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Conserved domains on  [gi|497653205|ref|WP_009967389|]
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MULTISPECIES: polysaccharide lyase family 1 protein [Bacillus]

Protein Classification

polysaccharide lyase family 1 protein( domain architecture ID 10652760)

polysaccharide lyase family 1 protein such as pectate lyase that catalyzes the eliminative cleavage of pectate to yield oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at the non-reducing ends, and pectin lyase that catalyzes the eliminative cleavage of the methyl ester pectin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
92-277 4.20e-57

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 183.63  E-value: 4.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205    92 SAKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSAFgNVIFQNLTFEHSPQINGNNDIQLYLDSGMNYWIDHVTFSG-HSYN 170
Cdd:smart00656   7 DNAGTIIINSNKTIDGRGSKVEIKGGGLTIKSVS-NVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVSLSGcTVTG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   171 ASGSDLDKLVYIGKSADYITISNSKFANHKYGLILGYPDDsqHQYDGYPHMTIANNYFENLYVRGPGLmRYGYFHVKNNY 250
Cdd:smart00656  86 FGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDS--DTDDGKMRVTIAHNYFGNLRQRAPRV-RFGYVHVYNNY 162

                          170       180
                   ....*....|....*....|....*...
gi 497653205   251 SNNFNQ-AITIATKAKIYSEYNYFGKGS 277
Cdd:smart00656 163 YTGWTSyAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
92-277 4.20e-57

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 183.63  E-value: 4.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205    92 SAKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSAFgNVIFQNLTFEHSPQINGNNDIQLYLDSGMNYWIDHVTFSG-HSYN 170
Cdd:smart00656   7 DNAGTIIINSNKTIDGRGSKVEIKGGGLTIKSVS-NVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVSLSGcTVTG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   171 ASGSDLDKLVYIGKSADYITISNSKFANHKYGLILGYPDDsqHQYDGYPHMTIANNYFENLYVRGPGLmRYGYFHVKNNY 250
Cdd:smart00656  86 FGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDS--DTDDGKMRVTIAHNYFGNLRQRAPRV-RFGYVHVYNNY 162

                          170       180
                   ....*....|....*....|....*...
gi 497653205   251 SNNFNQ-AITIATKAKIYSEYNYFGKGS 277
Cdd:smart00656 163 YTGWTSyAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
3-335 6.93e-45

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 156.30  E-value: 6.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   3 RLCLWFTVFSLFLVLLPGKALGAVDFPNTSTNGLLGFAGnaknekgiSKTGTTGGKNGQIVYIQSVNDLKTHLGGSTPKI 82
Cdd:COG3866    2 KLLLVLLLALAASAATAGAATAVPDAAAAAAPAPEGFAS--------VNGGTTGGAGGTVVTVTTLADLRAALEASGPRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205  83 LVLQNDLSASaKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSAfGNVIFQNLTFEH--SPQINGNNDIQLylDSGMNYWID 160
Cdd:COG3866   74 IVVSGTIDLS-KSPLKVNSNKTIAGQGDGATITGGGLNIKGA-SNVIIRNLRFRNgdDGGGSGGDAIGI--EGAHNVWID 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205 161 HVTFSGHSynasgsdlDKLVYIGKSADYITISNSKFA----NHKYGLILGYPDDsqhQYDGYPHMTIANNYFENLYVRGP 236
Cdd:COG3866  150 HCTFSWGY--------DGLLDIKRGSDNVTVSWNIFAegkgDHGKGMLIGSSDS---DTTGKLRVTFHHNLFANNDSRNP 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205 237 gLMRYGYFHVKNNYSNNFNQ--AITIATKAKIYSEYNYF--GKG---SEKGGILDDKGTGYFKD-IGSYPSLNKQTSPLT 308
Cdd:COG3866  219 -RVRFGQVHVYNNYFYNWGNnyGIGSGGGAQVLVENNYFenVKGplaTSDGSSLLDPGYLYARGnVFDNSTGTAPAGSGT 297

                        330       340
                 ....*....|....*....|....*..
gi 497653205 309 SWNPGsnYSYRVQTPEYTKEFVTKYAG 335
Cdd:COG3866  298 VFTPP--YSYTLDPASDVKTLVLAGAG 322
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 93-273 1.67e-42

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.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 146.58  E-value: 1.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   93 AKTTVTIGSNKTLVGSY-AKKTLKNIYLTTSSAFGNVIFQNLTFEHSPQINGNNDiQLYLDSGMNYWIDHVTFSGHSYNA 171
Cdd:pfam00544  26 ARSQIGVPSNTTIIGIIgTNGKFTNFGSLIIKGSSNVIVRNLYIGTPDGWNKDWD-AIRIDNSPNVWVDHVTISDGSFTD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205  172 SG-----SDLDKLVYIGKSADYITISNSKFANHKYGLILGYPDDSQHQYDGYPHMTIANNYFENLYVRGPgLMRYGYFHV 246
Cdd:pfam00544 105 DGyttkyVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNSQDTGKLRVTYHHNVYNRVTERAP-LVRYGSIHA 183

                         170       180
                  ....*....|....*....|....*...
gi 497653205  247 KNN-YSNNFNQAITIATKAKIYSEYNYF 273
Cdd:pfam00544 184 YNNvYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
92-277 4.20e-57

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 183.63  E-value: 4.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205    92 SAKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSAFgNVIFQNLTFEHSPQINGNNDIQLYLDSGMNYWIDHVTFSG-HSYN 170
Cdd:smart00656   7 DNAGTIIINSNKTIDGRGSKVEIKGGGLTIKSVS-NVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVSLSGcTVTG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   171 ASGSDLDKLVYIGKSADYITISNSKFANHKYGLILGYPDDsqHQYDGYPHMTIANNYFENLYVRGPGLmRYGYFHVKNNY 250
Cdd:smart00656  86 FGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDS--DTDDGKMRVTIAHNYFGNLRQRAPRV-RFGYVHVYNNY 162

                          170       180
                   ....*....|....*....|....*...
gi 497653205   251 SNNFNQ-AITIATKAKIYSEYNYFGKGS 277
Cdd:smart00656 163 YTGWTSyAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
3-335 6.93e-45

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 156.30  E-value: 6.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   3 RLCLWFTVFSLFLVLLPGKALGAVDFPNTSTNGLLGFAGnaknekgiSKTGTTGGKNGQIVYIQSVNDLKTHLGGSTPKI 82
Cdd:COG3866    2 KLLLVLLLALAASAATAGAATAVPDAAAAAAPAPEGFAS--------VNGGTTGGAGGTVVTVTTLADLRAALEASGPRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205  83 LVLQNDLSASaKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSAfGNVIFQNLTFEH--SPQINGNNDIQLylDSGMNYWID 160
Cdd:COG3866   74 IVVSGTIDLS-KSPLKVNSNKTIAGQGDGATITGGGLNIKGA-SNVIIRNLRFRNgdDGGGSGGDAIGI--EGAHNVWID 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205 161 HVTFSGHSynasgsdlDKLVYIGKSADYITISNSKFA----NHKYGLILGYPDDsqhQYDGYPHMTIANNYFENLYVRGP 236
Cdd:COG3866  150 HCTFSWGY--------DGLLDIKRGSDNVTVSWNIFAegkgDHGKGMLIGSSDS---DTTGKLRVTFHHNLFANNDSRNP 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205 237 gLMRYGYFHVKNNYSNNFNQ--AITIATKAKIYSEYNYF--GKG---SEKGGILDDKGTGYFKD-IGSYPSLNKQTSPLT 308
Cdd:COG3866  219 -RVRFGQVHVYNNYFYNWGNnyGIGSGGGAQVLVENNYFenVKGplaTSDGSSLLDPGYLYARGnVFDNSTGTAPAGSGT 297

                        330       340
                 ....*....|....*....|....*..
gi 497653205 309 SWNPGsnYSYRVQTPEYTKEFVTKYAG 335
Cdd:COG3866  298 VFTPP--YSYTLDPASDVKTLVLAGAG 322
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 93-273 1.67e-42

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.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 146.58  E-value: 1.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205   93 AKTTVTIGSNKTLVGSY-AKKTLKNIYLTTSSAFGNVIFQNLTFEHSPQINGNNDiQLYLDSGMNYWIDHVTFSGHSYNA 171
Cdd:pfam00544  26 ARSQIGVPSNTTIIGIIgTNGKFTNFGSLIIKGSSNVIVRNLYIGTPDGWNKDWD-AIRIDNSPNVWVDHVTISDGSFTD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653205  172 SG-----SDLDKLVYIGKSADYITISNSKFANHKYGLILGYPDDSQHQYDGYPHMTIANNYFENLYVRGPgLMRYGYFHV 246
Cdd:pfam00544 105 DGyttkyVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNSQDTGKLRVTYHHNVYNRVTERAP-LVRYGSIHA 183

                         170       180
                  ....*....|....*....|....*...
gi 497653205  247 KNN-YSNNFNQAITIATKAKIYSEYNYF 273
Cdd:pfam00544 184 YNNvYVNIYLYSFGVGQNGSVLSESNSF 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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