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CAZyme Information: MGYG000003575_01013
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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 | Treponema_D sp900770075 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900770075 | |||||||||||
| CAZyme ID | MGYG000003575_01013 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2934; End: 4424 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 249 | 450 | 1.5e-61 | 0.9812206572769953 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 3.83e-43 | 246 | 453 | 2 | 189 | Amb_all domain. |
| COG3866 | PelB | 9.22e-33 | 243 | 496 | 84 | 343 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 7.27e-32 | 255 | 450 | 29 | 211 | Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QPH85838.1 | 1.35e-78 | 136 | 496 | 24 | 411 |
| QPI07285.1 | 1.90e-78 | 136 | 496 | 24 | 411 |
| QPI00741.1 | 3.77e-78 | 136 | 496 | 24 | 411 |
| QPH98945.1 | 3.77e-78 | 136 | 496 | 24 | 411 |
| QPH93180.1 | 1.05e-77 | 136 | 452 | 24 | 349 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AMV_A | 1.27e-38 | 166 | 421 | 43 | 295 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
| 1BN8_A | 1.88e-38 | 166 | 421 | 64 | 316 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 4.93e-38 | 166 | 421 | 64 | 316 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 2NZM_A | 8.81e-38 | 166 | 421 | 43 | 295 | ChainA, Pectate lyase [Bacillus subtilis],2O04_A Chain A, Pectate lyase [Bacillus subtilis],2O0V_A Chain A, Pectate lyase [Bacillus subtilis],2O0W_A Chain A, Pectate lyase [Bacillus subtilis],2O17_A Chain A, Pectate lyase [Bacillus subtilis],2O1D_A Chain A, Pectate lyase [Bacillus subtilis] |
| 1VBL_A | 1.06e-35 | 178 | 450 | 60 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39116 | 1.03e-37 | 166 | 421 | 64 | 316 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| P0C1A4 | 2.17e-33 | 157 | 450 | 47 | 324 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=3 SV=1 |
| P0C1A5 | 2.17e-33 | 157 | 450 | 47 | 324 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| P18209 | 1.08e-31 | 255 | 450 | 111 | 312 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
| P04960 | 8.89e-31 | 200 | 450 | 73 | 306 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000034 | 0.000658 | 0.999352 | 0.000006 | 0.000002 | 0.000001 |