Species | Kwoniella heveanensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella heveanensis | |||||||||||
CAZyme ID | I317_07117-t43_1-p1 | |||||||||||
CAZy Family | GT69 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 226 | 378 | 1.5e-27 | 0.8909090909090909 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238141 | SGNH_hydrolase | 5.09e-16 | 198 | 388 | 1 | 187 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
404371 | Lipase_GDSL_2 | 5.10e-06 | 220 | 380 | 11 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
225353 | TesA | 7.83e-06 | 228 | 393 | 32 | 212 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
238863 | SGNH_hydrolase_peri1 | 1.96e-04 | 249 | 385 | 33 | 181 | SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
238873 | SGNH_hydrolase_like_3 | 0.001 | 196 | 386 | 2 | 190 | SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.75e-60 | 152 | 614 | 705 | 1123 | |
2.37e-60 | 152 | 614 | 705 | 1123 | |
8.22e-55 | 173 | 639 | 351 | 753 | |
1.24e-19 | 182 | 390 | 19 | 211 | |
1.36e-19 | 167 | 390 | 8 | 211 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.51e-19 | 163 | 390 | 4 | 211 | Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82] |
|
1.18e-17 | 163 | 390 | 4 | 211 | Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000059 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.