Species | Prevotella sp900540375 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900540375 | |||||||||||
CAZyme ID | MGYG000001001_02130 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 40587; End: 42965 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 471 | 638 | 1.5e-39 | 0.8168316831683168 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 3.29e-50 | 330 | 752 | 2 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 8.53e-29 | 473 | 639 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.26e-14 | 479 | 635 | 42 | 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 | 6.31e-256 | 208 | 789 | 2 | 587 |
QCP73706.1 | 6.31e-256 | 208 | 789 | 2 | 587 |
QUT73893.1 | 1.19e-211 | 274 | 789 | 25 | 541 |
QOR20273.1 | 3.09e-203 | 248 | 785 | 26 | 554 |
CBW15186.1 | 5.21e-203 | 248 | 785 | 41 | 569 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.01e-25 | 474 | 683 | 81 | 300 | 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 | 1.64e-17 | 478 | 711 | 138 | 408 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 6.87e-17 | 479 | 751 | 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 | 1.66e-16 | 479 | 751 | 94 | 342 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
3ZSC_A | 1.56e-14 | 475 | 620 | 71 | 221 | 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 |
---|---|---|---|---|---|---|
Q8GCB2 | 7.95e-24 | 410 | 643 | 57 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 7.95e-24 | 410 | 643 | 57 | 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 |
B1B6T1 | 7.95e-24 | 410 | 643 | 57 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q5AVN4 | 5.85e-18 | 478 | 648 | 104 | 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 | 4.74e-16 | 479 | 751 | 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 |
---|---|---|---|---|---|
0.000278 | 0.999063 | 0.000208 | 0.000161 | 0.000148 | 0.000134 |
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