Species | UMGS1441 sp900551755 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900551755 | |||||||||||
CAZyme ID | MGYG000001183_00883 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 111620; End: 114100 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 236 | 404 | 5e-44 | 0.8217821782178217 |
CBM77 | 647 | 750 | 7.4e-24 | 0.970873786407767 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 2.37e-52 | 101 | 408 | 2 | 279 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 1.57e-32 | 240 | 406 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 2.74e-18 | 238 | 402 | 33 | 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 | 1.33e-11 | 770 | 825 | 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. |
pfam00404 | Dockerin_1 | 5.10e-07 | 771 | 825 | 1 | 56 | Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ACX62589.1 | 2.40e-199 | 1 | 752 | 1 | 680 |
AIQ71967.1 | 3.67e-199 | 1 | 752 | 1 | 714 |
AIQ50255.1 | 5.97e-199 | 1 | 752 | 1 | 729 |
AWV31328.1 | 6.02e-199 | 1 | 752 | 1 | 708 |
ASR49574.1 | 2.83e-198 | 1 | 752 | 1 | 713 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 9.74e-24 | 204 | 404 | 47 | 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] |
1AIR_A | 6.22e-20 | 186 | 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 | 1.51e-19 | 186 | 418 | 22 | 273 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
1VBL_A | 3.09e-18 | 236 | 402 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5FU5_A | 1.12e-16 | 642 | 755 | 5 | 114 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B1B6T1 | 4.63e-27 | 188 | 411 | 67 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 4.63e-27 | 188 | 411 | 67 | 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 |
Q8GCB2 | 4.63e-27 | 188 | 411 | 67 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q6CZT2 | 9.06e-22 | 197 | 418 | 65 | 294 | Pectate lyase 3 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel3 PE=3 SV=1 |
P0C1C2 | 9.06e-22 | 197 | 418 | 65 | 294 | Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001469 | 0.997447 | 0.000287 | 0.000309 | 0.000233 | 0.000214 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.