| Species | Barnesiella sp900538555 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900538555 | |||||||||||
| CAZyme ID | MGYG000003099_00682 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 7853; End: 10081 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 219 | 388 | 1.5e-34 | 0.8267326732673267 |
| CBM77 | 565 | 658 | 9e-17 | 0.8737864077669902 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 4.32e-48 | 210 | 499 | 85 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam18283 | CBM77 | 6.97e-21 | 556 | 665 | 1 | 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 | 2.61e-20 | 224 | 384 | 17 | 184 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 4.38e-11 | 198 | 384 | 7 | 209 | 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. |
| pfam18962 | Por_Secre_tail | 0.001 | 690 | 739 | 11 | 68 | Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AQR94278.1 | 2.08e-167 | 21 | 532 | 83 | 594 |
| AQS15728.1 | 3.55e-166 | 23 | 532 | 61 | 570 |
| AGX44552.1 | 3.55e-166 | 23 | 532 | 61 | 570 |
| AQS01745.1 | 3.55e-166 | 23 | 532 | 61 | 570 |
| AQR91843.1 | 3.55e-166 | 23 | 532 | 61 | 570 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 1.20e-19 | 222 | 388 | 78 | 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 | 5.27e-12 | 219 | 405 | 85 | 276 | 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] |
| 3ZSC_A | 8.50e-12 | 220 | 363 | 65 | 213 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
| 2EWE_A | 1.25e-11 | 219 | 405 | 85 | 276 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
| 1VBL_A | 2.36e-11 | 223 | 364 | 132 | 302 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8GCB2 | 2.47e-19 | 162 | 364 | 58 | 250 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| Q65DC2 | 2.47e-19 | 162 | 364 | 58 | 250 | 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 | 2.47e-19 | 162 | 364 | 58 | 250 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| P0C1C3 | 7.79e-15 | 219 | 405 | 106 | 297 | Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1 |
| P0C1C2 | 1.04e-14 | 219 | 405 | 106 | 297 | Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000760 | 0.977499 | 0.020910 | 0.000351 | 0.000229 | 0.000205 |
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