Species | Terrisporobacter sp902363255 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Terrisporobacter; Terrisporobacter sp902363255 | |||||||||||
CAZyme ID | MGYG000000102_02991 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 71196; End: 72536 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 7 | 184 | 7.7e-51 | 0.9943502824858758 |
CBM50 | 345 | 387 | 4e-16 | 0.95 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06525 | GH25_Lyc-like | 2.86e-84 | 5 | 193 | 1 | 184 | Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. |
pfam01183 | Glyco_hydro_25 | 3.30e-63 | 7 | 184 | 1 | 180 | Glycosyl hydrolases family 25. |
cd00599 | GH25_muramidase | 2.80e-58 | 5 | 193 | 1 | 186 | Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity. |
COG3757 | Acm | 1.59e-44 | 4 | 198 | 63 | 258 | Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis]. |
cd06524 | GH25_YegX-like | 4.91e-42 | 5 | 194 | 1 | 193 | YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QBJ75914.1 | 1.15e-127 | 5 | 445 | 10 | 442 |
ATD56705.1 | 1.15e-127 | 5 | 445 | 10 | 442 |
SLK20760.1 | 1.15e-127 | 5 | 445 | 10 | 442 |
ATD55618.1 | 1.15e-127 | 5 | 445 | 10 | 442 |
QAS60493.1 | 1.27e-117 | 5 | 387 | 10 | 384 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4KRU_A | 6.21e-54 | 5 | 200 | 21 | 214 | X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
4KRT_A | 1.98e-52 | 5 | 200 | 21 | 214 | X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
5A6S_A | 1.65e-19 | 8 | 195 | 26 | 203 | Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1] |
1JFX_A | 3.62e-19 | 5 | 193 | 6 | 202 | Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor] |
2WAG_A | 6.32e-14 | 3 | 194 | 15 | 207 | TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P26836 | 6.18e-51 | 5 | 197 | 10 | 200 | Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2 |
P34020 | 8.36e-38 | 5 | 199 | 2 | 186 | Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1 |
Q8CMN2 | 9.12e-29 | 223 | 387 | 31 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Q5HRU2 | 9.12e-29 | 223 | 387 | 31 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q49UX4 | 2.52e-28 | 221 | 396 | 29 | 200 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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