Species | Prevotella sp900770025 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900770025 | |||||||||||
CAZyme ID | MGYG000003572_00391 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 39422; End: 41827 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 478 | 648 | 2.2e-39 | 0.8316831683168316 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.86e-50 | 383 | 763 | 17 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 6.70e-27 | 483 | 649 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.02e-14 | 459 | 645 | 8 | 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 |
---|---|---|---|---|---|
QCD40816.1 | 1.10e-288 | 215 | 801 | 2 | 588 |
QCP73706.1 | 1.10e-288 | 215 | 801 | 2 | 588 |
QUT73893.1 | 5.84e-220 | 284 | 801 | 25 | 542 |
QOR20273.1 | 1.24e-207 | 276 | 793 | 44 | 551 |
CBW15186.1 | 2.08e-207 | 276 | 793 | 59 | 566 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 2.18e-29 | 433 | 701 | 33 | 310 | 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] |
1AIR_A | 3.70e-18 | 489 | 761 | 94 | 342 | ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi] |
2EWE_A | 8.94e-18 | 489 | 761 | 94 | 342 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
1VBL_A | 3.96e-17 | 483 | 645 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 2.04e-15 | 485 | 634 | 71 | 225 | Catalyticfunction 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 |
---|---|---|---|---|---|---|
B1B6T1 | 8.08e-27 | 425 | 653 | 62 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 8.08e-27 | 425 | 653 | 62 | 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 |
Q8GCB2 | 8.08e-27 | 425 | 653 | 62 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q5AVN4 | 4.41e-18 | 483 | 658 | 99 | 277 | 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 |
P11073 | 2.60e-17 | 489 | 761 | 116 | 364 | Pectate lyase C OS=Dickeya chrysanthemi OX=556 GN=pelC PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000282 | 0.999086 | 0.000169 | 0.000168 | 0.000145 | 0.000137 |
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