CAZyme Information: RQM15554.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM15554.1
• CAZy Family: GT1
• CAZyme Description: Cellulase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A3M6VJD8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
651	QKXF01000152|CGC1	69886.47	4.6439

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=QKXF01000152:66048-68003(-)

Full Sequence      

MYGANASNTGERTNSNVWRDTTEEEIYGSYLGPMANNTGSEIPIMRPTMTARPSGSTHHD
IAVGQLDDIGETTAGGPVKTYSGRKVVWPGAVFLLFVTAAALSLIAYFGVQQYTAAQLQQ
SLTESVTEVDRNRRSKSIKSCLLPDYITLDGKIYAKNSNTGEKEPIVFTGINWSGMENVE
GVPHGLATKQSYLDDIAANLSDSGFNAVRLPLNAQMIIKNSAPNTKLFVNSLDTDLNVET
YIDMIKKIVQGLGKQQIGVLLDIHKIDPKFTADTSEHLWFTKEYPIATIYKMFETLAMEL
CSDLEYNIIGIDLKNEPVGGCWPEDDTETYCDPDINWPRAVETIGNKILAICPNWLIVAE
GTYAVNTVAEINGKNVTYNDWYGASLQNASVNPIVLDTKGKLVYAPHFYSPSVYPAGYYF
QKQSSSGDTVSVTEYSNTTEGNKLLKAALTSVLDNAFGNAVTKAGVPTFYGEFGGIYGAA
ELLAGMTSTRTIEMLIEYANKMNMTGGFAWAANPDGSFDFNDVYKPDDPWQYGLYTDSTW
KKFHTDFATGLKNLRGSGSFPCFSKTTIVTTSGSDSKAATTTLDSAGGNPTGTGTSKTTV
PTAATTTTLAPPGAAPTTAIAPPATVPTTATTPPVAAPATAITPATATTAL

Enzyme Prediction     

No EC number prediction in RQM15554.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	164	516	2.4e-141	0.9941860465116279

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.81e-19	160	561	39	407	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.61e-17	187	516	24	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ24458.1|GH5_20	0.0	1	600	1	600
ABL75348.1|GH5_20	0.0	1	570	1	574
ABL75347.1|GH5_20	0.0	1	572	1	575
CCA27479.1|GH5_20	3.18e-197	3	565	6	577
CCA26601.1|GH5_20	3.83e-183	17	563	22	564

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	1.60e-33	153	515	15	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	2.18e-33	153	515	15	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	8.17e-33	153	515	48	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	2.03e-32	153	515	48	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	6.79e-32	153	515	48	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|P54583|GUN1_ACIC1	8.92e-29	165	531	61	378	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	5.55e-27	168	413	56	279	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	3.50e-25	148	420	625	902	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	8.15e-21	145	428	44	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
1.000044	0.000003

TMHMM  Annotations     

Start	End
86	108