| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; ; | |||||||||||
| CAZyme ID | MGYG000004067_00289 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 23017; End: 25989 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 232 | 399 | 1.3e-43 | 0.8267326732673267 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 1.15e-50 | 154 | 403 | 50 | 279 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 2.08e-33 | 234 | 401 | 14 | 190 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 4.07e-18 | 203 | 397 | 1 | 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. |
| cd14256 | Dockerin_I | 6.76e-12 | 931 | 984 | 1 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
| pfam00404 | Dockerin_1 | 4.52e-07 | 932 | 984 | 1 | 56 | Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCJ94010.1 | 1.61e-150 | 38 | 574 | 40 | 563 |
| AQR94278.1 | 3.71e-143 | 39 | 574 | 83 | 593 |
| AGF55382.1 | 1.03e-142 | 39 | 574 | 83 | 593 |
| QGG58534.1 | 1.50e-140 | 2 | 574 | 10 | 562 |
| AIQ21570.1 | 1.67e-140 | 34 | 574 | 29 | 556 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 2.06e-24 | 147 | 399 | 1 | 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] |
| 1AIR_A | 1.53e-18 | 238 | 479 | 91 | 337 | 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 | 3.70e-18 | 238 | 479 | 91 | 337 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
| 1VBL_A | 1.28e-16 | 233 | 397 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1PCL_A | 5.53e-16 | 189 | 425 | 33 | 298 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| B1B6T1 | 8.78e-29 | 184 | 411 | 64 | 286 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q65DC2 | 8.78e-29 | 184 | 411 | 64 | 286 | 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 | 8.78e-29 | 184 | 411 | 64 | 286 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| B8NBC2 | 1.31e-18 | 182 | 400 | 54 | 261 | Probable pectate lyase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyB PE=3 SV=1 |
| Q2TZY0 | 1.31e-18 | 182 | 400 | 54 | 261 | 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 |
|---|---|---|---|---|---|
| 0.000419 | 0.998781 | 0.000181 | 0.000234 | 0.000168 | 0.000153 |
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