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CAZyme Information: KFA46516.1
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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 | Stachybotrys chartarum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum | |||||||||||
| CAZyme ID | KFA46516.1 | |||||||||||
| CAZy Family | AA7 | |||||||||||
| CAZyme Description | unspecified product | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 93 | 265 | 1.9e-93 | 0.9886363636363636 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 214765 | Amb_all | 5.48e-56 | 95 | 264 | 12 | 186 | Amb_all domain. |
| 226384 | PelB | 8.05e-56 | 12 | 347 | 8 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| 366158 | Pec_lyase_C | 4.40e-32 | 96 | 264 | 31 | 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 |
|---|---|---|---|---|---|
| 3.53e-174 | 24 | 347 | 8 | 336 | |
| 2.74e-171 | 33 | 347 | 21 | 335 | |
| 4.69e-170 | 25 | 347 | 13 | 335 | |
| 3.70e-169 | 24 | 347 | 13 | 336 | |
| 6.82e-169 | 33 | 347 | 21 | 335 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.64e-41 | 43 | 264 | 5 | 246 | Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5] |
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| 8.84e-32 | 54 | 241 | 21 | 213 | Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
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| 2.78e-29 | 99 | 241 | 132 | 301 | Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
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| 1.02e-23 | 95 | 241 | 123 | 295 | Structural insights 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] |
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| 1.25e-23 | 95 | 241 | 144 | 316 | Bacillus Subtilis 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 |
|---|---|---|---|---|---|---|
| 2.90e-53 | 44 | 272 | 39 | 266 | Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1 |
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| 2.90e-53 | 44 | 272 | 39 | 266 | Probable pectate lyase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyB PE=3 SV=1 |
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| 7.14e-51 | 37 | 347 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
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| 7.14e-51 | 37 | 347 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
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| 7.14e-51 | 37 | 347 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000345 | 0.999626 | CS pos: 17-18. Pr: 0.9762 |