Species | Magnaporthiopsis poae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU86099.1 | |||||||||||
CAZy Family | GH15 | |||||||||||
CAZyme Description | Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0C4DYJ6] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 4.2.2.2:31 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 77 | 257 | 2.7e-83 | 0.988950276243094 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
214765 | Amb_all | 6.95e-61 | 77 | 261 | 2 | 190 | Amb_all domain. |
226384 | PelB | 3.59e-48 | 3 | 316 | 1 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
366158 | Pec_lyase_C | 4.50e-37 | 87 | 257 | 30 | 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 |
---|---|---|---|---|---|
4.40e-119 | 1 | 321 | 1 | 330 | |
4.26e-117 | 1 | 321 | 1 | 331 | |
6.04e-117 | 1 | 321 | 1 | 331 | |
8.01e-117 | 12 | 320 | 9 | 328 | |
7.25e-115 | 12 | 320 | 9 | 327 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.78e-31 | 38 | 265 | 6 | 254 | 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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1.75e-30 | 33 | 278 | 5 | 295 | Chain A, PECTATE LYASE E [Dickeya chrysanthemi] |
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7.65e-26 | 45 | 316 | 8 | 323 | Chain A, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
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3.87e-25 | 46 | 316 | 9 | 323 | Chain A, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
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6.21e-25 | 37 | 235 | 7 | 214 | 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 |
---|---|---|---|---|---|---|
1.76e-106 | 25 | 321 | 35 | 331 | Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1 |
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5.39e-94 | 12 | 319 | 9 | 326 | Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1 |
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5.39e-94 | 12 | 319 | 9 | 326 | 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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3.07e-93 | 33 | 319 | 34 | 326 | 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 |
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5.49e-91 | 8 | 319 | 5 | 325 | Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000248 | 0.999733 | CS pos: 28-29. Pr: 0.9230 |
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