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Conserved domains on  [gi|1063709964|ref|NP_001327532|]
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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;
109-303 4.84e-83

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 4.84e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  109 DMVITLKQ--ELIMNSFKTIDGRGVNVHIANGaCLTIQYVTNIIVHGIHVHDCKPTGNAmvrsspshygfrsmaDGDAIS 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  187 IFGSSHIWIDHNSLSNCA---------DGLVDAVMSSTAITVSNNFFTHHNEVMLLGHSDSYTRDKVMQVTIAYNHFGeG 257
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1063709964  258 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRFLAP 303
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
109-303 4.84e-83

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 4.84e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  109 DMVITLKQ--ELIMNSFKTIDGRGVNVHIANGaCLTIQYVTNIIVHGIHVHDCKPTGNAmvrsspshygfrsmaDGDAIS 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  187 IFGSSHIWIDHNSLSNCA---------DGLVDAVMSSTAITVSNNFFTHHNEVMLLGHSDSYTRDKVMQVTIAYNHFGeG 257
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1063709964  258 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRFLAP 303
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
59-336 2.23e-51

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 174.41  E-value: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  59 IGFGR---NAIGGRDGRFYVVTDPGDddpvnpipgtLRHAVIQDEPLWIIFkrDMVITL-KQELIMNSFKTIDGRGVNVH 134
Cdd:COG3866    36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 135 IANGAcLTIQYVTNIIVHGIHVHDCKPTGNAmvrsspshygfrsmaDGDAISIFGSSHIWIDHNSLSNCADGLVDAVMSS 214
Cdd:COG3866   104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 215 TAITVSNNFF----THHNEVMLLGHSDSYTRDKvMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 289
Cdd:COG3866   168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1063709964 290 GPTINSQGNRFLAPVNPFAKevtkreYTGESKWKHWNWRSEGDLFLN 336
Cdd:COG3866   246 GAQVLVENNYFENVKGPLAT------SDGSSLLDPGYLYARGNVFDN 286
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 154-300 2.85e-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: 85.34  E-value: 2.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 154 IHVHDCKPTGNAMVRSSPSHYGFRSMADGDAISIFGSSHIWIDHNSLS----NCA---------DGLVDAVMSSTAITVS 220
Cdd:pfam00544  51 FGSLIIKGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTIS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 221 NNFFTHHNEVMLLGHSDSY--TRDKVMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGN 298
Cdd:pfam00544 131 YSLFHGHKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209


                  ..
gi 1063709964 299 RF 300
Cdd:pfam00544 210 SF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
109-303 4.84e-83

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 4.84e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  109 DMVITLKQ--ELIMNSFKTIDGRGVNVHIANGaCLTIQYVTNIIVHGIHVHDCKPTGNAmvrsspshygfrsmaDGDAIS 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKPVYGS---------------DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  187 IFGSSHIWIDHNSLSNCA---------DGLVDAVMSSTAITVSNNFFTHHNEVMLLGHSDSYTRDKVMQVTIAYNHFGeG 257
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1063709964  258 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRFLAP 303
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
59-336 2.23e-51

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 174.41  E-value: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964  59 IGFGR---NAIGGRDGRFYVVTDPGDddpvnpipgtLRHAVIQDEPLWIIFkrDMVITL-KQELIMNSFKTIDGRGVNVH 134
Cdd:COG3866    36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 135 IANGAcLTIQYVTNIIVHGIHVHDCKPTGNAmvrsspshygfrsmaDGDAISIFGSSHIWIDHNSLSNCADGLVDAVMSS 214
Cdd:COG3866   104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 215 TAITVSNNFF----THHNEVMLLGHSDSYTRDKvMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 289
Cdd:COG3866   168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1063709964 290 GPTINSQGNRFLAPVNPFAKevtkreYTGESKWKHWNWRSEGDLFLN 336
Cdd:COG3866   246 GAQVLVENNYFENVKGPLAT------SDGSSLLDPGYLYARGNVFDN 286
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 154-300 2.85e-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: 85.34  E-value: 2.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 154 IHVHDCKPTGNAMVRSSPSHYGFRSMADGDAISIFGSSHIWIDHNSLS----NCA---------DGLVDAVMSSTAITVS 220
Cdd:pfam00544  51 FGSLIIKGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTIS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709964 221 NNFFTHHNEVMLLGHSDSY--TRDKVMQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGN 298
Cdd:pfam00544 131 YSLFHGHKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209


                  ..
gi 1063709964 299 RF 300
Cdd:pfam00544 210 SF 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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