Species | Paenibacillus odorifer | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer | |||||||||||
CAZyme ID | MGYG000002414_00220 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 218257; End: 220392 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM77 | 606 | 706 | 5.6e-49 | 0.9805825242718447 |
PL1 | 237 | 403 | 1e-42 | 0.8168316831683168 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 2.09e-52 | 96 | 407 | 2 | 279 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam18283 | CBM77 | 4.26e-44 | 603 | 708 | 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 | 2.51e-31 | 240 | 401 | 17 | 186 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.83e-19 | 207 | 401 | 1 | 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 |
---|---|---|---|---|---|
AWV31328.1 | 0.0 | 1 | 711 | 1 | 711 |
AIQ71967.1 | 0.0 | 1 | 711 | 1 | 717 |
CQR51569.1 | 0.0 | 1 | 711 | 1 | 729 |
AIQ21570.1 | 0.0 | 1 | 711 | 1 | 713 |
QSF45311.1 | 0.0 | 1 | 711 | 1 | 730 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FU5_A | 1.34e-31 | 602 | 709 | 5 | 112 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
3VMV_A | 9.51e-25 | 204 | 401 | 47 | 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] |
1VBL_A | 3.19e-19 | 236 | 401 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1PCL_A | 1.31e-18 | 199 | 401 | 42 | 276 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
5AMV_A | 6.80e-17 | 240 | 463 | 128 | 381 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B1B6T1 | 1.08e-27 | 172 | 409 | 54 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 1.08e-27 | 172 | 409 | 54 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 1.08e-27 | 172 | 409 | 54 | 280 | 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 |
Q5AVN4 | 1.41e-19 | 240 | 405 | 99 | 268 | Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1 |
P04959 | 6.43e-19 | 246 | 427 | 115 | 304 | Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000386 | 0.998809 | 0.000190 | 0.000222 | 0.000188 | 0.000172 |
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