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Conserved domains on  [gi|5107654]
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Chain A, PECTIN LYASE B

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;
91-280 1.63e-59

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 190.18  E-value: 1.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654      91 KVSVTYDKAGilPITVNSNKSIVGQGTKGVIKGKGLRVVSgAKNVIIQNIAVTDINPKYVWGGDAITVDDSDLVWIDHVT 170
Cdd:smart00656   1 DVTITLDNAG--TIIINSNKTIDGRGSKVEIKGGGLTIKS-VSNVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654     171 TARigRQHIVLGTSADNRVTISYSLIDGRSDYSATCNGHHYWGVYLDGSNDM------VTLKGNYFYNLSGRMPKVQGNT 244
Cdd:smart00656  78 LSG--CTVTGFGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTddgkmrVTIAHNYFGNLRQRAPRVRFGY 155

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 5107654     245 lLHAVNNLFHNFDGHAFEIGTGGYVLAEGNVFQDVN 280
Cdd:smart00656 156 -VHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
91-280 1.63e-59

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 190.18  E-value: 1.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654      91 KVSVTYDKAGilPITVNSNKSIVGQGTKGVIKGKGLRVVSgAKNVIIQNIAVTDINPKYVWGGDAITVDDSDLVWIDHVT 170
Cdd:smart00656   1 DVTITLDNAG--TIIINSNKTIDGRGSKVEIKGGGLTIKS-VSNVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654     171 TARigRQHIVLGTSADNRVTISYSLIDGRSDYSATCNGHHYWGVYLDGSNDM------VTLKGNYFYNLSGRMPKVQGNT 244
Cdd:smart00656  78 LSG--CTVTGFGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTddgkmrVTIAHNYFGNLRQRAPRVRFGY 155

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 5107654     245 lLHAVNNLFHNFDGHAFEIGTGGYVLAEGNVFQDVN 280
Cdd:smart00656 156 -VHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
1-294 1.05e-40

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 145.52  E-value: 1.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    1 AGVVGAAEGFA---HGVTGGGSASPVYPTTTDELVSYLGDNEPRVIILDQTFDFTGTegtetttgcapwgtasqcqvain 77
Cdd:COG3866  29 AAAAPAPEGFAsvnGGTTGGAGGTVVTVTTLADLRAALEASGPRIIVVSGTIDLSKS----------------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654   78 lhswcdnyqasapkvsvtydkagilPITVNSNKSIVGQGTKGVIKGKGLRVvSGAKNVIIQNIAVTDINPKYVWGGDAIT 157
Cdd:COG3866  86 -------------------------PLKVNSNKTIAGQGDGATITGGGLNI-KGASNVIIRNLRFRNGDDGGGSGGDAIG 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654  158 VDDSDLVWIDHVTTARIGRQHIVLGTSADNrVTISYSLIdgrsdySATCNGHHYWGvyLDGSNDM-------VTLKGNYF 230
Cdd:COG3866 140 IEGAHNVWIDHCTFSWGYDGLLDIKRGSDN-VTVSWNIF------AEGKGDHGKGM--LIGSSDSdttgklrVTFHHNLF 210

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5107654  231 YNLSGRMPKVQGNTlLHAVNNLFHNF-DGHAFEIGTGGYVLAEGNVFQDVNVVVETPISGQLFSS 294
Cdd:COG3866 211 ANNDSRNPRVRFGQ-VHVYNNYFYNWgNNYGIGSGGGAQVLVENNYFENVKGPLATSDGSSLLDP 274
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 103-276 4.62e-20

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: 87.26  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    103 PITVNSNKSIVGQ-GTKGVIKGKGLRVVSGAKNVIIQNIaVTDINPKYVWGGDAITVDDSDLVWIDHVT----------T 171
Cdd:pfam00544  29 QIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNL-YIGTPDGWNKDWDAIRIDNSPNVWVDHVTisdgsftddgY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    172 ARIGRQH---IVLGTSADNrVTISYSLIDGrsdYSATC-NGHHYWGVYLDGSNDMVTLKGNYFYNLSGRMPKVQGNtLLH 247
Cdd:pfam00544 108 TTKYVQHdgaLDIKKGSDY-VTISYSLFHG---HKKTGlIGHSDDNNSQDTGKLRVTYHHNVYNRVTERAPLVRYG-SIH 182

                         170       180
                  ....*....|....*....|....*....
gi 5107654    248 AVNNLFHNFDGHAFEIGTGGYVLAEGNVF 276
Cdd:pfam00544 183 AYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
91-280 1.63e-59

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 190.18  E-value: 1.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654      91 KVSVTYDKAGilPITVNSNKSIVGQGTKGVIKGKGLRVVSgAKNVIIQNIAVTDINPKYVWGGDAITVDDSDLVWIDHVT 170
Cdd:smart00656   1 DVTITLDNAG--TIIINSNKTIDGRGSKVEIKGGGLTIKS-VSNVIIRNLTIHDPKPVYGSDGDAISIDGSSNVWIDHVS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654     171 TARigRQHIVLGTSADNRVTISYSLIDGRSDYSATCNGHHYWGVYLDGSNDM------VTLKGNYFYNLSGRMPKVQGNT 244
Cdd:smart00656  78 LSG--CTVTGFGDDTYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTddgkmrVTIAHNYFGNLRQRAPRVRFGY 155

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 5107654     245 lLHAVNNLFHNFDGHAFEIGTGGYVLAEGNVFQDVN 280
Cdd:smart00656 156 -VHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
1-294 1.05e-40

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 145.52  E-value: 1.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    1 AGVVGAAEGFA---HGVTGGGSASPVYPTTTDELVSYLGDNEPRVIILDQTFDFTGTegtetttgcapwgtasqcqvain 77
Cdd:COG3866  29 AAAAPAPEGFAsvnGGTTGGAGGTVVTVTTLADLRAALEASGPRIIVVSGTIDLSKS----------------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654   78 lhswcdnyqasapkvsvtydkagilPITVNSNKSIVGQGTKGVIKGKGLRVvSGAKNVIIQNIAVTDINPKYVWGGDAIT 157
Cdd:COG3866  86 -------------------------PLKVNSNKTIAGQGDGATITGGGLNI-KGASNVIIRNLRFRNGDDGGGSGGDAIG 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654  158 VDDSDLVWIDHVTTARIGRQHIVLGTSADNrVTISYSLIdgrsdySATCNGHHYWGvyLDGSNDM-------VTLKGNYF 230
Cdd:COG3866 140 IEGAHNVWIDHCTFSWGYDGLLDIKRGSDN-VTVSWNIF------AEGKGDHGKGM--LIGSSDSdttgklrVTFHHNLF 210

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5107654  231 YNLSGRMPKVQGNTlLHAVNNLFHNF-DGHAFEIGTGGYVLAEGNVFQDVNVVVETPISGQLFSS 294
Cdd:COG3866 211 ANNDSRNPRVRFGQ-VHVYNNYFYNWgNNYGIGSGGGAQVLVENNYFENVKGPLATSDGSSLLDP 274
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 103-276 4.62e-20

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: 87.26  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    103 PITVNSNKSIVGQ-GTKGVIKGKGLRVVSGAKNVIIQNIaVTDINPKYVWGGDAITVDDSDLVWIDHVT----------T 171
Cdd:pfam00544  29 QIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNL-YIGTPDGWNKDWDAIRIDNSPNVWVDHVTisdgsftddgY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107654    172 ARIGRQH---IVLGTSADNrVTISYSLIDGrsdYSATC-NGHHYWGVYLDGSNDMVTLKGNYFYNLSGRMPKVQGNtLLH 247
Cdd:pfam00544 108 TTKYVQHdgaLDIKKGSDY-VTISYSLFHG---HKKTGlIGHSDDNNSQDTGKLRVTYHHNVYNRVTERAPLVRYG-SIH 182

                         170       180
                  ....*....|....*....|....*....
gi 5107654    248 AVNNLFHNFDGHAFEIGTGGYVLAEGNVF 276
Cdd:pfam00544 183 AYNNVYVNIYLYSFGVGQNGSVLSESNSF 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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