Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; | |||||||||||
CAZyme ID | MGYG000000605_00236 | |||||||||||
CAZy Family | CBM22 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 965; End: 2845 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH10 | 193 | 530 | 4.4e-102 | 0.9933993399339934 |
CBM22 | 38 | 165 | 1.9e-26 | 0.9694656488549618 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00331 | Glyco_hydro_10 | 3.41e-114 | 194 | 530 | 1 | 310 | Glycosyl hydrolase family 10. |
smart00633 | Glyco_10 | 1.29e-107 | 236 | 528 | 1 | 263 | Glycosyl hydrolase family 10. |
COG3693 | XynA | 1.91e-76 | 210 | 535 | 36 | 344 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
cd14256 | Dockerin_I | 2.83e-19 | 567 | 619 | 1 | 53 | 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 | 1.22e-16 | 36 | 165 | 1 | 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 | 3.09e-252 | 1 | 594 | 1 | 595 |
CAB65753.1 | 6.17e-197 | 7 | 533 | 3 | 533 |
CAL91979.1 | 2.33e-187 | 39 | 533 | 29 | 526 |
CAL91978.1 | 2.85e-170 | 71 | 532 | 2 | 465 |
ADU21885.1 | 2.21e-162 | 1 | 533 | 1 | 541 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2W5F_A | 6.34e-100 | 68 | 528 | 52 | 524 | ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus] |
2WYS_A | 2.43e-95 | 68 | 528 | 52 | 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] |
6FHE_A | 2.07e-68 | 188 | 529 | 7 | 339 | Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct] |
7NL2_A | 1.77e-65 | 186 | 532 | 4 | 341 | ChainA, Beta-xylanase [Pseudothermotoga thermarum DSM 5069],7NL2_B Chain B, Beta-xylanase [Pseudothermotoga thermarum DSM 5069] |
5OFJ_A | 2.39e-65 | 190 | 530 | 7 | 337 | Crystalstructure of N-terminal domain of bifunctional CbXyn10C [Caldicellulosiruptor bescii DSM 6725] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P29126 | 4.51e-105 | 193 | 525 | 629 | 946 | Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens OX=1265 GN=xynA PE=3 SV=1 |
P51584 | 3.86e-95 | 68 | 528 | 63 | 535 | Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1 |
Q60042 | 4.56e-80 | 38 | 529 | 200 | 686 | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1 |
Q60037 | 9.03e-80 | 38 | 529 | 205 | 690 | 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 |
P26223 | 7.50e-71 | 193 | 529 | 2 | 335 | Endo-1,4-beta-xylanase B OS=Butyrivibrio fibrisolvens OX=831 GN=xynB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000320 | 0.998848 | 0.000236 | 0.000220 | 0.000184 | 0.000162 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.