Species | Prevotella sp900548535 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548535 | |||||||||||
CAZyme ID | MGYG000000553_00455 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 191282; End: 193075 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 276 | 445 | 1.4e-39 | 0.8168316831683168 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.40e-52 | 137 | 557 | 1 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 3.60e-30 | 279 | 445 | 19 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 2.85e-18 | 279 | 441 | 38 | 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 |
---|---|---|---|---|---|
ACX75949.1 | 1.18e-197 | 79 | 588 | 20 | 544 |
AWK03841.1 | 1.05e-196 | 76 | 597 | 17 | 529 |
ABQ04263.1 | 1.06e-191 | 73 | 596 | 13 | 528 |
AIF26139.1 | 2.88e-191 | 119 | 588 | 2 | 488 |
AIF26212.1 | 2.33e-190 | 119 | 588 | 2 | 488 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.73e-21 | 278 | 443 | 81 | 248 | 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 | 2.41e-15 | 279 | 441 | 135 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 1.83e-14 | 279 | 426 | 71 | 221 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
1AIR_A | 2.75e-14 | 272 | 459 | 85 | 275 | 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 | 6.58e-14 | 272 | 459 | 85 | 275 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GCB2 | 4.82e-21 | 217 | 450 | 55 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 4.82e-21 | 217 | 450 | 55 | 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 |
B1B6T1 | 4.82e-21 | 217 | 450 | 55 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q5AVN4 | 9.64e-21 | 279 | 454 | 101 | 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 |
B0XT32 | 8.54e-18 | 267 | 454 | 81 | 271 | Probable pectate lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000289 | 0.998963 | 0.000211 | 0.000186 | 0.000170 | 0.000154 |
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