| Species | CAG-462 sp900765575 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462; CAG-462 sp900765575 | |||||||||||
| CAZyme ID | MGYG000004823_01729 | |||||||||||
| CAZy Family | PL10 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 8829; End: 10451 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL10 | 116 | 399 | 2.2e-129 | 0.9963636363636363 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR02474 | pec_lyase | 3.06e-21 | 116 | 377 | 1 | 263 | pectate lyase, PelA/Pel-15E family. Members of this family are isozymes of pectate lyase (EC 4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
| pfam09492 | Pec_lyase | 2.03e-20 | 116 | 377 | 1 | 262 | Pectic acid lyase. Members of this family are isozymes of pectate lyase (EC:4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase. |
| cd02889 | SQCY | 0.006 | 152 | 210 | 12 | 72 | Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QJR66990.1 | 2.69e-267 | 8 | 535 | 13 | 535 |
| QJR71330.1 | 2.69e-267 | 8 | 535 | 13 | 535 |
| QUT87327.1 | 2.69e-267 | 8 | 535 | 13 | 535 |
| QJR62731.1 | 2.69e-267 | 8 | 535 | 13 | 535 |
| AII65137.1 | 7.69e-267 | 8 | 535 | 13 | 535 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1R76_A | 1.88e-13 | 56 | 300 | 18 | 292 | ChainA, pectate lyase [Niveispirillum irakense] |
| 1GXM_A | 1.58e-11 | 109 | 307 | 37 | 223 | Family10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXM_B Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXN_A Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus] |
| 1GXO_A | 1.60e-10 | 109 | 307 | 37 | 223 | MutantD189A of Family 10 polysaccharide lyase from Cellvibrio cellulosa in complex with trigalaturonic acid [Cellvibrio japonicus] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000785 | 0.724769 | 0.273415 | 0.000367 | 0.000357 | 0.000289 |
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