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CAZyme Information: MGYG000002433_01153
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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 | Campylobacter_A concisus_P | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter_A; Campylobacter_A concisus_P | |||||||||||
| CAZyme ID | MGYG000002433_01153 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | Pectate lyase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 8470; End: 9720 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 142 | 347 | 2.5e-69 | 0.9859154929577465 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 1.28e-54 | 152 | 350 | 14 | 189 | Amb_all domain. |
| COG3866 | PelB | 7.73e-50 | 138 | 412 | 85 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 2.34e-37 | 127 | 347 | 8 | 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 | 1.66e-287 | 1 | 416 | 1 | 416 |
| QPI00741.1 | 2.75e-286 | 1 | 416 | 1 | 416 |
| QPH98945.1 | 2.75e-286 | 1 | 416 | 1 | 416 |
| QPI07285.1 | 4.55e-285 | 1 | 416 | 1 | 416 |
| QPH83961.1 | 3.07e-283 | 1 | 416 | 1 | 416 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1VBL_A | 1.05e-45 | 33 | 412 | 13 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 5AMV_A | 1.10e-39 | 44 | 412 | 23 | 398 | 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 | 1.18e-39 | 27 | 412 | 19 | 419 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 3.14e-39 | 27 | 412 | 19 | 419 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 2NZM_A | 7.88e-39 | 44 | 412 | 23 | 398 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39116 | 6.43e-39 | 27 | 412 | 19 | 419 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| P04960 | 2.36e-37 | 84 | 412 | 40 | 385 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
| P18209 | 3.63e-36 | 150 | 412 | 112 | 391 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
| P0C1A5 | 3.13e-34 | 150 | 412 | 124 | 404 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| Q51915 | 1.44e-33 | 4 | 412 | 11 | 380 | Pectate lyase OS=Pseudomonas marginalis OX=298 GN=pel PE=1 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 |
|---|---|---|---|---|---|
| 0.000228 | 0.999075 | 0.000180 | 0.000179 | 0.000165 | 0.000148 |