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CAZyme Information: MGYG000001624_02851
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Proteus cibarius | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus cibarius | |||||||||||
| CAZyme ID | MGYG000001624_02851 | |||||||||||
| CAZy Family | GH25 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 410; End: 1402 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH25 | 6 | 185 | 3.2e-45 | 0.9887005649717514 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06417 | GH25_LysA-like | 7.76e-96 | 3 | 202 | 1 | 195 | LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis. |
| pfam01183 | Glyco_hydro_25 | 4.19e-58 | 6 | 186 | 1 | 180 | Glycosyl hydrolases family 25. |
| pfam16775 | ZoocinA_TRD | 3.76e-50 | 225 | 329 | 1 | 106 | Target recognition domain of lytic exoenzyme. ZoocinA_TRD is domain found downstream of various lytic enzymes, such as peptidase M23 and phage lysins. The domain is composed of strands of antiparallel beta sheet with one short alpha helix at the C-terminal end. |
| cd00599 | GH25_muramidase | 1.01e-40 | 5 | 195 | 2 | 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. |
| cd06525 | GH25_Lyc-like | 1.47e-35 | 4 | 195 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AAR59481.1 | 8.92e-254 | 1 | 330 | 5 | 334 |
| QRG96708.1 | 3.76e-248 | 1 | 330 | 4 | 333 |
| QSO20641.1 | 3.76e-248 | 1 | 330 | 4 | 333 |
| QFY93950.2 | 3.76e-248 | 1 | 330 | 4 | 333 |
| QSO28228.1 | 3.76e-248 | 1 | 330 | 4 | 333 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2LS0_1 | 2.65e-17 | 228 | 330 | 24 | 127 | SolutionStructure of the Target Recognition Domain of Zoocin A [Streptococcus equi subsp. zooepidemicus] |
| 4KRU_A | 4.00e-15 | 3 | 195 | 20 | 207 | X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
| 4KRT_A | 1.57e-14 | 3 | 195 | 20 | 207 | 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] |
| 2WAG_A | 3.76e-13 | 3 | 206 | 16 | 217 | TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames] |
| 6ZMV_A | 9.34e-10 | 5 | 191 | 4 | 198 | ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8FFY2 | 2.18e-14 | 2 | 197 | 66 | 256 | Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2 |
| P76421 | 4.05e-14 | 2 | 197 | 66 | 256 | Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2 |
| Q8X7H0 | 5.52e-14 | 2 | 197 | 66 | 256 | Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2 |
| P00721 | 1.17e-09 | 2 | 125 | 1 | 139 | N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |