Species | CAG-274 sp000432155 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; CAG-274; CAG-274 sp000432155 | |||||||||||
CAZyme ID | MGYG000001160_00492 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 67384; End: 70776 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 229 | 422 | 1.8e-38 | 0.8613861386138614 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.19e-26 | 238 | 420 | 99 | 273 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 8.22e-24 | 239 | 420 | 15 | 186 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 7.58e-13 | 305 | 420 | 89 | 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 | 4.51e-06 | 1059 | 1120 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ADU23076.1 | 1.18e-152 | 32 | 509 | 759 | 1242 |
BBF42492.1 | 1.96e-149 | 1 | 654 | 1 | 667 |
ACR71161.1 | 2.94e-143 | 33 | 620 | 44 | 655 |
CDR31241.1 | 7.07e-127 | 30 | 635 | 329 | 907 |
QEH68115.1 | 9.22e-76 | 24 | 505 | 27 | 478 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.78e-21 | 200 | 423 | 47 | 249 | 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 | 5.26e-10 | 240 | 421 | 132 | 331 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5AMV_A | 1.51e-09 | 307 | 421 | 195 | 326 | 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] |
1BN8_A | 1.64e-09 | 307 | 421 | 216 | 347 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2BSP_A | 3.79e-09 | 307 | 421 | 216 | 347 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q65DC2 | 1.89e-12 | 173 | 508 | 54 | 341 | 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 | 1.89e-12 | 173 | 508 | 54 | 341 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 1.89e-12 | 173 | 508 | 54 | 341 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q5AVN4 | 2.20e-12 | 240 | 442 | 98 | 286 | 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 |
Q59671 | 6.19e-12 | 307 | 505 | 181 | 379 | Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000225 | 0.999178 | 0.000161 | 0.000158 | 0.000137 | 0.000129 |
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