Species | Bifidobacterium dentium | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium dentium | |||||||||||
CAZyme ID | MGYG000001354_01961 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2380135; End: 2381622 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam05257 | CHAP | 1.40e-17 | 249 | 336 | 4 | 81 | 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. |
COG3942 | COG3942 | 4.07e-17 | 249 | 349 | 67 | 160 | Surface antigen [Cell wall/membrane/envelope biogenesis]. |
PRK08581 | PRK08581 | 2.56e-16 | 230 | 359 | 490 | 618 | amidase domain-containing protein. |
pfam05382 | Amidase_5 | 3.32e-05 | 80 | 203 | 18 | 140 | Bacteriophage peptidoglycan hydrolase. At least one of the members of this family, the Pal protein from the pneumococcal bacteriophage Dp-1 has been shown to be a N-acetylmuramoyl-L-alanine amidase. According to the known modular structure of this and other peptidoglycan hydrolases from the pneumococcal system, the active site should reside at the N-terminal domain whereas the C-terminal domain binds to the choline residues of the cell wall teichoic acids. This family appears to be related to pfam00877. |
pfam00877 | NLPC_P60 | 3.90e-05 | 91 | 192 | 14 | 95 | NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAQ26934.1 | 0.0 | 1 | 495 | 1 | 495 |
ADB09628.1 | 0.0 | 1 | 495 | 1 | 495 |
VEG23600.1 | 0.0 | 1 | 495 | 1 | 495 |
QGM62701.1 | 4.96e-255 | 19 | 495 | 16 | 495 |
QTL82534.1 | 3.48e-212 | 19 | 495 | 16 | 494 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4CGK_A | 7.61e-09 | 248 | 340 | 285 | 365 | Crystalstructure of the essential protein PcsB from Streptococcus pneumoniae [Streptococcus pneumoniae D39],4CGK_B Crystal structure of the essential protein PcsB from Streptococcus pneumoniae [Streptococcus pneumoniae D39] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q2G278 | 1.42e-11 | 250 | 356 | 178 | 275 | Probable autolysin LDP OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=SAOUHSC_00773 PE=1 SV=1 |
Q8DVU8 | 6.25e-08 | 249 | 325 | 104 | 168 | Putative hydrolase SMU_367 OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=SMU_367 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.992464 | 0.007288 | 0.000030 | 0.000037 | 0.000023 | 0.000161 |
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