| Species | Dysgonomonas capnocytophagoides | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas capnocytophagoides | |||||||||||
| CAZyme ID | MGYG000000815_00908 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1146077; End: 1147486 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd01825 | SGNH_hydrolase_peri1 | 1.53e-36 | 305 | 460 | 24 | 189 | SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| cd00229 | SGNH_hydrolase | 1.09e-13 | 300 | 459 | 30 | 187 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
| pfam13472 | Lipase_GDSL_2 | 3.15e-12 | 312 | 446 | 40 | 175 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| PRK06347 | PRK06347 | 1.44e-11 | 94 | 294 | 397 | 572 | 1,4-beta-N-acetylmuramoylhydrolase. |
| pfam01476 | LysM | 3.30e-11 | 199 | 240 | 1 | 42 | LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QIK56104.1 | 1.70e-165 | 1 | 467 | 1 | 488 |
| QIK61460.1 | 1.09e-162 | 20 | 467 | 5 | 473 |
| AOE53578.1 | 1.31e-116 | 26 | 466 | 43 | 474 |
| ALM49961.1 | 1.31e-116 | 26 | 466 | 43 | 474 |
| QEE49512.1 | 1.90e-114 | 35 | 467 | 47 | 469 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4K3U_A | 3.75e-09 | 41 | 453 | 38 | 365 | PeptidoglycanO-acetylesterase in action, 30 min [Neisseria meningitidis 4119],4K3U_B Peptidoglycan O-acetylesterase in action, 30 min [Neisseria meningitidis 4119],4K40_A Peptidoglycan O-acetylesterase in action, 0 min [Neisseria meningitidis LNP21362],4K40_B Peptidoglycan O-acetylesterase in action, 0 min [Neisseria meningitidis LNP21362],4K7J_A Peptidoglycan O-acetylesterase in action, 5 min [Neisseria meningitidis 4119],4K7J_B Peptidoglycan O-acetylesterase in action, 5 min [Neisseria meningitidis 4119] |
| 4K9S_A | 6.44e-08 | 41 | 445 | 38 | 357 | PeptidoglycanO-acetylesterase in action, setmet [Neisseria meningitidis 4119],4K9S_B Peptidoglycan O-acetylesterase in action, setmet [Neisseria meningitidis 4119] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000289 | 0.998990 | 0.000212 | 0.000159 | 0.000164 | 0.000148 |
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