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CAZyme Information: MGYG000001998_01692
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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 | Lachnospira sp900552795 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp900552795 | |||||||||||
| CAZyme ID | MGYG000001998_01692 | |||||||||||
| CAZy Family | CE12 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 26410; End: 30015 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE12 | 45 | 261 | 1.5e-53 | 0.9761904761904762 |
| PL1 | 744 | 911 | 1.1e-42 | 0.8168316831683168 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 3.99e-54 | 616 | 915 | 18 | 279 | Pectate lyase [Carbohydrate transport and metabolism]. |
| cd01821 | Rhamnogalacturan_acetylesterase_like | 1.66e-47 | 43 | 261 | 2 | 196 | Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria. |
| smart00656 | Amb_all | 3.01e-34 | 747 | 913 | 17 | 190 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 9.98e-20 | 745 | 909 | 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. |
| PTZ00449 | PTZ00449 | 5.80e-15 | 1076 | 1164 | 577 | 666 | 104 kDa microneme/rhoptry antigen; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADL50681.1 | 7.92e-228 | 37 | 526 | 40 | 529 |
| QAV09174.1 | 1.61e-197 | 42 | 516 | 1412 | 1888 |
| ACR72246.1 | 1.87e-191 | 545 | 1082 | 32 | 586 |
| ACX62589.1 | 5.49e-191 | 549 | 1082 | 37 | 573 |
| BCJ94010.1 | 7.88e-191 | 549 | 1070 | 43 | 567 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 1.30e-25 | 702 | 911 | 38 | 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 | 2.20e-18 | 743 | 910 | 129 | 331 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1AIR_A | 9.58e-15 | 688 | 924 | 17 | 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] |
| 3ZSC_A | 2.00e-14 | 749 | 894 | 71 | 221 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
| 2EWE_A | 2.29e-14 | 688 | 924 | 17 | 272 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8GCB2 | 9.42e-25 | 688 | 918 | 59 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| B1B6T1 | 9.42e-25 | 688 | 918 | 59 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q65DC2 | 9.42e-25 | 688 | 918 | 59 | 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 |
| O31523 | 4.52e-18 | 45 | 279 | 9 | 227 | Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1 |
| Q0CBV0 | 5.42e-18 | 691 | 912 | 54 | 260 | Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999886 | 0.000121 | 0.000003 | 0.000000 | 0.000000 | 0.000015 |
