CAZyme Information: H257_10138-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_10138-t26_1-p1
• CAZy Family: GH6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632		68637.61	6.2515

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=KI913139:447625-449643(+)

Full Sequence      

MSRPQYYTQDTHDSVAAHDDPMENVEVWQDTTAERGYNTYLVQQSSVMDSSHSNESNLQS
GGARPTFGDRQTMADRGTIAAARPDIRIGKVEDGDRPTKTSGRKRVWPGWLLLFLMVAGS
LFGITWFSIKLYKAAQKQQEKAEFILNRTPRPITPAKICEQPDFINDKGVIYATYKSAPP
QKIVITGINWSGMENSEGVPHGLAFGQAALDDIVERMAKQGMTAVRLPLNVLMINSNAAP
NVKDFVDPVVNPELVVSDYMTMIKKIVQGLAKKGVSVLLDIHKLDPAVEGKTEGLWYSAT
VPASAINQAIQTLATDLCNSNYYNVLGVDLKNEPHDGCWPGGAADVSCPDAKNWPKAAAK
LADTMLAACPKWMAFVEGLASATLTNHGFVTKAGPNTTLYYQEWWGAALQNVTKYPVPVA
PAHKNKLVYVPHFYSPSVYPAPYYFASFASAGGGAVVEEWPTTADGNASLKANVYRALDL
AFGNAVKNIESPVMFGEFGGIYGAKDLFPLKTSSRVIELFVQYSADRNMSGGFAWSLNPD
SVYQFNGDTSKAGEFNYGLYENDPVRPWSAYNQDYSDALLKFKGTGTIDCVKIDAAGNDT
TTTTTTTAGPAVVVPTSTTAPVSTAVLTTKKP

Enzyme Prediction     

No EC number prediction in H257_10138-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	182	541	2.7e-116	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	1.49e-20	185	542	47	364	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	2.98e-13	195	541	9	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA26601.1|GH5_20	1.02e-141	26	590	21	563
ABL75348.1|GH5_20	1.19e-139	27	590	20	566
ABL75347.1|GH5_20	8.24e-139	27	590	20	565
UIZ24458.1|GH5_20	1.42e-133	24	600	14	576
CCA27479.1|GH5_20	1.22e-127	27	590	20	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	5.69e-30	183	568	28	365	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	5.69e-30	183	568	28	365	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	1.85e-29	183	568	61	398	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	4.53e-29	183	568	61	398	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	1.50e-28	183	568	61	398	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	2.62e-30	181	579	52	378	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P50400|GUND_CELFI	1.34e-27	155	541	36	387	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P10474|GUNB_CALSA	3.26e-26	162	448	622	905	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P19487|GUNA_XANCP	7.13e-23	183	585	42	371	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
1.000062	0.000001

TMHMM  Annotations     

Start	End
106	128