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CAZyme Information: MGYG000002230_00757
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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 | Ruminococcus sp900545125 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900545125 | |||||||||||
| CAZyme ID | MGYG000002230_00757 | |||||||||||
| CAZy Family | CBM22 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 9342; End: 11051 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE1 | 329 | 565 | 9.9e-39 | 0.973568281938326 |
| CBM22 | 44 | 171 | 6.5e-30 | 0.9694656488549618 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG2382 | Fes | 2.66e-24 | 314 | 569 | 61 | 298 | Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]. |
| pfam02018 | CBM_4_9 | 4.70e-23 | 43 | 175 | 3 | 134 | Carbohydrate binding domain. This family includes diverse carbohydrate binding domains. |
| pfam00756 | Esterase | 8.66e-17 | 329 | 486 | 1 | 151 | Putative esterase. This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family. |
| COG2819 | YbbA | 3.72e-12 | 333 | 477 | 20 | 171 | Predicted hydrolase of the alpha/beta superfamily [General function prediction only]. |
| cd14256 | Dockerin_I | 1.16e-10 | 204 | 259 | 1 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAB93667.1 | 4.95e-142 | 34 | 568 | 247 | 792 |
| AAR39816.1 | 4.85e-131 | 24 | 539 | 251 | 782 |
| CAA90271.1 | 4.85e-131 | 24 | 539 | 251 | 782 |
| CBL17231.1 | 1.12e-126 | 33 | 569 | 557 | 1074 |
| ADU21987.1 | 1.32e-113 | 24 | 568 | 719 | 1232 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5CXU_A | 1.45e-71 | 319 | 569 | 23 | 272 | Structureof the CE1 ferulic acid esterase AmCE1/Fae1A, from the anaerobic fungi Anaeromyces mucronatus in the absence of substrate [Anaeromyces mucronatus],5CXX_A Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_B Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_C Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus] |
| 1JJF_A | 1.97e-43 | 320 | 564 | 30 | 255 | ChainA, Endo-1,4-beta-xylanase Z [Acetivibrio thermocellus] |
| 1JT2_A | 5.25e-43 | 320 | 564 | 30 | 255 | ChainA, PROTEIN (ENDO-1,4-BETA-XYLANASE Z) [Acetivibrio thermocellus] |
| 1H6X_A | 2.62e-21 | 40 | 191 | 6 | 159 | ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus] |
| 1H6Y_A | 2.62e-21 | 40 | 191 | 6 | 159 | ChainA, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus],1H6Y_B Chain B, Endo-1,4-beta-xylanase Y [Acetivibrio thermocellus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P10478 | 2.70e-39 | 320 | 564 | 49 | 274 | Endo-1,4-beta-xylanase Z OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xynZ PE=1 SV=3 |
| P51584 | 8.21e-34 | 40 | 470 | 564 | 973 | Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1 |
| Q53317 | 2.00e-32 | 32 | 189 | 249 | 405 | Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2 |
| D5EY13 | 5.31e-16 | 318 | 472 | 496 | 650 | Endo-1,4-beta-xylanase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=xyn10D-fae1A PE=1 SV=1 |
| Q60037 | 3.27e-14 | 45 | 198 | 207 | 364 | 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 | 0.998775 | 0.000209 | 0.000232 | 0.000204 | 0.000177 |