Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; | |||||||||||
CAZyme ID | MGYG000004634_01141 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1022; End: 5212 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 243 | 434 | 4.8e-33 | 0.8613861386138614 |
CBM77 | 789 | 891 | 9.3e-17 | 0.9320388349514563 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.84e-26 | 251 | 523 | 98 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 4.87e-15 | 255 | 436 | 17 | 190 | Amb_all domain. |
cd14256 | Dockerin_I | 1.95e-12 | 1333 | 1388 | 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. |
pfam00544 | Pec_lyase_C | 1.78e-09 | 290 | 432 | 64 | 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. |
pfam00404 | Dockerin_1 | 1.10e-07 | 1334 | 1388 | 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 |
---|---|---|---|---|---|
BBF42492.1 | 3.11e-134 | 34 | 527 | 39 | 504 |
ACR71161.1 | 7.39e-97 | 33 | 910 | 43 | 901 |
ADU23076.1 | 1.96e-96 | 35 | 527 | 761 | 1239 |
CDR31241.1 | 1.09e-84 | 40 | 530 | 338 | 812 |
ADZ82421.1 | 1.77e-69 | 1 | 526 | 2 | 478 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 7.16e-18 | 254 | 437 | 79 | 251 | 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 | 1.84e-12 | 253 | 432 | 131 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 2.12e-12 | 211 | 442 | 50 | 267 | 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 | 5.02e-12 | 211 | 442 | 50 | 267 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
5AMV_A | 3.77e-11 | 229 | 416 | 102 | 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 |
---|---|---|---|---|---|---|
P0C1C3 | 4.17e-16 | 238 | 442 | 94 | 288 | Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1 |
P0C1C2 | 7.46e-16 | 249 | 442 | 105 | 288 | Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 PE=1 SV=1 |
Q65DC2 | 9.18e-16 | 255 | 495 | 109 | 324 | 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 | 9.18e-16 | 255 | 495 | 109 | 324 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 9.18e-16 | 255 | 495 | 109 | 324 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000493 | 0.998622 | 0.000324 | 0.000201 | 0.000171 | 0.000167 |
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