Species | Duncaniella sp001701225 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp001701225 | |||||||||||
CAZyme ID | MGYG000001738_01424 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 35608; End: 37098 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 152 | 444 | 1.6e-89 | 0.9891304347826086 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 6.46e-50 | 140 | 445 | 4 | 270 | Cellulase (glycosyl hydrolase family 5). |
COG2730 | BglC | 1.82e-22 | 135 | 472 | 54 | 389 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
cd14948 | BACON | 4.06e-06 | 27 | 110 | 4 | 82 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
pfam13004 | BACON | 0.008 | 59 | 110 | 8 | 60 | Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALJ60576.1 | 1.37e-174 | 1 | 496 | 14 | 512 |
QUT88430.1 | 3.93e-172 | 44 | 496 | 143 | 598 |
AVM57519.1 | 3.18e-165 | 1 | 496 | 58 | 563 |
AIF26005.1 | 4.67e-163 | 132 | 496 | 37 | 402 |
ADY35478.1 | 1.21e-161 | 42 | 496 | 147 | 592 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6WQY_A | 2.33e-155 | 114 | 480 | 18 | 384 | ChainA, Cellulase [Phocaeicola salanitronis DSM 18170] |
4YHE_A | 4.23e-131 | 132 | 496 | 14 | 386 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
4YHG_A | 3.41e-130 | 132 | 496 | 14 | 386 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
2JEP_A | 4.52e-70 | 130 | 448 | 40 | 368 | Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli] |
3NDY_A | 1.35e-63 | 132 | 459 | 19 | 324 | Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O08342 | 1.12e-63 | 132 | 448 | 47 | 373 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
P28623 | 2.64e-61 | 132 | 459 | 50 | 355 | Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2 |
Q12647 | 1.16e-58 | 132 | 460 | 32 | 347 | Endoglucanase B OS=Neocallimastix patriciarum OX=4758 GN=CELB PE=2 SV=1 |
P28621 | 5.59e-58 | 111 | 451 | 24 | 348 | Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1 |
P10477 | 3.40e-55 | 132 | 460 | 64 | 369 | Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000028 | 0.000004 | 1.000004 | 0.000000 | 0.000000 | 0.000000 |
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