CAZyme Information: PIW_T012923-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T012923-RA-p1
• CAZy Family: GT50
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
455		52231.76	4.8996

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC04603:112-1727(-)

Full Sequence      

MANADEDESEWTYMDTLRPPVYICLRRKPSADGKFHPMALDGRSSSSHAANLIACLLRIH
KEAWSHVPWSEPFVDIEGAAKKPTEYLPTRFKMMYDDAHLYIGAELVEPKIWGTICKKNS
TMYHENDFEVFLNPDGSRHNYYEMELNCLNTIWELLLHKPYKDGYSIENPYNLSGFRSAV
YVDGITNSPQTVCTKWCIEMSYPLAELVQFDTLRQRSAKAGDVWRVNFSRVQYELEVVVD
EESSELCYEKVPDKREANIVWAPTGVIDIHRPEKWGFVFFSSQDELPGGEDELASAMAEF
LREQIAMERVLDTIYYDQREFYKRHEGFASHWEQLYPTPEAFRHMDLITKFALSTPTISC
QSELGVAAGSSSSAAEIGSATPRRRRSYVPSLDVDDDDEVSTMNDPALSLLSPRSREIKR
KEASGLFRTYTASVKSATQLWNMENDARLWKTSTM

Enzyme Prediction     

No EC number prediction in PIW_T012923-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	61	231	5e-30	0.7857142857142857

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187678	CBM9_like_3	7.39e-58	61	277	7	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.
187675	DOMON_like	3.89e-07	73	228	4	142	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
187676	CBM9_like_2	4.31e-06	62	231	20	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	5.78e-05	62	208	7	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UOK64684.1|CBM0	3.25e-67	19	330	15	292
BCM88676.1|CBM9	1.17e-66	18	330	4	275
QOT09656.1|CBM0	3.37e-63	19	335	15	298
UPK45153.1|CBM9	4.61e-63	19	330	15	292
QZN78207.1|CBM9	1.28e-62	19	330	15	292

PDB Hits     

PIW_T012923-RA-p1 has no PDB hit.

Swiss-Prot Hits     

PIW_T012923-RA-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000076	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PIW_T012923-RA-p1.