Species | Plesiomonas shigelloides | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Plesiomonas; Plesiomonas shigelloides | |||||||||||
CAZyme ID | MGYG000002536_00457 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9228; End: 10934 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 97 | 500 | 3.6e-46 | 0.8444976076555024 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd02850 | E_set_Cellulase_N | 2.44e-17 | 2 | 88 | 2 | 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 | 6.29e-12 | 98 | 390 | 3 | 287 | Glycosyl hydrolase family 9. |
pfam02927 | CelD_N | 1.55e-06 | 4 | 83 | 5 | 83 | Cellulase N-terminal ig-like domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QOH80208.1 | 0.0 | 1 | 568 | 1 | 568 |
QWK97565.1 | 0.0 | 1 | 568 | 1 | 568 |
QWK94945.1 | 0.0 | 1 | 568 | 1 | 568 |
AVQ87285.1 | 0.0 | 1 | 568 | 1 | 568 |
QIY09407.1 | 0.0 | 1 | 568 | 1 | 568 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3H7L_A | 2.32e-231 | 1 | 561 | 3 | 564 | ChainA, ENDOGLUCANASE [Vibrio parahaemolyticus],3H7L_B Chain B, ENDOGLUCANASE [Vibrio parahaemolyticus],3H7L_C Chain C, ENDOGLUCANASE [Vibrio parahaemolyticus] |
6GDT_A | 6.63e-230 | 1 | 562 | 2 | 563 | 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] |
5DGQ_A | 2.35e-226 | 2 | 568 | 3 | 578 | 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] |
5U2O_A | 1.25e-07 | 64 | 499 | 53 | 463 | Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
5U0H_A | 1.26e-07 | 118 | 499 | 118 | 463 | Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999654 | 0.000358 | 0.000011 | 0.000001 | 0.000000 | 0.000001 |
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