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CAZyme Information: MGYG000001063_02311
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Robinsoniella sp900540475 | |||||||||||
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| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475 | |||||||||||
| CAZyme ID | MGYG000001063_02311 | |||||||||||
| CAZy Family | CBM9 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 60475; End: 64185 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM9 | 759 | 941 | 2.1e-48 | 0.9945054945054945 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00005 | CBM9_like_1 | 9.94e-74 | 750 | 941 | 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 | 1.71e-51 | 759 | 942 | 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 | 1.29e-20 | 756 | 922 | 1 | 172 | 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. |
| sd00036 | LRR_3 | 1.83e-12 | 1143 | 1213 | 1 | 70 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| pfam13229 | Beta_helix | 1.16e-11 | 412 | 588 | 29 | 157 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AFH61176.2 | 1.19e-188 | 42 | 976 | 289 | 1186 |
| AFK65328.1 | 1.54e-188 | 42 | 976 | 300 | 1197 |
| AEI40311.1 | 2.81e-188 | 42 | 976 | 297 | 1194 |
| AFC28944.1 | 1.08e-187 | 42 | 976 | 297 | 1194 |
| AEI40309.1 | 3.15e-105 | 283 | 728 | 40 | 455 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1I82_A | 9.56e-42 | 750 | 941 | 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] |
| 7NWN_AAA | 2.38e-23 | 755 | 942 | 28 | 203 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P38535 | 5.22e-39 | 748 | 941 | 710 | 894 | Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1 |
| P36917 | 1.33e-38 | 750 | 941 | 860 | 1042 | Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1 |
| O69230 | 3.58e-38 | 745 | 941 | 895 | 1083 | Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1 |
| Q60042 | 1.22e-36 | 750 | 941 | 869 | 1053 | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1 |
| Q60037 | 3.68e-36 | 750 | 941 | 873 | 1057 | Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000380 | 0.998815 | 0.000240 | 0.000213 | 0.000178 | 0.000148 |
