CAZyme Information: EPrPRT00000018385-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000018385-p1
• CAZy Family: GH35
• CAZyme Description: Glycoside hydrolase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
534		58553.23	6.5674

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC00725:11476-13238(+)

Full Sequence      

MAVRRVLLASSTALLALATPTLAKLECRQPNYVTHDGKIWAQDPHTPGTETEVTIRGVAW
SGMEKENMIPDGLWDSTKRSQTGIQGTKVSKLLEFLGNNSINSVRLPLSAQYLIQNPMPQ
LAYINGWENKELSTWTNPNAVTYFDLVGRVVQTLQNQRVSVLLDIHLLDKYLQDAFWYTA
PYVEIGKSPTYQAAEYLAKAFCNATYWNILGIDLKDEMSDVQWSASAADANPKNDWASAA
TTIANRVLELCPSWLVFVGGASSPTTAQGFTLPDYKTPSRHWDGGNLHNATKRPLNMTVA
NKIVFAPHAHAHGKLPQNYFYGTDVNCTKDSPTDYFGFEDDQLNMECVDFVNGAKVKSKM
QCSTTEYGCSTYKHITGAQIATNYKKVMDEAMGDVLKEAKTPVILGSFSGVYGAAVQPHQ
TAALDFLIDYAATTLRGGYFYALNPDTEYYLEDSTNNGSGLFGKTHYGLFKTTSWQEPNT
DLLEALKKLPASAIPCYGGKNTGKGGMQSAASATRTNLLVAIGSFVAAAMVYAM

Enzyme Prediction     

No EC number prediction in EPrPRT00000018385-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	50	346	5.8e-69	0.7994186046511628

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.58e-10	41	458	33	379	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	6.49e-06	101	337	38	222	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA26601.1|GH5_20	9.48e-62	19	501	137	568
ABL75348.1|GH5_20	6.93e-58	27	497	145	567
ABL75347.1|GH5_20	7.65e-57	27	497	144	566
ABG80550.1|GH5_20	7.87e-57	27	505	163	582
ABG80551.1|GH5_20	7.87e-57	27	505	163	582

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	2.83e-21	46	320	21	276	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	5.90e-21	46	320	54	309	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	5.90e-21	46	320	54	309	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]
3QHM_A	5.90e-21	46	320	54	309	Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_B Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_C Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
3W6M_A	6.92e-21	46	320	21	276	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	6.80e-17	45	320	40	285	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	7.85e-17	53	321	645	902	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	4.67e-12	49	320	57	316	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000795	0.999173	CS pos: 23-24. Pr: 0.9737

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000018385-p1.