Species | Macrophomina phaseolina | |||||||||||
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Lineage | Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina | |||||||||||
CAZyme ID | EKG17806.1 | |||||||||||
CAZy Family | GH47 | |||||||||||
CAZyme Description | Glycoside hydrolase subgroup catalytic core | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH128 | 280 | 502 | 8.9e-53 | 0.9151785714285714 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
371727 | Glyco_hydro_cc | 6.26e-53 | 279 | 490 | 13 | 206 | Glycosyl hydrolase catalytic core. This family is probably a glycosyl hydrolase, and is conserved in fungi and some Proteobacteria. The pombe member is annotated as being from IPR013781. |
236766 | rne | 9.12e-05 | 32 | 239 | 817 | 1030 | ribonuclease E; Reviewed |
215130 | PLN02217 | 0.001 | 166 | 239 | 566 | 650 | probable pectinesterase/pectinesterase inhibitor |
273167 | rad23 | 0.002 | 166 | 235 | 82 | 155 | UV excision repair protein Rad23. All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] |
165527 | PHA03269 | 0.004 | 164 | 262 | 22 | 131 | envelope glycoprotein C; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.31e-42 | 265 | 504 | 178 | 395 | |
1.31e-42 | 265 | 504 | 178 | 395 | |
9.19e-39 | 265 | 493 | 182 | 390 | |
3.76e-38 | 265 | 492 | 32 | 238 | |
4.45e-38 | 265 | 494 | 180 | 389 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.28e-24 | 265 | 490 | 95 | 316 | Crystal structure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Sorangium cellulosum (ScGH128_II) [Sorangium cellulosum So ce56],6UAX_B Crystal structure of a GH128 (subgroup II) endo-beta-1,3-glucanase from Sorangium cellulosum (ScGH128_II) [Sorangium cellulosum So ce56] |
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7.22e-16 | 265 | 494 | 25 | 239 | Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei],6UAR_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose [Amycolatopsis mediterranei] |
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1.78e-15 | 265 | 494 | 25 | 239 | Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) in the complex with laminarihexaose [Amycolatopsis mediterranei],6UFZ_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei] |
|
4.40e-15 | 265 | 494 | 25 | 239 | Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaripentaose [Amycolatopsis mediterranei] |
|
4.40e-15 | 265 | 494 | 25 | 239 | Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaripentaose [Amycolatopsis mediterranei],6UAU_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose and laminaribiose [Amycolatopsis mediterranei] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000666 | 0.999324 | CS pos: 19-20. Pr: 0.9729 |
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