CAZyme Information: H257_07686-t26_2-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_07686-t26_2-p1
• CAZy Family: GH3|CBM13
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		52815.97	6.4169

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913129:636660-638507(-)

Full Sequence      

MWPGLLLLVLVVGGAIAGITLGVKSSHEASRKRAIDVLSAERARRAIDSGVKDSSSSLPI
DRDPDDNQVGNPKTYVNQRCSMLNYVSKTGRVFAVLPNNTETQIDMKGINWFGMETGNAI
PLGLWTNENNGTTAYEIATYLAANKFNVVRLPVCIAHILADTAPRKGLVNLKENRAVDIS
SYMAALESIIKALAYRNIGVLISLHTLTPQVSGGTWFDDSVGITKDKFLLSVDILTKALC
KSDYWNVVGLDLKNEPHTATWADFSDGAETIGNRMHAGCTNWLAFVEGTNIEKHSTVIGG
VVTEYSNWWGGGLQGVKTKRVMLDLPNKVVYAPHYYNSGVYPQTYLYAPGGDELSDADLR
QRISETATDMFGFIAADKKEALVLGEFAGLYATDAHRFKTTKRTTDFLIEVMLRDGYAGG
FVWSLNPESAYQYNPNGPGTWTEGLLKDDWRSSNTEFVQGMAALDKLPSLKALPCVHTTP
SAP

Enzyme Prediction     

No EC number prediction in H257_07686-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	101	429	3e-128	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.62e-20	97	434	38	371	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.86e-14	123	429	17	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75350.1|GH5_20	2.68e-174	2	475	89	572
ABL75351.1|GH5_20	5.76e-173	2	475	87	570
ABC87086.1|GH5_20	7.79e-171	2	475	88	571
ABJ97692.1|GH5_20	5.60e-169	2	475	87	570
ABC87087.1|GH5_20	3.76e-168	2	475	95	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	9.19e-37	96	450	20	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	1.27e-36	96	450	20	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	3.72e-36	96	450	53	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	5.11e-36	96	450	53	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	1.82e-35	96	450	53	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	1.33e-31	90	452	21	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|P23548|GUN_PAEPO	2.05e-24	108	454	58	371	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	4.17e-24	98	455	58	382	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P10474|GUNB_CALSA	1.93e-21	106	458	647	1006	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P27033|GUNC_CELJU	1.40e-10	110	430	307	708	Endoglucanase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=celC PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.951178	0.048838

TMHMM  Annotations     

Start	End
5	23