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Conserved domains on  [gi|15242373|ref|NP_196490|]
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Pectin lyase-like superfamily protein [Arabidopsis thaliana]

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;
47-242 5.88e-76

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 230.24  E-value: 5.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373     47 NMKIKLHK--PLLISSFTALDGRGASVHISGpACLIVYRATDVIIHGLKIHDCKAHPPSsvmgpdskiiqlghmDGDAIR 124
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKG-GGLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373    125 LVTAKKVWIDHNTLYDC---------EDGLLDVTLGSTDVTVSNNWFRNQDKVMLLGHDDGYVKDKDMRVTVVFNHFGpN 195
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15242373    196 CNQRMPRVRHGYAHVANNYYQGWTQYAIGGSMSPRVKSESNYFVAPK 242
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
47-242 5.88e-76

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 230.24  E-value: 5.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373     47 NMKIKLHK--PLLISSFTALDGRGASVHISGpACLIVYRATDVIIHGLKIHDCKAHPPSsvmgpdskiiqlghmDGDAIR 124
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKG-GGLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373    125 LVTAKKVWIDHNTLYDC---------EDGLLDVTLGSTDVTVSNNWFRNQDKVMLLGHDDGYVKDKDMRVTVVFNHFGpN 195
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15242373    196 CNQRMPRVRHGYAHVANNYYQGWTQYAIGGSMSPRVKSESNYFVAPK 242
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
2-238 2.04e-51

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 171.71  E-value: 2.04e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373   2 TGniGKGVTQYKVTDPSDdplnpkpgtLRYGATlVKGKKWITFkrNMKIKLHK-PLLISSFTALDGRGASVHISGpACLI 80
Cdd:COG3866  46 TG--GAGGTVVTVTTLAD---------LRAALE-ASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGATITG-GGLN 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373  81 VYRATDVIIHGLKIHDCKAHPPSsvmgpdskiiqlghmDGDAIRLVTAKKVWIDHNTLYDCEDGLLDVTLGSTDVTVSNN 160
Cdd:COG3866 111 IKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSDNVTVSWN 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373 161 WFR----NQDKVMLLGHDDGYVKDKdMRVTVVFNHFGpNCNQRMPRVRHGYAHVANNYYQGWTQ-YAIGGSMSPRVKSES 235
Cdd:COG3866 176 IFAegkgDHGKGMLIGSSDSDTTGK-LRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWGNnYGIGSGGGAQVLVEN 253

                ...
gi 15242373 236 NYF 238
Cdd:COG3866 254 NYF 256
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
65-238 8.82e-24

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: 96.12  E-value: 8.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373    65 DGRGASVHIsgpacLIVYRATDVIIHGLKIhdckAHPPSsvmgpdskiiqlGHMDGDAIRLVTAKKVWIDHNTLYD---- 140
Cdd:pfam00544  45 NGKFTNFGS-----LIIKGSSNVIVRNLYI----GTPDG------------WNKDWDAIRIDNSPNVWVDHVTISDgsft 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373   141 CE---------DGLLDVTLGSTDVTVSNNWFRNQDKVMLLGH-DDGYVKDKDMRVTVVFNHFGPNCNQRMPRVRHGYAHV 210
Cdd:pfam00544 104 DDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHsDDNNSQDTGKLRVTYHHNVYNRVTERAPLVRYGSIHA 183
                         170       180
                  ....*....|....*....|....*...
gi 15242373   211 ANNYYQGWTQYAIGGSMSPRVKSESNYF 238
Cdd:pfam00544 184 YNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
47-242 5.88e-76

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 230.24  E-value: 5.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373     47 NMKIKLHK--PLLISSFTALDGRGASVHISGpACLIVYRATDVIIHGLKIHDCKAHPPSsvmgpdskiiqlghmDGDAIR 124
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKG-GGLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373    125 LVTAKKVWIDHNTLYDC---------EDGLLDVTLGSTDVTVSNNWFRNQDKVMLLGHDDGYVKDKDMRVTVVFNHFGpN 195
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15242373    196 CNQRMPRVRHGYAHVANNYYQGWTQYAIGGSMSPRVKSESNYFVAPK 242
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
2-238 2.04e-51

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 171.71  E-value: 2.04e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373   2 TGniGKGVTQYKVTDPSDdplnpkpgtLRYGATlVKGKKWITFkrNMKIKLHK-PLLISSFTALDGRGASVHISGpACLI 80
Cdd:COG3866  46 TG--GAGGTVVTVTTLAD---------LRAALE-ASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGATITG-GGLN 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373  81 VYRATDVIIHGLKIHDCKAHPPSsvmgpdskiiqlghmDGDAIRLVTAKKVWIDHNTLYDCEDGLLDVTLGSTDVTVSNN 160
Cdd:COG3866 111 IKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSDNVTVSWN 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373 161 WFR----NQDKVMLLGHDDGYVKDKdMRVTVVFNHFGpNCNQRMPRVRHGYAHVANNYYQGWTQ-YAIGGSMSPRVKSES 235
Cdd:COG3866 176 IFAegkgDHGKGMLIGSSDSDTTGK-LRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWGNnYGIGSGGGAQVLVEN 253

                ...
gi 15242373 236 NYF 238
Cdd:COG3866 254 NYF 256
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
65-238 8.82e-24

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: 96.12  E-value: 8.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373    65 DGRGASVHIsgpacLIVYRATDVIIHGLKIhdckAHPPSsvmgpdskiiqlGHMDGDAIRLVTAKKVWIDHNTLYD---- 140
Cdd:pfam00544  45 NGKFTNFGS-----LIIKGSSNVIVRNLYI----GTPDG------------WNKDWDAIRIDNSPNVWVDHVTISDgsft 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242373   141 CE---------DGLLDVTLGSTDVTVSNNWFRNQDKVMLLGH-DDGYVKDKDMRVTVVFNHFGPNCNQRMPRVRHGYAHV 210
Cdd:pfam00544 104 DDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHsDDNNSQDTGKLRVTYHHNVYNRVTERAPLVRYGSIHA 183
                         170       180
                  ....*....|....*....|....*...
gi 15242373   211 ANNYYQGWTQYAIGGSMSPRVKSESNYF 238
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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