CAZyme Information: RQM13481.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM13481.1
• CAZy Family: GH5
• CAZyme Description: Cellulase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A3R7XTX1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
514	QKXF01000255|CGC1	57420.49	6.5086

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000255:11077-12637(+)

Full Sequence      

MAETHEISRPLMDRVHSTYRNSDYTHEVMDSSRLTDSGAQRDSFVYGNGPGGQRMTEMKL
LAVEPDLGAAPERTRDYKGRLRTWPGVLFLLLLVAGAVTLITINAMTVSNKTKVNDERYE
NRKRLSRKIKDGLNDDHVLISDDGQIGNPKKYPDMGCELPDYQSKKGKVYAISKNGTEVP
IGIKGLSWFGMESGLAIPFGIMGKHEQWDIGLRDSGFFVSVRLPVCITNILKNTAPEKSL
INMDTNRAINITSYITTIQTIVQALGYRKISVMLSLHTLTPRIQGGAWYSKKLGVTQDEY
LSAVDILTKNLCGPKYWNILGLDLKNEPYECTWGGKAPDWQKGSTLIGNRMLEGCPNWLG
FVEGIASQGTITLDGIEKTYFDWWGSGLADAGSDPPTFDVKNKLVYAPHYYNPGVDPAWY
LYASGTREKTGALEDYVELDNKTLKNNIEKTMEKMFGYLLTENPTSALVMGEFAGLYSKD
AHPLLTTKRTTDFQIELMLEADYAGAYMWSLNPV

Enzyme Prediction     

No EC number prediction in RQM13481.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	178	513	9.9e-127	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.48e-09	175	513	39	361	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	3.75e-06	212	475	33	238	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ24403.1|GH5_20	0.0	1	513	1	518
UIZ24397.1|GH5_20	0.0	1	513	1	518
ABC87086.1|GH5_20	1.00e-279	3	513	2	522
ABL75350.1|GH5_20	1.04e-279	1	513	1	523
ABL75351.1|GH5_20	1.66e-273	1	513	1	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	7.25e-32	162	513	8	348	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	9.94e-32	162	513	8	348	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	2.45e-31	162	513	41	381	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	6.19e-31	162	513	41	381	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	2.13e-30	162	513	41	381	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	6.64e-21	162	475	39	320	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	4.38e-14	180	475	644	937	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
1.000053	0.000009

TMHMM  Annotations     

Start	End
86	108