Species | Paenibacillus lautus_A | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lautus_A | |||||||||||
CAZyme ID | MGYG000001371_02505 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 14308; End: 16371 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM77 | 581 | 682 | 2.5e-47 | 0.9805825242718447 |
PL1 | 237 | 404 | 7.7e-43 | 0.8217821782178217 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 1.33e-52 | 127 | 518 | 30 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam18283 | CBM77 | 2.58e-47 | 578 | 684 | 1 | 108 | Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan. |
smart00656 | Amb_all | 7.15e-32 | 241 | 402 | 17 | 186 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 2.37e-20 | 239 | 402 | 33 | 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 |
---|---|---|---|---|---|
AYB46946.1 | 0.0 | 1 | 687 | 1 | 685 |
ACX62589.1 | 0.0 | 1 | 687 | 1 | 683 |
QOT09127.1 | 0.0 | 1 | 687 | 1 | 685 |
AET58470.1 | 0.0 | 1 | 687 | 1 | 716 |
ASR49574.1 | 0.0 | 1 | 687 | 1 | 716 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FU5_A | 3.50e-29 | 578 | 685 | 6 | 112 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
3VMV_A | 6.05e-23 | 186 | 402 | 27 | 246 | Crystalstructure 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] |
1PCL_A | 3.36e-21 | 200 | 462 | 42 | 325 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
1VBL_A | 9.41e-20 | 237 | 402 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
2QY1_A | 3.16e-17 | 229 | 411 | 66 | 255 | ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B1B6T1 | 5.14e-26 | 182 | 411 | 59 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 5.14e-26 | 182 | 411 | 59 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 5.14e-26 | 182 | 411 | 59 | 281 | 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 |
P0C1C3 | 1.22e-21 | 157 | 454 | 32 | 335 | Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1 |
Q6CZT2 | 2.21e-21 | 157 | 454 | 32 | 335 | Pectate lyase 3 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel3 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000695 | 0.997767 | 0.000904 | 0.000231 | 0.000197 | 0.000177 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.