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CAZyme Information: MGYG000001018_01314
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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 | Mediterraneibacter sp900751785 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900751785 | |||||||||||
| CAZyme ID | MGYG000001018_01314 | |||||||||||
| CAZy Family | CBM13 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 17258; End: 21394 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM13 | 944 | 1085 | 2.2e-23 | 0.7074468085106383 |
| CBM13 | 1092 | 1232 | 3.9e-21 | 0.7074468085106383 |
| CBM13 | 807 | 933 | 5.2e-20 | 0.6808510638297872 |
| CBM13 | 507 | 650 | 1.1e-19 | 0.7180851063829787 |
| CBM13 | 1238 | 1319 | 4.5e-19 | 0.4148936170212766 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd02696 | MurNAc-LAA | 5.79e-27 | 289 | 491 | 1 | 172 | N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall. |
| pfam14200 | RicinB_lectin_2 | 1.03e-26 | 1275 | 1362 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
| pfam14200 | RicinB_lectin_2 | 6.43e-24 | 1221 | 1316 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
| pfam14200 | RicinB_lectin_2 | 7.45e-23 | 981 | 1067 | 1 | 88 | Ricin-type beta-trefoil lectin domain-like. |
| pfam14200 | RicinB_lectin_2 | 9.26e-22 | 692 | 775 | 2 | 86 | Ricin-type beta-trefoil lectin domain-like. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRT50579.1 | 3.06e-191 | 135 | 1292 | 119 | 1285 |
| VCV20908.1 | 5.53e-74 | 119 | 872 | 169 | 973 |
| CBL13779.1 | 7.22e-74 | 119 | 498 | 164 | 540 |
| CBL07763.1 | 9.55e-74 | 119 | 498 | 163 | 539 |
| QRO35993.1 | 5.51e-61 | 120 | 604 | 107 | 607 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3PG0_A | 4.42e-10 | 698 | 746 | 22 | 70 | Crystalstructure of designed 3-fold symmetric protein, ThreeFoil [synthetic construct] |
| 5J72_A | 4.36e-07 | 261 | 490 | 428 | 633 | ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630] |
| 2VSA_A | 7.44e-06 | 504 | 842 | 415 | 744 | Structureand mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus],2VSE_A Structure and mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus],2VSE_B Structure and mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O48471 | 2.14e-10 | 289 | 498 | 4 | 185 | Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1 |
| Q9U8Q4 | 1.57e-06 | 647 | 896 | 259 | 519 | Pierisin OS=Pieris rapae OX=64459 PE=1 SV=1 |
| P37134 | 1.60e-06 | 288 | 498 | 2 | 179 | N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.028114 | 0.970569 | 0.000543 | 0.000257 | 0.000237 | 0.000242 |
