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CAZyme Information: MGYG000001379_02683
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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 | Schaedlerella glycyrrhizinilytica | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Schaedlerella; Schaedlerella glycyrrhizinilytica | |||||||||||
| CAZyme ID | MGYG000001379_02683 | |||||||||||
| CAZy Family | GH0 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 117969; End: 119261 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01471 | PG_binding_1 | 1.46e-13 | 355 | 416 | 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. |
| COG3409 | PGRP | 8.27e-09 | 349 | 416 | 38 | 102 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
| COG3409 | PGRP | 2.76e-05 | 346 | 416 | 117 | 183 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
| pfam13620 | CarboxypepD_reg | 0.001 | 39 | 125 | 13 | 81 | Carboxypeptidase regulatory-like domain. |
| pfam08486 | SpoIID | 0.002 | 198 | 272 | 15 | 93 | Stage II sporulation protein. This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QEI32542.1 | 3.75e-252 | 22 | 429 | 21 | 429 |
| QHB25032.1 | 3.75e-252 | 22 | 429 | 21 | 429 |
| QRT31086.1 | 5.73e-252 | 22 | 429 | 23 | 431 |
| QRT50293.1 | 1.19e-243 | 5 | 429 | 3 | 418 |
| QUO33025.1 | 2.11e-232 | 25 | 429 | 12 | 417 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1LBU_A | 9.28e-06 | 344 | 419 | 5 | 76 | HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G] |
Swiss-Prot Hits help
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 |
|---|---|---|---|---|---|
| 1.000050 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |