CAZyme Information: PPTG_03844-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_03844-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
582		64069.00	4.3291

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=KI669566:494563-496311(+)

Full Sequence      

MAEAAEISRPMVGSMSGAPVSGSTFRNSEYTREAMESSRLTESGGRESAMYGPGGQRQTE
MKLMAVEPDLGAAPERTKDYKGRIRTWPGLLLLLAIVAAAVALITINAIDVQDQANINAQ
RYENAAQNRRKIKDGLDDDNVIVSDDGQVGNPKKYPDMGCELPDYQSKNGQIFAVAKNGT
EVPVGIKGLNWFGMETGLAIPFGLWENMDNGTSVYEVAAFLARNKFNSVRLPVCIKNILK
DVAPDKSLINLNTNRAINITSYITTIQTIVEALGYRHITVMISLHTLDPKKSGGAWFSED
LGVSEDDFLDAVDILTKNLCKSRYWNILGLDLKNEPHECSWGGEDPDWQKGATLIGNRML
EGCPNWLAFVEGIASKGTITLNGEENTYFDWWGGGLADAGGDPITFDVENKLVWAPHYYN
TGVSPAWYLYASGTQNAEGAREDYVELDDDTLRNNVEKTMDKMFGYLVTSDPNTAMVMGE
FAGLYGKDAHPMKTTKRTTDFTIEVMVKAGYAGGYMWSLNPESAYQYNPADTYGTFTEGL
LEDDWLTPNKAFVEGMAALDDIKDLKMFPCFEVEVESDAGSE

Enzyme Prediction     

No EC number prediction in PPTG_03844-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	181	523	9e-151	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	2.17e-14	169	528	32	371	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.57e-04	216	483	28	238	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75351.1|GH5_20	0.0	1	582	1	582
ABL75350.1|GH5_20	0.0	1	581	1	583
ABC87086.1|GH5_20	0.0	3	582	2	583
ABJ97692.1|GH5_20	0.0	1	582	1	582
UIZ24403.1|GH5_20	0.0	1	578	1	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.91e-37	165	547	8	363	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	2.63e-37	165	547	8	363	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	8.17e-37	165	547	41	396	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	1.12e-36	165	547	41	396	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	3.89e-36	165	547	41	396	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|P54583|GUN1_ACIC1	1.02e-28	165	547	46	379	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	6.33e-28	165	582	39	397	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P19487|GUNA_XANCP	8.24e-27	184	545	42	354	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|P10474|GUNB_CALSA	8.81e-19	183	437	644	909	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000030	0.000001

TMHMM  Annotations     

Start	End
87	109