Species | Prevotella sp900313215 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900313215 | |||||||||||
CAZyme ID | MGYG000001770_01928 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 15831; End: 17402 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 132 | 341 | 1.4e-43 | 0.8415841584158416 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
smart00656 | Amb_all | 3.07e-38 | 134 | 342 | 12 | 190 | Amb_all domain. |
COG3866 | PelB | 3.82e-37 | 24 | 427 | 13 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam00544 | Pec_lyase_C | 5.70e-23 | 119 | 338 | 11 | 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 |
---|---|---|---|---|---|
QUT75310.1 | 1.04e-122 | 42 | 428 | 23 | 384 |
QNH62939.1 | 4.16e-39 | 63 | 427 | 77 | 378 |
QHJ07062.1 | 4.14e-38 | 65 | 427 | 66 | 369 |
AAR45486.1 | 4.36e-36 | 42 | 427 | 2 | 300 |
CAW79729.1 | 5.54e-36 | 19 | 427 | 18 | 339 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 8.48e-25 | 63 | 343 | 12 | 251 | 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] |
2QXZ_A | 1.53e-20 | 209 | 347 | 110 | 255 | ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
2QY1_A | 1.53e-20 | 209 | 347 | 110 | 255 | ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
1VBL_A | 5.29e-20 | 83 | 338 | 91 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5AMV_A | 6.11e-20 | 167 | 427 | 150 | 398 | 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 | 1.11e-36 | 19 | 427 | 18 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 1.11e-36 | 19 | 427 | 18 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 1.11e-36 | 19 | 427 | 18 | 339 | 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 |
Q00645 | 1.29e-20 | 63 | 340 | 45 | 260 | Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1 |
Q2TZY0 | 1.07e-19 | 63 | 328 | 45 | 240 | Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001151 | 0.995987 | 0.001943 | 0.000363 | 0.000287 | 0.000255 |
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