Species | Brachyspira pilosicoli | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira pilosicoli | |||||||||||
CAZyme ID | MGYG000000470_01271 | |||||||||||
CAZy Family | GH108 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6075; End: 6623 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH108 | 11 | 108 | 6.3e-17 | 0.9418604651162791 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3926 | ZliS | 5.60e-17 | 4 | 182 | 5 | 164 | Lysozyme family protein [General function prediction only]. |
pfam05838 | Glyco_hydro_108 | 1.12e-16 | 13 | 108 | 6 | 86 | Glycosyl hydrolase 108. This family acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a C-terminal pfam09374 domain. |
cd13926 | N-acetylmuramidase_GH108 | 2.82e-12 | 2 | 108 | 1 | 91 | N-acetylmuramidase domain of the glycosyl hydrolase 108 family. This domain acts as a lysozyme (N-acetylmuramidase), EC:3.2.1.17. It contains a conserved EGGY motif near the N-terminus, the glutamic acid within this motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. It is frequently found at the N-terminus of proteins containing a peptidoglycan binding domain. |
pfam09374 | PG_binding_3 | 3.82e-09 | 111 | 179 | 1 | 75 | Predicted Peptidoglycan domain. This family contains a potential peptidoglycan binding domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCG56201.1 | 7.88e-112 | 1 | 182 | 1 | 182 |
QWM90197.1 | 1.49e-28 | 1 | 144 | 1 | 140 |
BBE19459.1 | 8.14e-28 | 1 | 179 | 1 | 173 |
CDF64526.1 | 2.68e-27 | 1 | 182 | 1 | 184 |
QEL44447.1 | 2.68e-27 | 1 | 182 | 1 | 184 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2IS5_A | 1.54e-08 | 4 | 178 | 6 | 154 | Crystalstructure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_B Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_C Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B],2IS5_D Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides [Neisseria meningitidis serogroup B] |
2IKB_A | 1.56e-08 | 4 | 178 | 5 | 153 | CrystalStructure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_B Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_C Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58],2IKB_D Crystal Structure of a Protein of Unknown Function NMB1012 from Neisseria meningitidis [Neisseria meningitidis MC58] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000076 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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