1_GALME	2.77e-22	93	377	180	445	Beta-1,3-glucan-binding protein 1 OS=Galleria mellonella OX=7137 GN=bgrp1 PE=1 SV=1
sp|Q76DI2|BGBP_TENMO	2.41e-20	92	370	168	430	Beta-1,3-glucan-binding protein OS=Tenebrio molitor OX=7067 GN=GRP PE=1 SV=1
sp|P23903|E13B_NIACI	9.25e-20	108	370	450	654	Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
sp|C1IE32|E13B_CRYAT	3.80e-19	96	370	26	238	Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999814	0.000197

TMHMM  Annotations     

Start	End
57	79