Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; ; | |||||||||||
CAZyme ID | MGYG000004547_01715 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 351; End: 2957 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 224 | 415 | 3.3e-35 | 0.8316831683168316 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 9.34e-29 | 226 | 493 | 97 | 343 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 6.73e-19 | 225 | 418 | 12 | 190 | Amb_all domain. |
pfam18283 | CBM77 | 2.27e-17 | 689 | 791 | 1 | 104 | 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 | 5.52e-12 | 299 | 414 | 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. |
cd14256 | Dockerin_I | 3.24e-08 | 807 | 865 | 2 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBF42492.1 | 5.04e-234 | 28 | 663 | 30 | 675 |
CDR31241.1 | 3.40e-120 | 34 | 522 | 329 | 837 |
ACR71161.1 | 9.14e-110 | 1 | 786 | 1 | 881 |
ADU23076.1 | 3.74e-107 | 38 | 468 | 761 | 1207 |
QEH68115.1 | 1.68e-74 | 38 | 504 | 40 | 487 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 5.14e-22 | 163 | 491 | 24 | 322 | 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] |
2QX3_A | 8.83e-15 | 280 | 497 | 108 | 330 | Structureof pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris],2QX3_B Structure of pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris] |
2QY1_A | 2.13e-14 | 280 | 497 | 108 | 330 | ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
2QXZ_A | 2.13e-14 | 280 | 497 | 108 | 330 | ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
5AMV_A | 6.89e-14 | 231 | 398 | 128 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q65DC2 | 3.31e-18 | 188 | 423 | 81 | 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 | 3.31e-18 | 188 | 423 | 81 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 3.31e-18 | 188 | 423 | 81 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
P0C1C1 | 2.29e-15 | 229 | 422 | 109 | 286 | Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 SV=1 |
Q6CZT3 | 7.32e-15 | 264 | 422 | 136 | 286 | 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 |
---|---|---|---|---|---|
0.000831 | 0.998070 | 0.000310 | 0.000381 | 0.000209 | 0.000170 |
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