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Conserved domains on  [gi|240255809|ref|NP_193057|]
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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;
127-322 9.88e-71

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 220.23  E-value: 9.88e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   127 DMVITLSQ--ELIMNSFKTIDGRGVNVHIAGGaCLTVQYVTniiihginihdckrtgNAMVRSSESHYGWRT-MADGDGI 203
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVS----------------NVIIRNLTIHDPKPVyGSDGDAI 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   204 SIFGSSHIWIDHNSLSSCA---------DGLIDAIMGSTAITISNNYLTHHNEAILLGHTDSYTRDKMMQVTIAYNHFGe 274
Cdd:smart00656  64 SIDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG- 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 240255809   275 GLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLAPG 322
Cdd:smart00656 143 NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
127-322 9.88e-71

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 220.23  E-value: 9.88e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   127 DMVITLSQ--ELIMNSFKTIDGRGVNVHIAGGaCLTVQYVTniiihginihdckrtgNAMVRSSESHYGWRT-MADGDGI 203
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVS----------------NVIIRNLTIHDPKPVyGSDGDAI 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   204 SIFGSSHIWIDHNSLSSCA---------DGLIDAIMGSTAITISNNYLTHHNEAILLGHTDSYTRDKMMQVTIAYNHFGe 274
Cdd:smart00656  64 SIDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG- 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 240255809   275 GLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLAPG 322
Cdd:smart00656 143 NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
76-318 4.83e-42

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 150.52  E-value: 4.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809  76 AIGFGR---NAVGGRDGRYYIVTDPSDhdpvtpkpgtLRYAVIQDEPLWIVFkrDMVITLSQ-ELIMNSFKTIDGRGVNV 151
Cdd:COG3866   35 PEGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809 152 HIAGGacltvqyvtniiihginIHDCKRTGNAMVRSSESHYGWRTMADG-DGISIFGSSHIWIDHNSLSSCADGLIDAIM 230
Cdd:COG3866  103 TITGG-----------------GLNIKGASNVIIRNLRFRNGDDGGGSGgDAIGIEGAHNVWIDHCTFSWGYDGLLDIKR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809 231 GSTAITISNNYL----THHNEAILLGHTDSYTRDKmMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGG 305
Cdd:COG3866  166 GSDNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGS 243

                        250
                 ....*....|...
gi 240255809 306 SANPTINSQGNRF 318
Cdd:COG3866  244 GGGAQVLVENNYF 256
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 178-318 4.91e-19

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: 84.95  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809  178 KRTGNAMVRSSESHYGWRTMADGDGISIFGSSHIWIDHNSLS----SCA---------DGLIDAIMGSTAITISNNYLTH 244
Cdd:pfam00544  57 KGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHG 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255809  245 HNEAILLGHTDSY--TRDKMMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRF 318
Cdd:pfam00544 137 HKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
127-322 9.88e-71

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 220.23  E-value: 9.88e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   127 DMVITLSQ--ELIMNSFKTIDGRGVNVHIAGGaCLTVQYVTniiihginihdckrtgNAMVRSSESHYGWRT-MADGDGI 203
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVS----------------NVIIRNLTIHDPKPVyGSDGDAI 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809   204 SIFGSSHIWIDHNSLSSCA---------DGLIDAIMGSTAITISNNYLTHHNEAILLGHTDSYTRDKMMQVTIAYNHFGe 274
Cdd:smart00656  64 SIDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG- 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 240255809   275 GLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLAPG 322
Cdd:smart00656 143 NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
76-318 4.83e-42

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 150.52  E-value: 4.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809  76 AIGFGR---NAVGGRDGRYYIVTDPSDhdpvtpkpgtLRYAVIQDEPLWIVFkrDMVITLSQ-ELIMNSFKTIDGRGVNV 151
Cdd:COG3866   35 PEGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809 152 HIAGGacltvqyvtniiihginIHDCKRTGNAMVRSSESHYGWRTMADG-DGISIFGSSHIWIDHNSLSSCADGLIDAIM 230
Cdd:COG3866  103 TITGG-----------------GLNIKGASNVIIRNLRFRNGDDGGGSGgDAIGIEGAHNVWIDHCTFSWGYDGLLDIKR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809 231 GSTAITISNNYL----THHNEAILLGHTDSYTRDKmMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGG 305
Cdd:COG3866  166 GSDNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGS 243

                        250
                 ....*....|...
gi 240255809 306 SANPTINSQGNRF 318
Cdd:COG3866  244 GGGAQVLVENNYF 256
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 178-318 4.91e-19

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: 84.95  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255809  178 KRTGNAMVRSSESHYGWRTMADGDGISIFGSSHIWIDHNSLS----SCA---------DGLIDAIMGSTAITISNNYLTH 244
Cdd:pfam00544  57 KGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHG 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255809  245 HNEAILLGHTDSY--TRDKMMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRF 318
Cdd:pfam00544 137 HKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 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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