| Species | Helicobacter_C cinaedi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Helicobacteraceae; Helicobacter_C; Helicobacter_C cinaedi | |||||||||||
| CAZyme ID | MGYG000001432_01533 | |||||||||||
| CAZy Family | GH104 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1478913; End: 1482326 Strand: + | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR02594 | TIGR02594 | 1.05e-37 | 983 | 1111 | 2 | 129 | TIGR02594 family protein. Members of this protein family known so far are restricted to the bacteria, and for the most to the proteobacteria. The function is unknown. |
| pfam05257 | CHAP | 1.46e-05 | 1023 | 1092 | 10 | 83 | CHAP domain. This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Escherichia coli gss, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QOQ95511.1 | 0.0 | 1 | 979 | 1 | 979 |
| BAM12578.1 | 0.0 | 1 | 979 | 1 | 974 |
| BBB20404.1 | 1.76e-179 | 717 | 979 | 18 | 280 |
| BBB20284.1 | 4.71e-178 | 717 | 979 | 18 | 280 |
| QKF91469.1 | 7.52e-47 | 46 | 899 | 132 | 883 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000069 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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