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CAZyme Information: EEU36368.1
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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 | Fusarium vanettenii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii | |||||||||||
| CAZyme ID | EEU36368.1 | |||||||||||
| CAZy Family | CE16 | |||||||||||
| CAZyme Description | polysaccharide lyase family 1 | |||||||||||
| 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 | 80 | 260 | 1.1e-99 | 0.9943181818181818 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 214765 | Amb_all | 4.09e-53 | 83 | 259 | 12 | 186 | Amb_all domain. |
| 226384 | PelB | 3.23e-52 | 3 | 342 | 10 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| 366158 | Pec_lyase_C | 2.14e-34 | 85 | 259 | 32 | 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 |
|---|---|---|---|---|---|
| 2.39e-245 | 1 | 344 | 1 | 337 | |
| 1.26e-217 | 11 | 343 | 11 | 336 | |
| 4.86e-216 | 11 | 344 | 11 | 337 | |
| 6.06e-213 | 20 | 343 | 5 | 324 | |
| 4.86e-212 | 11 | 344 | 11 | 340 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.93e-39 | 29 | 273 | 3 | 261 | 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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| 2.87e-31 | 85 | 342 | 130 | 415 | Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
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| 1.08e-27 | 36 | 233 | 16 | 214 | Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
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| 2.51e-26 | 32 | 236 | 10 | 246 | Chain A, PECTATE LYASE E [Dickeya chrysanthemi] |
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| 1.33e-23 | 85 | 237 | 125 | 296 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.28e-55 | 32 | 323 | 44 | 307 | Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1 |
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| 2.69e-52 | 32 | 323 | 40 | 303 | Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1 |
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| 2.69e-52 | 32 | 323 | 40 | 303 | Probable pectate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=plyA PE=3 SV=1 |
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| 8.50e-52 | 25 | 342 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
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| 8.50e-52 | 25 | 342 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000327 | 0.999653 | CS pos: 17-18. Pr: 0.9841 |