Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; ; | |||||||||||
CAZyme ID | MGYG000004067_01105 | |||||||||||
CAZy Family | CBM13 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6367; End: 8856 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 559 | 754 | 1.6e-79 | 0.9897435897435898 |
CBM13 | 207 | 371 | 2.7e-24 | 0.824468085106383 |
CBM13 | 41 | 193 | 6.1e-21 | 0.7446808510638298 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 9.28e-51 | 508 | 819 | 27 | 341 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam00544 | Pec_lyase_C | 6.56e-40 | 569 | 754 | 26 | 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. |
smart00656 | Amb_all | 1.04e-35 | 565 | 758 | 4 | 190 | Amb_all domain. |
pfam14200 | RicinB_lectin_2 | 8.70e-20 | 174 | 285 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
pfam14200 | RicinB_lectin_2 | 7.33e-19 | 243 | 334 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CDM68184.1 | 9.50e-122 | 364 | 822 | 25 | 486 |
VEB20252.1 | 2.07e-110 | 407 | 827 | 71 | 486 |
QII50179.1 | 2.91e-110 | 407 | 827 | 71 | 486 |
ARC69127.1 | 1.13e-109 | 409 | 827 | 73 | 486 |
AKQ74328.1 | 1.59e-109 | 409 | 827 | 73 | 486 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 4.19e-10 | 530 | 731 | 21 | 212 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
3KRG_A | 2.60e-06 | 573 | 755 | 123 | 326 | ChainA, Pectate lyase [Bacillus subtilis] |
5AMV_A | 2.60e-06 | 573 | 755 | 123 | 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 | 2.73e-06 | 573 | 755 | 144 | 347 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2BSP_A | 6.29e-06 | 573 | 755 | 144 | 347 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94449 | 1.25e-89 | 511 | 826 | 35 | 343 | Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB PE=1 SV=1 |
O34819 | 2.83e-86 | 511 | 826 | 35 | 343 | Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1 |
P27027 | 9.08e-81 | 528 | 826 | 18 | 310 | Pectin lyase OS=Pseudomonas marginalis OX=298 GN=pnl PE=1 SV=2 |
P24112 | 3.91e-78 | 528 | 826 | 18 | 312 | Pectin lyase OS=Pectobacterium carotovorum OX=554 GN=pnl PE=1 SV=1 |
Q00645 | 8.27e-18 | 517 | 731 | 39 | 234 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000393 | 0.998861 | 0.000172 | 0.000232 | 0.000167 | 0.000146 |
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