Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; KM106-2; | |||||||||||
CAZyme ID | MGYG000004891_03186 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7900; End: 10437 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 214 | 418 | 1e-39 | 0.9158415841584159 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 3.37e-32 | 232 | 493 | 97 | 341 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 1.65e-24 | 232 | 417 | 12 | 187 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 2.94e-15 | 301 | 416 | 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. |
pfam04886 | PT | 5.95e-10 | 686 | 721 | 1 | 36 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
pfam04886 | PT | 4.14e-05 | 684 | 709 | 11 | 36 | PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBF42492.1 | 0.0 | 1 | 844 | 1 | 855 |
CDR31241.1 | 7.25e-129 | 14 | 647 | 307 | 896 |
ADU23076.1 | 2.09e-123 | 36 | 489 | 757 | 1228 |
ACR71161.1 | 1.49e-112 | 35 | 504 | 40 | 560 |
ADZ82421.1 | 2.48e-94 | 1 | 658 | 2 | 635 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.55e-18 | 206 | 417 | 43 | 247 | 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 | 1.68e-12 | 231 | 394 | 127 | 302 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5AMV_A | 2.71e-12 | 231 | 400 | 122 | 302 | 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 | 3.02e-12 | 231 | 400 | 143 | 323 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2BSP_A | 7.05e-12 | 231 | 400 | 143 | 323 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GCB2 | 8.67e-16 | 232 | 425 | 104 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 8.67e-16 | 232 | 425 | 104 | 281 | 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 | 8.67e-16 | 232 | 425 | 104 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
P0C1C1 | 4.01e-14 | 188 | 427 | 64 | 289 | Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 SV=1 |
Q6CZT3 | 3.03e-13 | 188 | 427 | 64 | 289 | Pectate lyase 2 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000328 | 0.998240 | 0.000928 | 0.000184 | 0.000173 | 0.000147 |
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