CAZyme Information: H257_05010-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_05010-t26_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
552		59833.64	7.3223

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=KI913122:573787-575445(-)

Full Sequence      

MSVDDRPRKSEDILAVTEAPIVGSDGKSIRRKQKFGGRRSVWPGALALILGIAGAIGALV
YWGTWEHTQMLGRQPDESSLAKAYGSGHTISDGQVVNTTTELPLEVTNPVEYKDMKCAQI
DYLSKNNRIYTVSKGKETPLVFKGVNWLGLEGWDHVITGLWDGPRDGNSFYRIASFLSSN
GFNAVRFPLDIDSAARNIPIKTNFNTNSQRALASVKTYVDLITRLTEGLGQFKIAVVLDF
NTRSKATDLNSTDQSVISLDQRPSSDGSTGNGWENVNVRYAEYEKAIANLATALCNEVHW
NVVGLDIKDAPAGDAGQWDGEEKTSWQMFASKVGAAVVKACPTWLVFAQGLTGKTKFGTG
DDTKSVADWPGSSLREALTSPINVGKANKLVYAPPFWSPSIYPAPYFFKSSTGGSLLTKW
TGFTTQVDMDTNVGDAMKAIFGDLLNKQSAAVVLSSFGGLFGTEDLDKGKVSTMAITAIV
NQMTLSQKPLSGGFWWSLNPDNRWPHPAPDSPVSVASGLLDPTWRKGNSEALRATKLMDA
IPGLAFLPCDPR

Enzyme Prediction     

No EC number prediction in H257_05010-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	138	501	3.7e-91	0.9912790697674418

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	6.02e-05	130	409	35	287	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ25210.1|GH5_20	8.69e-114	31	550	39	541
CCA23923.1|GH5_20	4.52e-112	8	549	15	535
ABC87090.1|GH5_20	9.78e-76	6	549	112	627
ABK59037.1|GH5_20	9.78e-76	6	549	112	627
CCA15003.1|GH5_20	1.60e-74	31	549	23	517

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W6M_A	2.47e-26	120	502	6	350	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	4.53e-26	120	502	6	350	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]
3QHN_A	6.60e-26	120	502	39	383	Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_B Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_C Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
2ZUM_A	1.20e-25	120	502	39	383	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]
3QHM_A	2.17e-25	120	502	39	383	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19487|GUNA_XANCP	5.23e-17	122	502	26	343	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|P23548|GUN_PAEPO	5.59e-16	122	502	39	356	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P50400|GUND_CELFI	2.35e-13	121	502	44	387	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
sp|P10474|GUNB_CALSA	1.62e-10	139	417	644	911	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999951	0.000049

TMHMM  Annotations     

Start	End
40	62