Species | Stachybotrys chartarum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum | |||||||||||
CAZyme ID | KFA51384.1 | |||||||||||
CAZy Family | GH17 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 4.2.2.2:30 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 145 | 305 | 3.3e-62 | 0.9558011049723757 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
214765 | Amb_all | 4.14e-44 | 151 | 308 | 14 | 189 | Amb_all domain. |
226384 | PelB | 1.26e-33 | 149 | 370 | 97 | 341 | Pectate lyase [Carbohydrate transport and metabolism]. |
366158 | Pec_lyase_C | 1.56e-26 | 145 | 305 | 26 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.00e-100 | 74 | 373 | 2 | 329 | |
1.32e-95 | 74 | 373 | 2 | 328 | |
1.32e-95 | 74 | 373 | 2 | 328 | |
1.32e-95 | 74 | 373 | 2 | 328 | |
1.32e-95 | 74 | 373 | 2 | 328 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.80e-27 | 116 | 310 | 6 | 251 | 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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8.68e-17 | 110 | 319 | 4 | 290 | Chain A, PECTATE LYASE E [Dickeya chrysanthemi] |
|
2.60e-15 | 148 | 373 | 67 | 328 | Chain A, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
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2.60e-15 | 148 | 373 | 67 | 328 | Chain A, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
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1.27e-14 | 149 | 305 | 64 | 226 | Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.69e-74 | 91 | 364 | 24 | 321 | Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1 |
|
7.26e-72 | 81 | 350 | 7 | 303 | 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 |
|
7.26e-72 | 81 | 350 | 7 | 303 | Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1 |
|
2.22e-70 | 87 | 350 | 11 | 302 | Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1 |
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5.07e-69 | 74 | 364 | 2 | 318 | Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.948168 | 0.051835 |
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