Species | Clostridium_J sp902363375 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_J; Clostridium_J sp902363375 | |||||||||||
CAZyme ID | MGYG000000115_01593 | |||||||||||
CAZy Family | GH0 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 69161; End: 70933 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3409 | PGRP | 3.98e-20 | 327 | 488 | 39 | 180 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
COG3409 | PGRP | 4.17e-20 | 425 | 580 | 39 | 180 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
pfam01471 | PG_binding_1 | 5.69e-14 | 522 | 583 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
pfam01471 | PG_binding_1 | 3.93e-13 | 430 | 491 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
pfam01471 | PG_binding_1 | 2.21e-12 | 332 | 394 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGH20837.1 | 2.22e-114 | 4 | 413 | 5 | 419 |
QSX02883.1 | 2.22e-114 | 4 | 413 | 5 | 419 |
QMW92695.1 | 2.22e-114 | 4 | 413 | 5 | 419 |
AXB86494.1 | 2.22e-114 | 4 | 413 | 5 | 419 |
QUF83418.1 | 2.22e-114 | 4 | 413 | 5 | 419 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5TV7_A | 1.56e-08 | 516 | 583 | 108 | 169 | ChainA, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630],5TV7_B Chain B, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630] |
5NM7_A | 1.57e-07 | 517 | 589 | 5 | 71 | Crystalstructure of Burkholderia AP3 phage endolysin [Burkholderia],5NM7_G Crystal structure of Burkholderia AP3 phage endolysin [Burkholderia] |
3BKH_A | 1.23e-06 | 424 | 495 | 11 | 77 | ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ] |
6TCI_A | 5.08e-06 | 512 | 588 | 2 | 73 | Thecrystal structure of SleB N-terminal domain [Bacillus cereus ATCC 14579] |
1LBU_A | 5.79e-06 | 517 | 589 | 10 | 79 | HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q99125 | 1.54e-11 | 417 | 588 | 187 | 354 | Probable N-acetylmuramoyl-L-alanine amidase OS=Bacillus licheniformis OX=1402 PE=3 SV=1 |
P36550 | 2.12e-09 | 344 | 579 | 138 | 351 | N-acetylmuramoyl-L-alanine amidase CwlL OS=Bacillus licheniformis OX=1402 GN=cwlL PE=3 SV=1 |
L7N653 | 3.93e-06 | 422 | 579 | 9 | 156 | N-acetylmuramoyl-L-alanine amidase CwlM OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cwlM PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000032 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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