CAZyme Information: H257_06858-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_06858-t26_1-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
492		54103.03	5.1266

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913127:204703-206547(-)

Full Sequence      

MVYPSASGDYEASVVTTAKPAGRKLLFLGLGLVVVVAAPTPAPTRQVFSFGKIQDGSTRS
KDEETNPLTYDGQGCYLPNYISKKGKIYIVTNTNQEIPIAIKGINWFGMETENAIPFGLW
TNDQNGTTLFELASFLSRNQFNSVRLPLTVSSILNNTAPNRGLIHEYANAALDLTNYTST
IGGVVEALGYRSISVLLDIHNLDIYTKGDAWFGNMTTEADVLNAVDVLTTSFCNDKYWNI
IGIDLKNEPFNITWGDNGPKDFRVGAATMAHRMLVKCPQWLAFIEGNALKQNGTYTGQKS
WFFDWWGGGLRDVGTDPLTLNTAHKVVYAPHYYSPSVYPQAYLVQGGKREGDILTGYREW
DDATLEQIVADSSEDMFGYLRSTQDGALVLGEFGGLFTQDTHVNKTNQRVTQNVIKMVAS
QPGYAGGYVWSLNPESGYEYSASGTKGASGTKGYFMEGLLTLDWVHVNTPLLKALEGMNS
LNNLTPFPCLKM

Enzyme Prediction     

No EC number prediction in H257_06858-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	96	436	1.3e-125	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	2.85e-14	96	441	42	371	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	2.52e-10	118	436	17	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABG80550.1|GH5_20	4.26e-138	52	489	134	573
ABG80551.1|GH5_20	4.26e-138	52	489	134	573
CCA15003.1|GH5_20	4.33e-138	45	489	77	517
CCA25494.1|GH5_20	4.33e-138	45	489	77	517
ABC87086.1|GH5_20	6.61e-137	53	492	137	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.62e-39	87	437	15	351	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	4.30e-39	87	437	15	351	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	7.25e-39	87	437	48	384	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	7.25e-39	87	437	48	384	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	2.61e-38	87	437	48	384	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|P19487|GUNA_XANCP	2.44e-30	88	437	26	344	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
sp|P54583|GUN1_ACIC1	6.72e-30	97	437	60	367	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P10474|GUNB_CALSA	1.08e-28	98	395	644	937	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P23548|GUN_PAEPO	1.56e-28	100	437	55	357	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P50400|GUND_CELFI	6.41e-28	89	437	53	388	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
0.622263	0.377737

TMHMM  Annotations     

Start	End
25	42