Species | Enterovibrio hollisae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Enterovibrio; Enterovibrio hollisae | |||||||||||
CAZyme ID | MGYG000002532_02609 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2879355; End: 2881058 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 97 | 502 | 5.9e-45 | 0.8588516746411483 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd02850 | E_set_Cellulase_N | 5.73e-20 | 2 | 89 | 1 | 86 | N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. |
pfam00759 | Glyco_hydro_9 | 1.03e-06 | 99 | 210 | 3 | 114 | Glycosyl hydrolase family 9. |
pfam02927 | CelD_N | 3.48e-05 | 6 | 84 | 6 | 83 | Cellulase N-terminal ig-like domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMG31028.1 | 0.0 | 1 | 567 | 1 | 567 |
AMG03708.1 | 6.43e-277 | 1 | 560 | 1 | 562 |
CAG18943.1 | 1.10e-276 | 1 | 563 | 1 | 574 |
AOW83420.1 | 3.02e-275 | 1 | 560 | 1 | 562 |
QXC57055.1 | 4.88e-272 | 1 | 560 | 1 | 562 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5DGQ_A | 5.35e-278 | 1 | 563 | 1 | 574 | Crystalstructure of GH9 exo-beta-D-glucosaminidase PBPRA0520 [Photobacterium profundum],5DGQ_B Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520 [Photobacterium profundum],5DGR_A Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520, glucosamine complex [Photobacterium profundum],5DGR_B Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520, glucosamine complex [Photobacterium profundum] |
3H7L_A | 1.06e-270 | 3 | 560 | 4 | 564 | ChainA, ENDOGLUCANASE [Vibrio parahaemolyticus],3H7L_B Chain B, ENDOGLUCANASE [Vibrio parahaemolyticus],3H7L_C Chain C, ENDOGLUCANASE [Vibrio parahaemolyticus] |
6GDT_A | 1.74e-268 | 1 | 560 | 1 | 562 | Crystalstructure of exo-glucosidase/glucosaminidase VC0615 from Vibrio Cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6GDT_B Crystal structure of exo-glucosidase/glucosaminidase VC0615 from Vibrio Cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6GDT_C Crystal structure of exo-glucosidase/glucosaminidase VC0615 from Vibrio Cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6GDT_D Crystal structure of exo-glucosidase/glucosaminidase VC0615 from Vibrio Cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6GDT_E Crystal structure of exo-glucosidase/glucosaminidase VC0615 from Vibrio Cholerae [Vibrio cholerae O1 biovar El Tor str. N16961] |
6FHJ_A | 1.85e-06 | 61 | 499 | 59 | 476 | Structuraldynamics and catalytic properties of a multi-modular xanthanase, native. [Paenibacillus],6FHN_A Structural dynamics and catalytic properties of a multi-modular xanthanase (Pt derivative) [Paenibacillus sp.] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999627 | 0.000405 | 0.000006 | 0.000001 | 0.000001 | 0.000001 |
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