Species | Prevotella sp900557255 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900557255 | |||||||||||
CAZyme ID | MGYG000002293_01058 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 30511; End: 32409 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 281 | 460 | 2.5e-41 | 0.8762376237623762 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 1.38e-51 | 159 | 573 | 1 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 2.36e-28 | 295 | 461 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.06e-15 | 333 | 457 | 80 | 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 |
---|---|---|---|---|---|
QNT67442.1 | 0.0 | 1 | 626 | 1 | 626 |
QCD40816.1 | 3.15e-210 | 40 | 613 | 1 | 588 |
QCP73706.1 | 3.15e-210 | 40 | 613 | 1 | 588 |
QUT73893.1 | 6.10e-204 | 105 | 617 | 20 | 546 |
ATA84997.1 | 3.36e-193 | 97 | 606 | 32 | 542 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.16e-23 | 206 | 523 | 6 | 311 | 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 | 3.45e-18 | 281 | 571 | 76 | 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 | 8.34e-18 | 281 | 571 | 76 | 342 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
1VBL_A | 1.12e-17 | 295 | 457 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 2.00e-14 | 303 | 572 | 76 | 331 | 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 | 4.91e-22 | 240 | 573 | 60 | 340 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 4.91e-22 | 240 | 573 | 60 | 340 | 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 | 4.91e-22 | 240 | 573 | 60 | 340 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
P11073 | 2.39e-17 | 281 | 571 | 98 | 364 | Pectate lyase C OS=Dickeya chrysanthemi OX=556 GN=pelC PE=1 SV=1 |
Q5AVN4 | 5.08e-15 | 295 | 483 | 99 | 290 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000323 | 0.998934 | 0.000195 | 0.000190 | 0.000178 | 0.000162 |
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