NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1850192399|gb|QKJ05333|]
View 

alginate lyase family protein [Yersinia mollaretii ATCC 43969]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 63-343 3.09e-98

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: 293.97  E-value: 3.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399  63 SVMDKSI-VPPSGSKHDYLSLSAYWwpDSEKSDDLPWVRKDGQINPAskNGDSDGVRLADFTAQVQTLTLAWYFSSEQQY 141
Cdd:pfam05426   1 SVTAKYKlSDPSGDKHDYLSEAPYW--DPTKPDGLPYIRRDGQRNPE--DLVCDRKALAAWADAVALLALAYYLTGDKRY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 142 ADKAISLIRAWFIAPQTRMNPNLNFAQGVPGIAAGRGTGVLDgryfaTRIVDSLMMLRQNQHWTAEDESQMRQWMTAYLQ 221
Cdd:pfam05426  77 AEKAGELLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIID-----TEVLDALILLEAAPAWDPKDRKAIEAWFAQLLD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 222 WLQNSPAGKKEASAQNNHGNWYTAQVAGIAWYLQQPKVVAEMAELLKTK-LDTQLAAEGAQPLELARTRSFHYSYFSLQA 300
Cdd:pfam05426 152 WLQTSPKGRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAiLPDQIAPDGSLPLELARTRALHYSNFALQA 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1850192399 301 AVLMAQLADKVHIDLWRYQTPNGSGLIKALDFMAPFSDEQKKW 343
Cdd:pfam05426 232 LVMIAEIAERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
 
Name Accession Description Interval E-value
Alginate_lyase pfam05426
Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a ...
 63-343 3.09e-98

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: 293.97  E-value: 3.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399  63 SVMDKSI-VPPSGSKHDYLSLSAYWwpDSEKSDDLPWVRKDGQINPAskNGDSDGVRLADFTAQVQTLTLAWYFSSEQQY 141
Cdd:pfam05426   1 SVTAKYKlSDPSGDKHDYLSEAPYW--DPTKPDGLPYIRRDGQRNPE--DLVCDRKALAAWADAVALLALAYYLTGDKRY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 142 ADKAISLIRAWFIAPQTRMNPNLNFAQGVPGIAAGRGTGVLDgryfaTRIVDSLMMLRQNQHWTAEDESQMRQWMTAYLQ 221
Cdd:pfam05426  77 AEKAGELLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIID-----TEVLDALILLEAAPAWDPKDRKAIEAWFAQLLD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 222 WLQNSPAGKKEASAQNNHGNWYTAQVAGIAWYLQQPKVVAEMAELLKTK-LDTQLAAEGAQPLELARTRSFHYSYFSLQA 300
Cdd:pfam05426 152 WLQTSPKGRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAiLPDQIAPDGSLPLELARTRALHYSNFALQA 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1850192399 301 AVLMAQLADKVHIDLWRYQTPNGSGLIKALDFMAPFSDEQKKW 343
Cdd:pfam05426 232 LVMIAEIAERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
algL PRK00325
polysaccharide lyase;
212-339 1.28e-03

polysaccharide lyase;


Pssm-ID: 234727  Cd Length: 359  Bit Score: 40.46  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 212 MRQWM-----TAYLQWLQNSPAGKKEASAQ------------------------NNHGNWYTAQVAGIAWYLQQPKVVAE 262
Cdd:PRK00325  140 MRKWAlgamaGAYLRSTSRPLAAHQAQSRAieawlakladqvvadwdnlplekiNNHSYWAAWAVMATGVATDRRDLFDW 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1850192399 263 MAELLKTKLDtQLAAEGAQPLELAR-TRSFHYSYFSLQAAVLMAQLADKVHIDLWRYqtpNGSGLIKALDFMAPFSDE 339
Cdd:PRK00325  220 AVKEYRVGIN-QIDDDGFLPNEMKRgQRALAYHNYALPPLVMIAEFAQANGVDLYEE---NNGALQRLAERVAAGVRD 293
 
Name Accession Description Interval E-value
Alginate_lyase pfam05426
Alginate lyase; This family contains several bacterial alginate lyase proteins. Alginate is a ...
 63-343 3.09e-98

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: 293.97  E-value: 3.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399  63 SVMDKSI-VPPSGSKHDYLSLSAYWwpDSEKSDDLPWVRKDGQINPAskNGDSDGVRLADFTAQVQTLTLAWYFSSEQQY 141
Cdd:pfam05426   1 SVTAKYKlSDPSGDKHDYLSEAPYW--DPTKPDGLPYIRRDGQRNPE--DLVCDRKALAAWADAVALLALAYYLTGDKRY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 142 ADKAISLIRAWFIAPQTRMNPNLNFAQGVPGIAAGRGTGVLDgryfaTRIVDSLMMLRQNQHWTAEDESQMRQWMTAYLQ 221
Cdd:pfam05426  77 AEKAGELLRAWFLDPATRMNPNLEYAQAIPGIATGRGAGIID-----TEVLDALILLEAAPAWDPKDRKAIEAWFAQLLD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 222 WLQNSPAGKKEASAQNNHGNWYTAQVAGIAWYLQQPKVVAEMAELLKTK-LDTQLAAEGAQPLELARTRSFHYSYFSLQA 300
Cdd:pfam05426 152 WLQTSPKGRDEKAAKNNHGYWAALQVAAIALYLGDRDLFDWALKRYKRAiLPDQIAPDGSLPLELARTRALHYSNFALQA 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1850192399 301 AVLMAQLADKVHIDLWRYQTPNGSGLIKALDFMAPFSDEQKKW 343
Cdd:pfam05426 232 LVMIAEIAERNGVDLWEYRTPDGATLHKAVDFLLPYVADPETW 274
algL PRK00325
polysaccharide lyase;
212-339 1.28e-03

polysaccharide lyase;


Pssm-ID: 234727  Cd Length: 359  Bit Score: 40.46  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850192399 212 MRQWM-----TAYLQWLQNSPAGKKEASAQ------------------------NNHGNWYTAQVAGIAWYLQQPKVVAE 262
Cdd:PRK00325  140 MRKWAlgamaGAYLRSTSRPLAAHQAQSRAieawlakladqvvadwdnlplekiNNHSYWAAWAVMATGVATDRRDLFDW 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1850192399 263 MAELLKTKLDtQLAAEGAQPLELAR-TRSFHYSYFSLQAAVLMAQLADKVHIDLWRYqtpNGSGLIKALDFMAPFSDE 339
Cdd:PRK00325  220 AVKEYRVGIN-QIDDDGFLPNEMKRgQRALAYHNYALPPLVMIAEFAQANGVDLYEE---NNGALQRLAERVAAGVRD 293
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH