Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; | |||||||||||
CAZyme ID | MGYG000001833_01520 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2393; End: 7387 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 1203 | 1554 | 4.3e-89 | 0.9755434782608695 |
PL1 | 238 | 404 | 7.9e-41 | 0.8118811881188119 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 3.24e-47 | 128 | 408 | 34 | 279 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 3.10e-34 | 240 | 406 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 3.53e-18 | 207 | 402 | 1 | 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 | 3.49e-10 | 1309 | 1518 | 2 | 157 | Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases. |
cd14256 | Dockerin_I | 1.56e-09 | 866 | 920 | 1 | 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 |
---|---|---|---|---|---|
ACX62589.1 | 2.19e-140 | 44 | 587 | 44 | 567 |
QOT09127.1 | 3.08e-138 | 28 | 587 | 30 | 567 |
AYB46946.1 | 5.90e-138 | 44 | 587 | 44 | 567 |
ASR49574.1 | 2.04e-137 | 5 | 590 | 1 | 567 |
AIQ38798.1 | 1.28e-136 | 5 | 590 | 1 | 570 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 2.14e-24 | 183 | 404 | 24 | 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 | 4.45e-17 | 240 | 402 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 1.45e-13 | 184 | 418 | 22 | 273 | ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi] |
2EWE_A | 3.44e-13 | 184 | 418 | 22 | 273 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
1PCL_A | 1.49e-12 | 199 | 432 | 39 | 300 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94576 | 3.96e-38 | 1195 | 1605 | 27 | 434 | Uncharacterized protein YwoF OS=Bacillus subtilis (strain 168) OX=224308 GN=ywoF PE=3 SV=1 |
B1B6T1 | 6.28e-24 | 191 | 416 | 63 | 286 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 6.28e-24 | 191 | 416 | 63 | 286 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 6.28e-24 | 191 | 416 | 63 | 286 | 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 |
Q5AVN4 | 5.22e-16 | 223 | 421 | 82 | 283 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000241 | 0.999093 | 0.000171 | 0.000188 | 0.000149 | 0.000140 |
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