CAZyme Information: PHYSODRAFT_495307-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_495307-t26_1-p1
• CAZy Family: GH81
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
581		64179.95	4.3585

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159153:8499206-8500951(+)

Full Sequence      

MAEVSRPMMNRESVEGSSTSYSENYSSGHFSLHLDSSQGPRPTESGGRVSSVYGGQRQTE
MKLKAADIDLAKPERKKDYKGRIRTWPGLLLLLLIIGGAAAIIVLQAKETSDLITVNREN
YEQRLANKRKIQDGKEDDQVIISDDGQVGNPKSYPDMGCELPDYQSKNGQIVAVSKNGTE
VPVAIKGANWFGMETGLAIPFGLWENMDNGTSVYEIAAFLARNNFNSVRLPVCIKNILND
AAPEKSLVNVQTNRALNITSYITTIQSIVEALGYRHVSVLISLHTLDPKKSGGAWYSDEL
EVTEDDFLSAVDILTKNLCGSKYWNILGLDLKNEPYDCSWGGDDPDWQKGATLIGNRMLE
GCPNWLAFVEGTAGSGTISLNGEEDRIYYDWWGGGMEKAGDNPITFDVESKLVWSPHYYN
TGVSPAWYLYASGTQNAEGGLDGYVELDDDSLRTNVEKTMDKMFGYLIGADSNIAMVMGE
FAGLYSKDKHPMLTTKRTTDFTIEVMLKAGYAGGYMWSLNPESAYQYNPADTYGTFTEGL
LEDDWLTPNKVFMEGIAALDVMENLQLFPCFPQEVEGSSSE

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_495307-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	180	523	1.4e-146	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.40e-13	177	553	39	384	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	4.58e-08	215	483	28	238	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC87088.1|GH5_20	0.0	1	581	1	581
ABG76934.1|GH5_20	0.0	3	581	2	577
UIZ24396.1|GH5_20	0.0	4	581	41	618
ABC87086.1|GH5_20	0.0	2	576	4	577
ABL75350.1|GH5_20	0.0	2	580	5	580

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	3.28e-36	164	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	4.49e-36	164	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	1.34e-35	164	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	1.83e-35	164	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	6.33e-35	164	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	1.44e-31	164	551	46	383	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	1.37e-28	164	550	39	372	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	1.16e-18	174	437	638	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
1.000051	0.000000

TMHMM  Annotations     

Start	End
85	107