CAZyme Information: FOXG_22849-t26_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOXG_22849-t26_1-p1
• CAZy Family: GT64
• CAZyme Description: endo-1,3(4)-beta-glucanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362		40142.73	5.0086

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum4287	21354	426428	429	20925

• Gene Location: location=CM000594.1:4305312-4306400(-)

Full Sequence      

MFCTYVQIWLASTSDPMGDICTSRSPRDLTHIIFLFFTIWMTIDRMRIICLAIASTAMIR
GINVSAQYTLSNRIDSSNFFNSFDFFDEEDPTHGFVEYVDSTTAKSQGLARVSGNGIYLG
VDYKTENPPNGRKSVRIHSQKSFTHGLFIADITHMPGSIPGVWPAFWMFGPDWPFSGEID
IIEGVNTQTHNGMYLHTGPGCIVNNEGSDQSTLQIGDDCNAPGGCGQITSRSQNYGNGFN
SVKGGVYATEWTSEYIAVWFFQRGSVPSDIRTGHPDPTSWGPAAARFNGGDGCHLDDHFK
EHRIVFDTTFCGDWAGSPGIWDSNPETAALGDCKTYIASNPSHLREAYWLIKSIEIYQEP
RA

Enzyme Prediction     

No EC number prediction in FOXG_22849-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	107	337	8.9e-82	0.9868995633187773

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185690	GH16_fungal_Lam16A_glucanase	1.80e-140	90	358	24	293	fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).
185693	GH16_laminarinase_like	7.84e-16	134	325	66	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.
395585	Glyco_hydro_16	5.64e-07	106	181	2	67	Glycosyl hydrolases family 16.
185691	GH16_Strep_laminarinase_like	1.01e-06	161	215	106	169	Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
185694	GH16_CCF	1.19e-06	163	288	130	263	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK89177.1|GH16_1	5.47e-158	46	357	1	314
CCT65987.1|GH16_1	3.71e-153	51	357	6	319
QGI62169.1|GH16_1	3.71e-153	51	357	6	319
QKD51241.1|GH16_1	1.60e-151	63	357	22	319
CZS72629.1|GH16_1	2.01e-148	51	359	6	324

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WDU_A	1.85e-88	77	357	12	295	The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_B The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_C The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_D The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila']
3WDT_A	1.91e-88	77	357	13	296	The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_B The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_C The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_D The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDV_A The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_B The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_C The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_D The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila']
3WDY_A	1.44e-87	77	357	11	294	The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_B The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_C The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_D The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila']
3WDW_A	1.54e-87	77	357	13	296	The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDW_B The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDX_A The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'],3WDX_B The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila']
5JVV_A	2.55e-83	67	357	2	297	Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'],5JVV_B Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila']

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AJR9|EGLX_ARTBC	7.44e-84	65	362	17	319	Endo-1,3(4)-beta-glucanase ARB_04519 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_04519 PE=3 SV=1
sp|A1C7B5|EGLX_ASPCL	1.13e-79	51	358	18	328	Probable endo-1,3(4)-beta-glucanase ACLA_073210 OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=ACLA_073210 PE=3 SV=1
sp|B0XTU6|EGLX_ASPFC	1.14e-78	65	358	29	327	Probable endo-1,3(4)-beta-glucanase AFUB_029980 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=AFUB_029980 PE=3 SV=1
sp|Q4X084|EGLX_ASPFU	1.14e-78	65	358	29	327	Probable endo-1,3(4)-beta-glucanase AFUA_2G14360 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_2G14360 PE=3 SV=1
sp|A1DHY9|EGLX_NEOFI	1.56e-78	65	358	29	327	Probable endo-1,3(4)-beta-glucanase NFIA_089530 OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=NFIA_089530 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.989904	0.010091

TMHMM  Annotations     

There is no transmembrane helices in FOXG_22849-t26_1-p1.