CAZyme Information: H257_14978-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_14978-t26_1-p1
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
357	KI913177|CGC1	41449.57	5.7100

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=KI913177:281895-283333(-)

Full Sequence      

MVVSEEWKYMSTLVPPQYPCVRRPGADTSTRMVLDGRLDKDEWEHAQWTDLFVDIEGPAR
KPNPSQRTRAKMMWDDNYLYVGADMEESRVWGTFTDKNTVMYHENDFEIFIDPDGSRHNY
YEFEMNCLNTIWELRLRRPYKDGNSIDNPYNLSDIHSAVYIDGTPNDPSVTCSKWSVEVA
IPLRELVQFDERRRRHVQAGDVWRMNFSRVQYDLLVQHGRYVKVPNQREYNFVWAPTGVI
DIHRPEKWSFVAFLGATAVDKAMTWQALRAAVDQGLAVEMLLDQVYYDQRAFHDVHARYA
ATLAELHPTSTGTPSPPPEHPITLECATDLQSYVVVVAARGHVHRMTHDAKYTITSE

Enzyme Prediction     

No EC number prediction in H257_14978-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	35	214	2.9e-41	0.8296703296703297

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187678	CBM9_like_3	7.77e-69	34	250	1	200	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
187676	CBM9_like_2	9.92e-19	28	210	7	170	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
399451	CBM9_1	8.81e-10	34	187	1	133	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
187674	CBM9_like_1	8.31e-08	33	184	10	134	DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
187677	CBM9_like_4	8.28e-07	33	183	3	138	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCM88676.1|CBM9	1.78e-88	15	306	5	280
QOT09656.1|CBM0	1.20e-81	15	306	15	298
QZN78207.1|CBM9	4.71e-78	15	306	15	297
QLG42346.1|CBM0	7.49e-77	15	306	15	297
QXD16319.1|CBM9	7.90e-77	14	306	31	317

PDB Hits     

H257_14978-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P38535|XYNX_ACETH	2.49e-06	33	182	720	842	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
sp|P36917|XYNA_THESA	4.42e-06	33	182	868	990	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000044	0.000000

TMHMM  Annotations     

There is no transmembrane helices in H257_14978-t26_1-p1.