Species | An172 sp002160515 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; An172; An172 sp002160515 | |||||||||||
CAZyme ID | MGYG000000924_00239 | |||||||||||
CAZy Family | GH51 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 47452; End: 51849 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3534 | AbfA | 1.76e-20 | 637 | 875 | 6 | 216 | Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism]. |
pfam13385 | Laminin_G_3 | 1.62e-19 | 394 | 548 | 2 | 151 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
pfam13385 | Laminin_G_3 | 4.32e-15 | 112 | 255 | 18 | 151 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
cd14256 | Dockerin_I | 9.79e-11 | 1404 | 1460 | 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. |
pfam06964 | Alpha-L-AF_C | 2.59e-10 | 1172 | 1310 | 56 | 192 | Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QZO76045.1 | 2.51e-238 | 338 | 1330 | 30 | 959 |
ALE10461.1 | 1.82e-221 | 343 | 1316 | 35 | 972 |
AXM90856.1 | 1.15e-220 | 343 | 1316 | 52 | 989 |
BBA56144.1 | 1.95e-220 | 343 | 1316 | 35 | 972 |
AFL03619.1 | 1.06e-219 | 343 | 1316 | 35 | 972 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4ATW_A | 2.41e-11 | 669 | 813 | 44 | 173 | Thecrystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8] |
3S2C_A | 2.42e-11 | 669 | 813 | 44 | 173 | Structureof the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1] |
3UG3_A | 2.56e-11 | 669 | 813 | 64 | 193 | Crystalstructure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima] |
5O7Z_A | 1.34e-10 | 637 | 840 | 5 | 192 | ChainA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_A Chain A, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila] |
2Y2W_A | 2.68e-10 | 675 | 828 | 93 | 223 | Elucidationof the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_B Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_C Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_D Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_E Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum],2Y2W_F Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum. [Bifidobacterium longum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P53627 | 1.57e-11 | 663 | 839 | 41 | 194 | Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfA PE=1 SV=1 |
E7CY70 | 6.39e-11 | 675 | 828 | 63 | 194 | Exo-alpha-(1->6)-L-arabinofuranosidase OS=Bifidobacterium longum OX=216816 GN=afuB PE=1 SV=1 |
Q9KBR4 | 7.96e-11 | 668 | 828 | 45 | 182 | Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=abfA PE=3 SV=1 |
A3DIH0 | 1.40e-10 | 637 | 840 | 6 | 193 | Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=Cthe_2548 PE=1 SV=1 |
Q841V6 | 1.45e-09 | 675 | 828 | 93 | 223 | Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Bifidobacterium longum OX=216816 GN=abfB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000580 | 0.599635 | 0.399054 | 0.000281 | 0.000239 | 0.000189 |
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