Species | Ruminococcus_F champanellensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_F; Ruminococcus_F champanellensis | |||||||||||
CAZyme ID | MGYG000001375_00636 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 709593; End: 712340 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 262 | 446 | 1.7e-55 | 0.9076923076923077 |
CBM13 | 557 | 701 | 3.8e-26 | 0.6968085106382979 |
CBM13 | 712 | 852 | 1.2e-18 | 0.6914893617021277 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 1.23e-44 | 185 | 517 | 33 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 9.08e-20 | 258 | 446 | 10 | 186 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.06e-18 | 234 | 443 | 2 | 208 | 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. |
pfam14200 | RicinB_lectin_2 | 3.97e-18 | 642 | 740 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
pfam14200 | RicinB_lectin_2 | 6.15e-18 | 596 | 685 | 5 | 89 | Ricin-type beta-trefoil lectin domain-like. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL16867.1 | 0.0 | 1 | 915 | 1 | 915 |
CDM68184.1 | 1.58e-120 | 36 | 615 | 29 | 584 |
VEB20252.1 | 2.01e-96 | 33 | 530 | 28 | 488 |
QII50179.1 | 2.01e-96 | 33 | 530 | 28 | 488 |
AJO19478.1 | 1.07e-95 | 33 | 530 | 28 | 488 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 2.68e-11 | 198 | 423 | 14 | 212 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
5B2H_A | 1.34e-06 | 626 | 753 | 163 | 281 | Crystalstructure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum],5B2H_B Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94449 | 2.96e-59 | 182 | 521 | 32 | 339 | Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB PE=1 SV=1 |
O34819 | 3.79e-58 | 182 | 521 | 32 | 339 | Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1 |
P27027 | 7.32e-51 | 198 | 521 | 12 | 306 | Pectin lyase OS=Pseudomonas marginalis OX=298 GN=pnl PE=1 SV=2 |
P24112 | 9.03e-47 | 182 | 521 | 7 | 308 | Pectin lyase OS=Pectobacterium carotovorum OX=554 GN=pnl PE=1 SV=1 |
Q00645 | 9.58e-12 | 191 | 423 | 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 |
---|---|---|---|---|---|
0.001469 | 0.997603 | 0.000289 | 0.000235 | 0.000189 | 0.000190 |
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