CAZyme Information: SPRG_11767-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_11767-t26_1-p1
• CAZy Family: GH6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
557	KK583260|CGC2	61099.40	6.2452

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

• Gene Location: location=KK583260:81795-83620(+)

Full Sequence      

MASDGYDRMSETDEHRSSFSYSQRGASSAGIDGFTRSSILDRDIVAAPVDHAVPIPPKAF
KGRIRRWPGVLLLLVMIAGSVAAIVYLAQHFRGLAQARATDVQKRLAKERSIADGTTSGS
SSGSTDIADDGQVNNPEVYPPSGCQLPNYVSKNGKLYAVAKNGTEVSFQIKGVNWFGMET
GMQAPFGLWDNDQNGTTVYEVAKFLANNKFNSVRVPLCVSSILANKPLEASIVNRVTNRA
LDLTSFLSLLQTVTQSLGYRQISVMLSMHTLDLMNHGGSLWYGSTVSEAQFLQSIDMLTE
ALCSDTYWNVLGVDVKNEPWEGTWGTGLKNDFKLGAELIGARVLKGCPKWLVFVEGVNAQ
NDVTLDGQAFAYYDWFGGGLQKAGAFPVVLPTPEKLVYAPHYYTPAVFPQYYLFGGGKVG
AGNAINGYVELSDEKLLGRVAQTMHQMFGYLNDKKDVAVVLGEFGGLYTKDAHPMKTTQR
CTDFTIQTMLNENYAGGYMWSLNPESAYQYNPADKPGHYTEGLVTDDWRSANVPFLKAMK
AMDAMKDLKMMPCFPIE

Enzyme Prediction     

No EC number prediction in SPRG_11767-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	165	506	1.2e-138	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	8.67e-22	162	550	39	398	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	4.00e-14	171	506	6	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75349.1|GH5_20	2.37e-199	25	557	107	631
ABG80555.1|GH5_20	2.77e-196	36	557	117	636
ABG80554.1|GH5_20	2.77e-196	36	557	117	636
ABC87090.1|GH5_20	1.75e-193	36	557	112	631
ABK59037.1|GH5_20	1.75e-193	36	557	112	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.34e-42	149	528	8	361	The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3W6M_A	1.85e-42	149	528	8	361	Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	6.69e-42	149	528	41	394	Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3AXX_A	6.69e-42	149	528	41	394	Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_B Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_C Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3QHO_A	2.40e-41	149	528	41	394	Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_B Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_C Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19487|GUNA_XANCP	2.01e-32	169	530	43	356	Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2
sp|P54583|GUN1_ACIC1	1.26e-30	162	532	56	381	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	7.11e-30	159	534	47	373	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P50400|GUND_CELFI	9.34e-23	170	530	63	400	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000000

TMHMM  Annotations     

Start	End
67	89