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CAZyme Information: FFUJ_12455-t31_1-p1
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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 fujikuroi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi | |||||||||||
| CAZyme ID | FFUJ_12455-t31_1-p1 | |||||||||||
| CAZy Family | GH88 | |||||||||||
| CAZyme Description | probable pectate lyase 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 | 65 | 241 | 1e-104 | 0.9943181818181818 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 214765 | Amb_all | 3.43e-55 | 68 | 240 | 12 | 186 | Amb_all domain. |
| 226384 | PelB | 2.11e-49 | 41 | 323 | 62 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| 366158 | Pec_lyase_C | 4.78e-36 | 66 | 240 | 28 | 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 |
|---|---|---|---|---|---|
| 2.77e-247 | 1 | 324 | 1 | 324 | |
| 1.04e-238 | 6 | 324 | 21 | 339 | |
| 1.50e-238 | 6 | 324 | 21 | 336 | |
| 1.79e-236 | 6 | 324 | 21 | 336 | |
| 8.69e-220 | 5 | 324 | 20 | 336 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4.92e-37 | 14 | 254 | 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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| 2.62e-32 | 70 | 323 | 130 | 415 | Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
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| 2.77e-29 | 27 | 323 | 21 | 331 | Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
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| 1.24e-26 | 17 | 240 | 10 | 276 | Chain A, PECTATE LYASE E [Dickeya chrysanthemi] |
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| 5.39e-25 | 70 | 218 | 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 |
|---|---|---|---|---|---|---|
| 5.99e-53 | 17 | 304 | 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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| 1.22e-52 | 10 | 323 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
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| 1.22e-52 | 10 | 323 | 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 |
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| 1.22e-52 | 10 | 323 | 39 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
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| 4.54e-52 | 17 | 248 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000057 | 0.000000 |