Species | UBA1394 sp900554975 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; UBA1394 sp900554975 | |||||||||||
CAZyme ID | MGYG000004471_00865 | |||||||||||
CAZy Family | CBM22 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 21943; End: 23844 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH10 | 202 | 538 | 4.1e-100 | 0.9933993399339934 |
CBM22 | 47 | 173 | 3.6e-23 | 0.9770992366412213 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00331 | Glyco_hydro_10 | 3.68e-111 | 203 | 538 | 1 | 310 | Glycosyl hydrolase family 10. |
smart00633 | Glyco_10 | 1.36e-104 | 244 | 536 | 1 | 263 | Glycosyl hydrolase family 10. |
COG3693 | XynA | 2.19e-71 | 202 | 537 | 19 | 338 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
cd14256 | Dockerin_I | 1.20e-14 | 575 | 628 | 2 | 55 | 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. |
pfam02018 | CBM_4_9 | 3.57e-14 | 47 | 173 | 2 | 129 | Carbohydrate binding domain. This family includes diverse carbohydrate binding domains. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL16579.1 | 3.25e-216 | 1 | 621 | 1 | 617 |
CAB65753.1 | 1.10e-191 | 42 | 541 | 27 | 533 |
CAL91979.1 | 5.06e-183 | 37 | 541 | 18 | 526 |
CAL91978.1 | 1.62e-176 | 89 | 539 | 12 | 464 |
ADU21885.1 | 5.07e-157 | 50 | 541 | 39 | 541 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2W5F_A | 9.78e-97 | 77 | 536 | 53 | 524 | ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus] |
2WYS_A | 8.75e-94 | 107 | 536 | 83 | 524 | ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WYS_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus] |
5OFJ_A | 1.09e-63 | 198 | 538 | 6 | 337 | Crystalstructure of N-terminal domain of bifunctional CbXyn10C [Caldicellulosiruptor bescii DSM 6725] |
6FHE_A | 2.12e-63 | 195 | 537 | 5 | 339 | Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct] |
7NL2_A | 5.97e-63 | 200 | 538 | 9 | 339 | ChainA, Beta-xylanase [Pseudothermotoga thermarum DSM 5069],7NL2_B Chain B, Beta-xylanase [Pseudothermotoga thermarum DSM 5069] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P29126 | 3.18e-101 | 202 | 533 | 629 | 946 | Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens OX=1265 GN=xynA PE=3 SV=1 |
P51584 | 4.41e-92 | 77 | 536 | 64 | 535 | Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1 |
Q60037 | 7.32e-79 | 43 | 543 | 200 | 696 | 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 |
Q60042 | 4.13e-76 | 43 | 543 | 195 | 692 | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1 |
P36917 | 1.90e-64 | 36 | 537 | 185 | 673 | Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.004068 | 0.464429 | 0.529038 | 0.001837 | 0.000408 | 0.000198 |
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