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Conserved domains on  [gi|1469545493|gb|RGR13880|]
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alginate lyase [Parabacteroides merdae]

Protein Classification

alginate lyase family protein( domain architecture ID 10527103)

alginate lyase family protein similar to Bacteroides ovatus alginate lyase that catalyzes the depolymerization of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alginate_lyase pfam05426
Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a ...
 51-325 6.02e-114

Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a family of 1-4-linked copolymers of beta -D-mannuronic acid (M) and alpha -L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyze the depolymerization of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end. This family adopts an all alpha fold.


:

Pssm-ID: 398861  Cd Length: 274  Bit Score: 333.26  E-value: 6.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493  51 AYRAERSAGGIHDFYSEGDYWwpNPINPD-SAYIRRDGQTNPDNFVAHRHAMIRFSSLVGDLTSAWLVTKDEKYIRQAVK 129
Cdd:pfam05426   5 KYKLSDPSGDKHDYLSEAPYW--DPTKPDgLPYIRRDGQRNPEDLVCDRKALAAWADAVALLALAYYLTGDKRYAEKAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 130 HIRAWFIAPETRMNPDLQYAQAIKGIVTGRGIGIIDTihllEVVQSLIKMEEAGVLAVEDVAGSRTWFSDYLKWLTTHPY 209
Cdd:pfam05426  83 LLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIIDT----EVLDALILLEAAPAWDPKDRKAIEAWFAQLLDWLQTSPK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 210 GVDEMNAKNNHGTCWVMQVAQYAKYTGDKEILDFCRNRYRSVLLPSQMAEDGSFPLELKRTKPYGYSLFNLDAMATICHI 289
Cdd:pfam05426 159 GRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAILPDQIAPDGSLPLELARTRALHYSNFALQALVMIAEI 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1469545493 290 LSDGEDDLWQYSMDDGRNMQKAVAWLFPYIADKSSW 325
Cdd:pfam05426 239 AERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
 
Name Accession Description Interval E-value
Alginate_lyase pfam05426
Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a ...
 51-325 6.02e-114

Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a family of 1-4-linked copolymers of beta -D-mannuronic acid (M) and alpha -L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyze the depolymerization of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end. This family adopts an all alpha fold.


Pssm-ID: 398861  Cd Length: 274  Bit Score: 333.26  E-value: 6.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493  51 AYRAERSAGGIHDFYSEGDYWwpNPINPD-SAYIRRDGQTNPDNFVAHRHAMIRFSSLVGDLTSAWLVTKDEKYIRQAVK 129
Cdd:pfam05426   5 KYKLSDPSGDKHDYLSEAPYW--DPTKPDgLPYIRRDGQRNPEDLVCDRKALAAWADAVALLALAYYLTGDKRYAEKAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 130 HIRAWFIAPETRMNPDLQYAQAIKGIVTGRGIGIIDTihllEVVQSLIKMEEAGVLAVEDVAGSRTWFSDYLKWLTTHPY 209
Cdd:pfam05426  83 LLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIIDT----EVLDALILLEAAPAWDPKDRKAIEAWFAQLLDWLQTSPK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 210 GVDEMNAKNNHGTCWVMQVAQYAKYTGDKEILDFCRNRYRSVLLPSQMAEDGSFPLELKRTKPYGYSLFNLDAMATICHI 289
Cdd:pfam05426 159 GRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAILPDQIAPDGSLPLELARTRALHYSNFALQALVMIAEI 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1469545493 290 LSDGEDDLWQYSMDDGRNMQKAVAWLFPYIADKSSW 325
Cdd:pfam05426 239 AERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
 
Name Accession Description Interval E-value
Alginate_lyase pfam05426
Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a ...
 51-325 6.02e-114

Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a family of 1-4-linked copolymers of beta -D-mannuronic acid (M) and alpha -L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyze the depolymerization of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end. This family adopts an all alpha fold.


Pssm-ID: 398861  Cd Length: 274  Bit Score: 333.26  E-value: 6.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493  51 AYRAERSAGGIHDFYSEGDYWwpNPINPD-SAYIRRDGQTNPDNFVAHRHAMIRFSSLVGDLTSAWLVTKDEKYIRQAVK 129
Cdd:pfam05426   5 KYKLSDPSGDKHDYLSEAPYW--DPTKPDgLPYIRRDGQRNPEDLVCDRKALAAWADAVALLALAYYLTGDKRYAEKAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 130 HIRAWFIAPETRMNPDLQYAQAIKGIVTGRGIGIIDTihllEVVQSLIKMEEAGVLAVEDVAGSRTWFSDYLKWLTTHPY 209
Cdd:pfam05426  83 LLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIIDT----EVLDALILLEAAPAWDPKDRKAIEAWFAQLLDWLQTSPK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545493 210 GVDEMNAKNNHGTCWVMQVAQYAKYTGDKEILDFCRNRYRSVLLPSQMAEDGSFPLELKRTKPYGYSLFNLDAMATICHI 289
Cdd:pfam05426 159 GRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAILPDQIAPDGSLPLELARTRALHYSNFALQALVMIAEI 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1469545493 290 LSDGEDDLWQYSMDDGRNMQKAVAWLFPYIADKSSW 325
Cdd:pfam05426 239 AERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
 
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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