Species | Clostridium neonatale | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale | |||||||||||
CAZyme ID | MGYG000000902_03365 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 182; End: 2446 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 257 | 423 | 4.5e-48 | 0.8168316831683168 |
CBM77 | 647 | 748 | 2.6e-33 | 0.9805825242718447 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 9.85e-76 | 124 | 530 | 6 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 3.34e-36 | 260 | 425 | 17 | 190 | Amb_all domain. |
pfam18283 | CBM77 | 2.05e-21 | 645 | 750 | 2 | 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. |
pfam00544 | Pec_lyase_C | 3.77e-21 | 266 | 421 | 42 | 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 | 0.001 | 272 | 425 | 21 | 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 |
---|---|---|---|---|---|
ACZ98651.1 | 1.87e-292 | 16 | 752 | 12 | 704 |
AQR94278.1 | 4.38e-267 | 7 | 573 | 12 | 598 |
AOR96287.1 | 2.04e-265 | 15 | 575 | 8 | 570 |
AQS15728.1 | 2.92e-265 | 17 | 574 | 18 | 575 |
AGX44552.1 | 2.92e-265 | 17 | 574 | 18 | 575 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 2.31e-22 | 260 | 423 | 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] |
5FU5_A | 6.71e-21 | 647 | 750 | 9 | 111 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
1VBL_A | 8.40e-19 | 260 | 421 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1PCL_A | 1.07e-18 | 205 | 503 | 22 | 348 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
3ZSC_A | 5.51e-17 | 254 | 406 | 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 |
---|---|---|---|---|---|---|
Q8GCB2 | 2.97e-27 | 203 | 430 | 55 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 2.97e-27 | 203 | 430 | 55 | 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 | 2.97e-27 | 203 | 430 | 55 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q5AVN4 | 3.45e-20 | 260 | 434 | 99 | 277 | 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 |
P0C1C3 | 3.67e-20 | 266 | 437 | 115 | 294 | Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000480 | 0.998722 | 0.000239 | 0.000197 | 0.000172 | 0.000153 |
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