Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
CAZyme ID | MGYG000004708_01203 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 2435; End: 4546 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 79 | 258 | 1.6e-50 | 0.8811881188118812 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 8.86e-57 | 18 | 308 | 29 | 324 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 1.65e-45 | 91 | 259 | 14 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 6.97e-29 | 68 | 255 | 8 | 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. |
pfam16656 | Pur_ac_phosph_N | 0.005 | 339 | 412 | 37 | 94 | Purple acid Phosphatase, N-terminal domain. This domain is found at the N-terminus of Purple acid phosphatase proteins. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CAW91090.1 | 1.12e-56 | 17 | 325 | 51 | 341 |
CAW61449.1 | 1.12e-56 | 17 | 325 | 51 | 341 |
CAX06650.1 | 1.12e-56 | 17 | 325 | 51 | 341 |
CAW70615.1 | 1.12e-56 | 17 | 325 | 51 | 341 |
CAW46004.1 | 1.12e-56 | 17 | 325 | 51 | 341 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 8.03e-35 | 24 | 230 | 7 | 211 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
3VMV_A | 3.39e-26 | 29 | 258 | 7 | 249 | 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] |
1PCL_A | 4.15e-26 | 36 | 230 | 17 | 244 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
5AMV_A | 2.48e-21 | 80 | 246 | 113 | 309 | 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] |
1BN8_A | 3.09e-21 | 80 | 246 | 134 | 330 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9WYR4 | 2.79e-38 | 5 | 230 | 13 | 238 | Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1 |
B1L969 | 4.99e-38 | 5 | 230 | 11 | 236 | Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1 |
O59939 | 1.68e-29 | 36 | 269 | 52 | 279 | Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1 |
Q9C2Z0 | 3.01e-28 | 14 | 325 | 24 | 318 | Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1 |
A2QV36 | 3.01e-28 | 14 | 325 | 24 | 318 | Probable pectate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=plyA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000800 | 0.550953 | 0.447352 | 0.000342 | 0.000289 | 0.000256 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.