CAZyme Information: H257_16610-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_16610-t26_1-p1
• CAZy Family: GT49
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
523	KI913202|CGC1	56576.81	6.6913

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=KI913202:33594-36081(-)

Full Sequence      

MRVFAAVAASMMALAAAQTPEDKVKTFRKCRQSNYVTEGNQIFAVDPLNPTIKTPILIKG
VQWKGMETTDGIPAGLWGKSVQRDSGINGTSLAYMLKFLSSNKFNTVRLPIMGDNFLNPS
FLPKVGYIHGENREIALYDKGFTPKMADLLARFIGSFQKYRISVVLDLHALSNEFLQDAY
WYYPVKETVEESTAYKVAVLLATYYCKPEYWNVLGIDLKDAMTDVDWPATAAASGDWPAA
AETIAAKVNELCPQWLVFVTGGSKGSFVVKTNSYKVWPGLNFANATTRPLKKATNIVYSP
QAFTQGVEPLGYFFNPSSNCSNAILPDKDTECVVIENGLKVPSTKRALACDNSKLQCQSF
TPLSTPDLTALYSRLLDENIGGVVKQASVPVVFASFGGIYGSSQPLQSAVIDQLIKYIAT
STAGGFFASLNPDTQMWLEGPPPGNKTIGRARYGLMTSSSWQVGHADLLAALAELKSTEI
PCYGDEQPGDPDAATSGAIMGTSWLQSGGGGVAVVTAMLLLLV

Enzyme Prediction     

No EC number prediction in H257_16610-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	54	320	8.1e-51	0.7383720930232558

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	6.60e-11	35	339	28	305	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	4.43e-06	59	433	6	271	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABL75347.1|GH5_20	3.63e-46	8	483	119	566
CCA26601.1|GH5_20	5.05e-44	23	483	135	564
ABL75348.1|GH5_20	1.00e-43	23	483	138	567
UIZ24458.1|GH5_20	2.09e-42	25	483	136	563
CCA27479.1|GH5_20	4.10e-40	30	483	153	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QHN_A	4.39e-16	35	313	41	309	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]
3QHO_A	7.78e-16	35	313	41	309	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]
3VVG_A	1.15e-15	35	313	8	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]
3W6M_A	1.15e-15	35	313	8	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]
2ZUM_A	1.84e-15	35	313	41	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]

Swiss-Prot Hits     

H257_16610-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999732	CS pos: 17-18. Pr: 0.9588

TMHMM  Annotations     

There is no transmembrane helices in H257_16610-t26_1-p1.