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Conserved domains on  [gi|28374119|pdb|1O8L|A]
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Chain A, PECTATE LYASE C

Protein Classification

polysaccharide lyase( domain architecture ID 10455512)

polysaccharide lyase family protein similar to pectate lyase, which catalyzes the eliminative cleavage of pectate to yield oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at the non-reducing ends in the soft rotting and maceration of plant tissue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 51-257 2.32e-101

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: 297.58  E-value: 2.32e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A         51 PLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGItiIGANGSSANFGIWI-KKSSDVVVQNMRIGYLPGGAKD 129
Cdd:pfam00544   1 PKVITYTGNEDISGGAAYANFCDQKARSQIGVPSNTTIIGI--IGTNGKFTNFGSLIiKGSSNVIVRNLYIGTPDGWNKD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A        130 GDMIRVDDSPNVWVDHNELFAANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSS----SSDTG-RN 204
Cdd:pfam00544  79 WDAIRIDNSPNVWVDHVTISDGSFTDDGYTTKYVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSddnnSQDTGkLR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
1O8L_A        205 ITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWF 257
Cdd:pfam00544 159 VTYHHNVYNRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 51-257 2.32e-101

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: 297.58  E-value: 2.32e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A         51 PLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGItiIGANGSSANFGIWI-KKSSDVVVQNMRIGYLPGGAKD 129
Cdd:pfam00544   1 PKVITYTGNEDISGGAAYANFCDQKARSQIGVPSNTTIIGI--IGTNGKFTNFGSLIiKGSSNVIVRNLYIGTPDGWNKD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A        130 GDMIRVDDSPNVWVDHNELFAANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSS----SSDTG-RN 204
Cdd:pfam00544  79 WDAIRIDNSPNVWVDHVTISDGSFTDDGYTTKYVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSddnnSQDTGkLR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
1O8L_A        205 ITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWF 257
Cdd:pfam00544 159 VTYHHNVYNRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
Amb_all smart00656
Amb_all domain;
53-261 7.38e-59

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 188.26  E-value: 7.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A          53 VITYTGNEDSLINAAAANICGQWSKdprgVEIKeftkgitiigangssaNFGIWIKKSSDVVVQNMRIGYLPGGAK-DGD 131
Cdd:smart00656   2 VTITLDNAGTIIINSNKTIDGRGSK----VEIK----------------GGGLTIKSVSNVIIRNLTIHDPKPVYGsDGD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A         132 MIRVDDSPNVWVDHNELFAanheCDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSSSSDT---GRNITYH 208
Cdd:smart00656  62 AISIDGSSNVWIDHVSLSG----CTVTGFGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTddgKMRVTIA 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
1O8L_A         209 HNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWFEKAI 261
Cdd:smart00656 138 HNYFGNLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
91-342 4.43e-53

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 177.87  E-value: 4.43e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A       91 ITIIGANGSS--ANFGIWIKKSSDVVVQNMRI-GYLPGGAKDGDMIRVDDSPNVWVDHNELFAANhecDGtpdndttfes 167
Cdd:COG3866  93 KTIAGQGDGAtiTGGGLNIKGASNVIIRNLRFrNGDDGGGSGGDAIGIEGAHNVWIDHCTFSWGY---DG---------- 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A      168 AVDIKGASNTVTVSYNYIHGVK----KVGLDGSSSSDT--GRNITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITG-S 240
Cdd:COG3866 160 LLDIKRGSDNVTVSWNIFAEGKgdhgKGMLIGSSDSDTtgKLRVTFHHNLFANNDSRNPRVRFGQVHVYNNYFYNWGNnY 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A      241 GLNVRQNGQALIENNWFEKAINPVTSRYDGKNF--GTWVLKGNNITkpadfstySITWTADtkpyvnadswTSTGTFPTV 318
Cdd:COG3866 240 GIGSGGGAQVLVENNYFENVKGPLATSDGSSLLdpGYLYARGNVFD--------NSTGTAP----------AGSGTVFTP 301

                       250       260
                ....*....|....*....|....
1O8L_A      319 AYNYSPVSAQCVKDKLPGYAGVGK 342
Cdd:COG3866 302 PYSYTLDPASDVKTLVLAGAGAGK 325
 
Name Accession Description Interval E-value
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 51-257 2.32e-101

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: 297.58  E-value: 2.32e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A         51 PLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGItiIGANGSSANFGIWI-KKSSDVVVQNMRIGYLPGGAKD 129
Cdd:pfam00544   1 PKVITYTGNEDISGGAAYANFCDQKARSQIGVPSNTTIIGI--IGTNGKFTNFGSLIiKGSSNVIVRNLYIGTPDGWNKD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A        130 GDMIRVDDSPNVWVDHNELFAANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSS----SSDTG-RN 204
Cdd:pfam00544  79 WDAIRIDNSPNVWVDHVTISDGSFTDDGYTTKYVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSddnnSQDTGkLR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
1O8L_A        205 ITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWF 257
Cdd:pfam00544 159 VTYHHNVYNRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
Amb_all smart00656
Amb_all domain;
53-261 7.38e-59

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 188.26  E-value: 7.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A          53 VITYTGNEDSLINAAAANICGQWSKdprgVEIKeftkgitiigangssaNFGIWIKKSSDVVVQNMRIGYLPGGAK-DGD 131
Cdd:smart00656   2 VTITLDNAGTIIINSNKTIDGRGSK----VEIK----------------GGGLTIKSVSNVIIRNLTIHDPKPVYGsDGD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A         132 MIRVDDSPNVWVDHNELFAanheCDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSSSSDT---GRNITYH 208
Cdd:smart00656  62 AISIDGSSNVWIDHVSLSG----CTVTGFGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTddgKMRVTIA 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
1O8L_A         209 HNYYNDVNARLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQALIENNWFEKAI 261
Cdd:smart00656 138 HNYFGNLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
91-342 4.43e-53

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 177.87  E-value: 4.43e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A       91 ITIIGANGSS--ANFGIWIKKSSDVVVQNMRI-GYLPGGAKDGDMIRVDDSPNVWVDHNELFAANhecDGtpdndttfes 167
Cdd:COG3866  93 KTIAGQGDGAtiTGGGLNIKGASNVIIRNLRFrNGDDGGGSGGDAIGIEGAHNVWIDHCTFSWGY---DG---------- 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A      168 AVDIKGASNTVTVSYNYIHGVK----KVGLDGSSSSDT--GRNITYHHNYYNDVNARLPLQRGGLVHAYNNLYTNITG-S 240
Cdd:COG3866 160 LLDIKRGSDNVTVSWNIFAEGKgdhgKGMLIGSSDSDTtgKLRVTFHHNLFANNDSRNPRVRFGQVHVYNNYFYNWGNnY 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O8L_A      241 GLNVRQNGQALIENNWFEKAINPVTSRYDGKNF--GTWVLKGNNITkpadfstySITWTADtkpyvnadswTSTGTFPTV 318
Cdd:COG3866 240 GIGSGGGAQVLVENNYFENVKGPLATSDGSSLLdpGYLYARGNVFD--------NSTGTAP----------AGSGTVFTP 301

                       250       260
                ....*....|....*....|....
1O8L_A      319 AYNYSPVSAQCVKDKLPGYAGVGK 342
Cdd:COG3866 302 PYSYTLDPASDVKTLVLAGAGAGK 325
 
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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