CAZyme Information: EPrPAT00000020508-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000020508-p1
• CAZy Family: GH72
• CAZyme Description: Cell 5A endo-1,4-betaglucanase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635		68442.65	5.0146

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0361:2651-4621(-)

Full Sequence      

MYQHSPVGRTDSMVSDPAPTPQGNIWKDTTDGELYGNYLDTASHASDMQLRPTMGAMNRN
TLAGGGAGGHPDITVGLLEEDTDGARGSGAKKEYTGRKRVWPGAVFLLLIVLAGSGAIAY
FGIQTYNDAQEQQKISQEFITPVVTKKATLKVCRVPNYVTDKTKLYATAGTEKHEVHFTG
INWSGMENVEGVPHGLAAGQSNLEDIAQKLADMEINAVRLPLNAKMVLDDSAPDTTDFVT
RVQAELYGVSTYIDMIKKIVQGLARKQIAVLLDLHKIDPAYKESTSEELWFTSDYSEGDI
ITMFETLAKQLCNEQHYNIIGVDIKNEPVGGCWPAKDTDAYCPKAKNWPRAVERIGNAIL
KVCPNWLIVAEGLYATNMVAEFNGKNATYSDWFGASLQNATKNPIKLNTPNKIVYAPHFY
SPSVYPSAYFFASQSSAASGAVTVEEYPNTAAGNASLKAAVDSVLDNAFGELLATGTAPV
FYGEFGGIYGSKELLKGKTSSRVIDFLIQYAEDKGMIGGFSWALNPDGNYDFNDEYVGYK
GSGKKPWEFGLYADSKWDDYNTDYARGLRALKGNGIIPCFARTVTVGSESGSGSTAVGDT
TTTTATNKTTTATTANTTTTGTDSSGSSAATIAKL

Enzyme Prediction     

No EC number prediction in EPrPAT00000020508-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	173	528	5e-136	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395098	Cellulase	7.98e-20	190	528	11	272	Cellulase (glycosyl hydrolase family 5).
225344	BglC	1.04e-18	163	532	33	372	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75348.1|GH5_20	1.81e-229	4	588	5	575
ABL75347.1|GH5_20	9.93e-226	4	590	5	576
UIZ24458.1|GH5_20	1.18e-214	14	596	6	578
CCA27479.1|GH5_20	1.60e-211	25	590	20	585
CCA26601.1|GH5_20	6.89e-198	21	581	18	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	1.25e-37	172	527	24	349	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]
3VVG_A	1.71e-37	172	527	24	349	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]
2ZUM_A	7.42e-37	172	527	57	382	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	1.01e-36	172	527	57	382	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	3.48e-36	172	527	57	382	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|P23548|GUN_PAEPO	4.85e-34	141	527	26	355	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	8.44e-33	176	527	62	365	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P10474|GUNB_CALSA	2.49e-21	176	431	645	902	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	8.84e-19	175	430	60	316	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
1.000035	0.000009

TMHMM  Annotations     

Start	End
100	122