CAZyme Information: EPrPAT00000013574-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000013574-p1
• CAZy Family: AA17
• CAZyme Description: Cell 5A endo-1,4-betaglucanase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
406	PaphDAOMBR444_SC0008|CGC2	44875.66	4.7780

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0008:105698-107118(+)

Full Sequence      

MCSRWPGIVFNLIIVGVSAALIALGAMDAHEKSTKSARQYEGNVASNRRIKDGLNNSDII
EDEGRIGNPKKYPNMGCELPDYLSKDGQIYARAMNWTEVAVGIKGVNWFGMENCVVESVA
SDYAVASFLARNKFNSVRLPVSIRSILEDTAPEDLVNLDSNRAFNITTYMSALKTIIQSL
AYRHVTVMISLHTLDPKATGGAWYSDELDISEDDYLHANVLGLDLKNEPHECSWGGDNPD
WLKGAELIGNRMLEGCPNWLAFVEGINCAHSITLNGAKNTYFDWWGGGLQKAGEQPVELQ
VADKVVYAPHYYNSAVSPAWYLYGGGTMRADGSIVDYVELDDDTLRLNVNATMWAMFGYL
TTRKTVLLGEFAGLYANDDHPKKTTKRTTDLTIQFAIENGFAGGYM

Enzyme Prediction     

No EC number prediction in EPrPAT00000013574-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	98	406	5.7e-107	0.9767441860465116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.71e-07	103	391	47	341	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	1.07e-05	124	378	28	243	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75351.1|GH5_20	8.77e-187	5	406	87	516
ABL75350.1|GH5_20	1.24e-184	5	406	89	518
ABC87086.1|GH5_20	2.41e-184	5	406	88	517
ABJ97692.1|GH5_20	5.75e-181	5	406	87	516
ABC87087.1|GH5_20	1.26e-173	5	406	95	525

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	8.80e-29	98	401	25	338	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	1.54e-27	98	401	25	338	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	4.08e-27	98	401	58	371	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	4.08e-27	98	401	58	371	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]
1VRX_A	4.12e-27	99	321	19	250	Chain A, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P54583|GUN1_ACIC1	2.66e-25	99	321	60	291	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	6.59e-23	105	373	58	320	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P19487|GUNA_XANCP	8.28e-22	101	405	42	335	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.767169	0.232842

TMHMM  Annotations     

Start	End
7	29