Species | Lachnospira sp000436475 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp000436475 | |||||||||||
CAZyme ID | MGYG000002580_00918 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 25481; End: 28162 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 231 | 412 | 5.6e-42 | 0.8762376237623762 |
CBM77 | 669 | 768 | 1.8e-31 | 0.9611650485436893 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.13e-47 | 137 | 462 | 34 | 321 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 7.33e-35 | 248 | 414 | 19 | 190 | Amb_all domain. |
pfam18283 | CBM77 | 6.97e-30 | 669 | 770 | 6 | 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 | 1.12e-19 | 216 | 410 | 14 | 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 | 2.66e-07 | 262 | 466 | 2 | 155 | 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 |
---|---|---|---|---|---|
ACR72247.1 | 4.41e-209 | 1 | 570 | 1 | 573 |
ACR72246.1 | 2.16e-207 | 1 | 784 | 1 | 744 |
BCJ94010.1 | 7.29e-193 | 45 | 770 | 47 | 712 |
AIQ38798.1 | 7.41e-192 | 48 | 770 | 43 | 709 |
CQR51569.1 | 5.10e-191 | 48 | 770 | 43 | 726 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FU5_A | 5.61e-23 | 669 | 772 | 11 | 113 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
3VMV_A | 1.93e-20 | 195 | 412 | 31 | 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 | 1.44e-14 | 242 | 410 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 1.19e-13 | 190 | 425 | 24 | 272 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q65DC2 | 3.13e-23 | 198 | 439 | 71 | 304 | 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 | 3.13e-23 | 198 | 439 | 71 | 304 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B1B6T1 | 3.13e-23 | 198 | 439 | 71 | 304 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
P0C1C2 | 2.25e-17 | 215 | 425 | 84 | 293 | Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 PE=1 SV=1 |
P0C1C3 | 5.41e-17 | 194 | 425 | 46 | 293 | 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 |
---|---|---|---|---|---|
0.003976 | 0.994955 | 0.000360 | 0.000269 | 0.000202 | 0.000203 |
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