Species | Prevotella sp900769055 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900769055 | |||||||||||
CAZyme ID | MGYG000003513_00316 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3118; End: 5256 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 252 | 418 | 1.5e-37 | 0.8118811881188119 |
CBM77 | 604 | 703 | 7e-23 | 0.9514563106796117 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 1.71e-55 | 174 | 536 | 35 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam18283 | CBM77 | 1.12e-32 | 603 | 705 | 6 | 108 | Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan. |
smart00656 | Amb_all | 1.51e-27 | 254 | 420 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.52e-14 | 254 | 416 | 35 | 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 |
---|---|---|---|---|---|
QUT73893.1 | 3.13e-212 | 68 | 709 | 20 | 683 |
QNT67442.1 | 5.11e-204 | 18 | 712 | 47 | 778 |
QCD40816.1 | 6.53e-202 | 11 | 574 | 1 | 588 |
QCP73706.1 | 6.53e-202 | 11 | 574 | 1 | 588 |
ATA84997.1 | 7.99e-186 | 60 | 567 | 28 | 542 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 7.83e-24 | 174 | 495 | 5 | 326 | 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] |
5FU5_A | 6.15e-16 | 604 | 711 | 12 | 117 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
1VBL_A | 1.30e-12 | 250 | 416 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 3.36e-12 | 256 | 401 | 71 | 221 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
1PCL_A | 8.81e-10 | 254 | 416 | 81 | 276 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q65DC2 | 2.90e-20 | 211 | 424 | 76 | 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 | 2.90e-20 | 211 | 424 | 76 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B1B6T1 | 2.90e-20 | 211 | 424 | 76 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
A1CYB8 | 1.88e-18 | 254 | 442 | 93 | 286 | Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1 |
Q5AVN4 | 5.01e-18 | 254 | 433 | 99 | 281 | 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 |
---|---|---|---|---|---|
0.000426 | 0.998878 | 0.000210 | 0.000158 | 0.000146 | 0.000139 |
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