CAZyme Information: PPTG_18765-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_18765-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635		67523.38	4.0334

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669655:77003-78910(+)

Full Sequence      

MYGGNSPIGENAGERTHSNVWKDTSEEEIYGSYLGPGDAGSDVPMMRPTMAARPSTAIHQ
DIAVGQLDDTGAAGGGAAKTYTGRKVVWPGALFLLVITAGALGLITYFGVEEYNSAQTQQ
SLTESVTEVDRERKVTSVKSCLLPDYSTADGKIYATDSNTGEKEQLVFTGINWSGMENAE
GVPHGLATKQSYLDDIAANLSDNGFNAVRLPLNAQMIIDNSAPNTKLFVNSLDTDLNVDT
YIDMIKKVVQGLGKQQIGVLLDIHKIDPNFTDDTSEHLWFTDDYPIATIYKMFETLATEL
CSDLEYNIIGIDLKNEPVGGCWPADDTDEYCDSDVNWPRAVETIGNKILAICPNWLIVAE
GNYATNTVAEINGANVTYNDWYGASLQNASVNPIALKTDGKLVFAPHFYSPSVYPSSYFF
KKQSSSGDTVSVTEYPNTTEGNVLLKAAVTAVLDNAFGNAVTEVGVPTFYGEFGGIYGSA
ELLAGLTSTRVIEMLIEYANDMNMTGGFAWAINPDGSYDFNDEYKPDDPWQYGLYTSSSW
DAYHTDFATGLQNLKGSGSFPCFSKTTTVTSSGSGSTSATITTDSTTSDSSSSTAATTAT
STAASTAASGSAAATTATTATTTTTASSAATATAI

Enzyme Prediction     

No EC number prediction in PPTG_18765-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	164	516	3.3e-144	0.9941860465116279

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	8.86e-21	146	561	28	407	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	4.93e-19	180	516	11	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75347.1|GH5_20	0.0	1	572	1	575
ABL75348.1|GH5_20	0.0	1	571	1	575
UIZ24458.1|GH5_20	0.0	1	573	1	573
CCA27479.1|GH5_20	7.32e-197	14	572	14	584
CCA26601.1|GH5_20	6.52e-188	20	564	22	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	1.71e-32	146	515	8	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	2.32e-32	146	515	8	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	8.33e-32	146	515	41	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	8.33e-32	146	515	41	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	2.79e-31	146	515	41	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	2.10e-27	164	515	52	355	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	2.39e-25	143	420	621	902	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	2.62e-22	164	428	59	328	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
1.000041	0.000000

TMHMM  Annotations     

Start	End
86	108