Species | Lachnoclostridium phytofermentans_A | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium phytofermentans_A | |||||||||||
CAZyme ID | MGYG000003355_02409 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 405; End: 4088 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 636 | 1043 | 1.5e-128 | 0.984 |
PL1 | 233 | 403 | 3.6e-44 | 0.8366336633663366 |
CBM77 | 1119 | 1217 | 7.4e-35 | 0.9514563106796117 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 5.10e-71 | 100 | 511 | 1 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam18283 | CBM77 | 1.54e-31 | 1118 | 1223 | 3 | 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 | 4.15e-29 | 240 | 405 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 6.05e-17 | 264 | 401 | 61 | 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. |
pfam13229 | Beta_helix | 1.32e-04 | 744 | 923 | 17 | 157 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AOR96287.1 | 0.0 | 34 | 1071 | 48 | 1108 |
QMW93302.1 | 0.0 | 34 | 1071 | 48 | 1108 |
BBK78741.1 | 0.0 | 34 | 1071 | 48 | 1108 |
ADL51369.1 | 0.0 | 29 | 1056 | 41 | 1249 |
ABX41986.1 | 4.23e-307 | 5 | 1061 | 3 | 1168 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1RU4_A | 2.17e-34 | 640 | 1043 | 18 | 374 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
5FU5_A | 1.29e-21 | 1120 | 1223 | 10 | 111 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
3VMV_A | 1.19e-20 | 240 | 403 | 80 | 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] |
1VBL_A | 5.23e-20 | 240 | 401 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 1.18e-19 | 234 | 386 | 63 | 221 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C1A6 | 2.86e-35 | 640 | 1043 | 43 | 399 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
P22751 | 8.34e-34 | 628 | 927 | 378 | 639 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
P0C1A7 | 1.89e-33 | 640 | 1043 | 43 | 399 | Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1 |
Q8GCB2 | 7.90e-27 | 188 | 409 | 62 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 7.90e-27 | 188 | 409 | 62 | 280 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000467 | 0.998715 | 0.000191 | 0.000233 | 0.000190 | 0.000169 |
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