Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; ; | |||||||||||
CAZyme ID | MGYG000000745_01769 | |||||||||||
CAZy Family | CBM9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4657; End: 8478 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE15 | 302 | 673 | 3e-71 | 0.9888475836431226 |
CBM9 | 39 | 212 | 7.4e-41 | 0.9945054945054945 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00005 | CBM9_like_1 | 9.53e-59 | 30 | 212 | 2 | 184 | 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. |
pfam06452 | CBM9_1 | 2.29e-42 | 39 | 213 | 1 | 182 | 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. |
cd09619 | CBM9_like_4 | 9.31e-20 | 36 | 208 | 1 | 187 | 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. |
cd09620 | CBM9_like_3 | 2.17e-08 | 39 | 103 | 1 | 76 | 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. |
cd00241 | DOMON_like | 8.53e-08 | 57 | 180 | 14 | 145 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QTE69547.1 | 1.89e-159 | 287 | 708 | 22 | 438 |
QUA54463.1 | 6.95e-157 | 290 | 708 | 1 | 414 |
QTE70682.1 | 7.42e-151 | 290 | 708 | 1 | 414 |
QTE74645.1 | 7.42e-151 | 290 | 708 | 1 | 414 |
ADQ41707.1 | 5.67e-129 | 34 | 679 | 1077 | 1691 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7NN3_A | 8.07e-71 | 302 | 679 | 24 | 373 | ChainA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NN3_B Chain B, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NN3_C Chain C, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NN3_D Chain D, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B] |
7NWN_AAA | 1.78e-44 | 34 | 225 | 27 | 215 | ChainAAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWO_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWP_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B],7NWQ_AAA Chain AAA, Beta-xylanase [Caldicellulosiruptor kristjanssonii I77R1B] |
1I82_A | 5.26e-33 | 30 | 212 | 3 | 187 | Family9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Cellobiose [Thermotoga maritima],1I8A_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Glucose [Thermotoga maritima],1I8U_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a [Thermotoga maritima] |
6RU2_A | 2.62e-26 | 293 | 655 | 7 | 325 | CrystalStructure of Glucuronoyl Esterase from Cerrena unicolor [Cerrena unicolor],6RU2_B Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor [Cerrena unicolor] |
6RTV_A | 6.20e-26 | 293 | 655 | 13 | 331 | CrystalStructure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant [Cerrena unicolor],6RTV_B Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant [Cerrena unicolor],6RU1_A Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid Um4X [Cerrena unicolor],6RU1_B Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid Um4X [Cerrena unicolor],6RV7_A Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid UXXR [Cerrena unicolor],6RV7_B Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid UXXR [Cerrena unicolor],6RV9_A Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid XUXXR [Cerrena unicolor],6RV9_B Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor inactive S270A variant in complex with the aldouronic acid XUXXR [Cerrena unicolor] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9RLB8 | 1.15e-82 | 291 | 704 | 370 | 762 | Multidomain esterase OS=Ruminococcus flavefaciens OX=1265 GN=cesA PE=1 SV=1 |
C6CRV0 | 4.56e-34 | 23 | 216 | 861 | 1053 | Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1 |
P36917 | 1.94e-31 | 30 | 215 | 860 | 1045 | Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1 |
P38535 | 3.11e-31 | 30 | 215 | 712 | 897 | Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1 |
D8QLP9 | 2.93e-29 | 300 | 678 | 34 | 364 | 4-O-methyl-glucuronoyl methylesterase OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_238770 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000234 | 0.999105 | 0.000170 | 0.000175 | 0.000155 | 0.000144 |
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