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Conserved domains on  [gi|2028332791|dbj|BCS43761|]
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alginate lyase [Pseudomonas amygdali pv. tabaci]

Protein Classification

polysaccharide lyase family 7 protein( domain architecture ID 10555824)

polysaccharide lyase family 7 protein similar to alginate lyase, which degrades alginates that contain guluronic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alginate_lyase2 pfam08787
Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. ...
2-218 1.06e-77

Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. They cleave the glycosidic linkage of alignate through a beta-elimination reaction. This family forms an all beta fold and is different to all alpha fold of pfam05426.


:

Pssm-ID: 400923  Cd Length: 222  Bit Score: 232.66  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791   2 IDLATWNLSVPVGSPATIIETPKLVKGYRDGYF---QSGDTLFFWAPVTGSTTENAKYPRSELRETTSDGRVFNWAYSSA 78
Cdd:pfam08787   1 FDLSNWKLTLPVYGSATEIEPSELNGGYASDYFyydSDDGALVFWAPNSGATTANSTYPRSELREMLPDGSSNNWSLSSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791  79 DNFLRATLEVDQVPSTGKIVIGQIHCYQS---TEPLLKVEYqykeKLQTGNIVAKFRR-TPDSEIEVITIAQGVPLNKQF 154
Cdd:pfam08787  81 DNQLEATLKVDHVPSGGKVVVGQIHGKDSsdnTEPLLKLYY----RHYKGSLYAYLRDnFDDGGDVNYTIYGGIDLGEWF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028332791 155 NYTINLSpSGDLTV----NAFDAVWYAKlDSAWASKLFYFKAGVYTQDNTGYTTEGGSATFYKLAIAH 218
Cdd:pfam08787 157 SYEIVVG-GGKLTVtingEGKSTVSYTL-DPAWAGSEFYFKAGVYNQDNTGDSGDYAEVTFYDLTVSH 222
 
Name Accession Description Interval E-value
Alginate_lyase2 pfam08787
Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. ...
2-218 1.06e-77

Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. They cleave the glycosidic linkage of alignate through a beta-elimination reaction. This family forms an all beta fold and is different to all alpha fold of pfam05426.


Pssm-ID: 400923  Cd Length: 222  Bit Score: 232.66  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791   2 IDLATWNLSVPVGSPATIIETPKLVKGYRDGYF---QSGDTLFFWAPVTGSTTENAKYPRSELRETTSDGRVFNWAYSSA 78
Cdd:pfam08787   1 FDLSNWKLTLPVYGSATEIEPSELNGGYASDYFyydSDDGALVFWAPNSGATTANSTYPRSELREMLPDGSSNNWSLSSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791  79 DNFLRATLEVDQVPSTGKIVIGQIHCYQS---TEPLLKVEYqykeKLQTGNIVAKFRR-TPDSEIEVITIAQGVPLNKQF 154
Cdd:pfam08787  81 DNQLEATLKVDHVPSGGKVVVGQIHGKDSsdnTEPLLKLYY----RHYKGSLYAYLRDnFDDGGDVNYTIYGGIDLGEWF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028332791 155 NYTINLSpSGDLTV----NAFDAVWYAKlDSAWASKLFYFKAGVYTQDNTGYTTEGGSATFYKLAIAH 218
Cdd:pfam08787 157 SYEIVVG-GGKLTVtingEGKSTVSYTL-DPAWAGSEFYFKAGVYNQDNTGDSGDYAEVTFYDLTVSH 222
 
Name Accession Description Interval E-value
Alginate_lyase2 pfam08787
Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. ...
2-218 1.06e-77

Alginate lyase; Alginate lyases are enzymes that degrade the linear polysaccharide alignate. They cleave the glycosidic linkage of alignate through a beta-elimination reaction. This family forms an all beta fold and is different to all alpha fold of pfam05426.


Pssm-ID: 400923  Cd Length: 222  Bit Score: 232.66  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791   2 IDLATWNLSVPVGSPATIIETPKLVKGYRDGYF---QSGDTLFFWAPVTGSTTENAKYPRSELRETTSDGRVFNWAYSSA 78
Cdd:pfam08787   1 FDLSNWKLTLPVYGSATEIEPSELNGGYASDYFyydSDDGALVFWAPNSGATTANSTYPRSELREMLPDGSSNNWSLSSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028332791  79 DNFLRATLEVDQVPSTGKIVIGQIHCYQS---TEPLLKVEYqykeKLQTGNIVAKFRR-TPDSEIEVITIAQGVPLNKQF 154
Cdd:pfam08787  81 DNQLEATLKVDHVPSGGKVVVGQIHGKDSsdnTEPLLKLYY----RHYKGSLYAYLRDnFDDGGDVNYTIYGGIDLGEWF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028332791 155 NYTINLSpSGDLTV----NAFDAVWYAKlDSAWASKLFYFKAGVYTQDNTGYTTEGGSATFYKLAIAH 218
Cdd:pfam08787 157 SYEIVVG-GGKLTVtingEGKSTVSYTL-DPAWAGSEFYFKAGVYNQDNTGDSGDYAEVTFYDLTVSH 222
 
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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