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CAZyme Information: MGYG000002602_01646
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | CAG-274 sp900545305 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; CAG-274; CAG-274 sp900545305 | |||||||||||
| CAZyme ID | MGYG000002602_01646 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 8250; End: 11672 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 228 | 422 | 1.2e-38 | 0.8663366336633663 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 1.51e-26 | 236 | 420 | 97 | 273 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 2.66e-23 | 239 | 420 | 15 | 186 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 1.62e-12 | 305 | 420 | 89 | 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 | 1.15e-07 | 1069 | 1130 | 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. |
| cd00051 | EFh | 0.004 | 1071 | 1118 | 10 | 54 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADU23076.1 | 2.08e-153 | 25 | 509 | 752 | 1242 |
| BBF42492.1 | 1.06e-146 | 1 | 654 | 1 | 667 |
| ACR71161.1 | 5.15e-143 | 33 | 620 | 44 | 655 |
| CDR31241.1 | 4.42e-126 | 30 | 635 | 329 | 907 |
| QEH68115.1 | 3.54e-75 | 33 | 505 | 39 | 478 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 1.08e-20 | 200 | 423 | 47 | 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] |
| 1VBL_A | 5.61e-11 | 240 | 421 | 132 | 331 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 5AMV_A | 3.73e-10 | 240 | 421 | 127 | 326 | 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 | 4.08e-10 | 240 | 421 | 148 | 347 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 3KRG_A | 8.70e-10 | 240 | 421 | 127 | 326 | ChainA, Pectate lyase [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q65DC2 | 4.57e-12 | 173 | 508 | 54 | 341 | 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 | 4.57e-12 | 173 | 508 | 54 | 341 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q8GCB2 | 4.57e-12 | 173 | 508 | 54 | 341 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| Q5AVN4 | 9.55e-12 | 240 | 442 | 98 | 286 | 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 |
| Q59671 | 4.63e-11 | 307 | 505 | 181 | 379 | Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000225 | 0.999140 | 0.000158 | 0.000158 | 0.000137 | 0.000130 |
