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Conserved domains on  [gi|2125645018|ref|WP_227403273|]
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hypothetical protein [Holdemanella sp. DFI.5.55]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AlgX_N_like super family cl16774
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
 28-164 6.53e-20

N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases.


The actual alignment was detected with superfamily member cd14440:

Pssm-ID: 450039 [Multi-domain]  Cd Length: 315  Bit Score: 84.33  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  28 QVYYKSDTHFNQIGAFVTVQALKDKIDGKTDKLKDVKFGKI-TNHYSGDLARLCDMQDTFNNDTQ-YQLDP--------- 96
Cdd:cd14440   141 PVYYKTDTHWNFYGAYVAYRAIAEALGPGVPALWPLASVEYdESTVGGDLANMLGLPEALEEDRLpDESKPplqarridd 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  97 -------------ATVNTKIKSDKKILVIGDSYSDEMLSILRQYFAEAQTVNIWSFEPSLLDEYKPDIVVWEHAERYTDR 163
Cdd:cd14440   221 dtatlpfpldkpkLTTNSPAGNNKSALVFRDSFGEALSPYLAETFSRVVYLWSPEIDQALIEAEKPDVVVLEIVERVLRQ 300


                  .
gi 2125645018 164 F 164
Cdd:cd14440   301 L 301
 
Name Accession Description Interval E-value
AlgX_N_like_3 cd14440
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
 28-164 6.53e-20

Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N.


Pssm-ID: 270206 [Multi-domain]  Cd Length: 315  Bit Score: 84.33  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  28 QVYYKSDTHFNQIGAFVTVQALKDKIDGKTDKLKDVKFGKI-TNHYSGDLARLCDMQDTFNNDTQ-YQLDP--------- 96
Cdd:cd14440   141 PVYYKTDTHWNFYGAYVAYRAIAEALGPGVPALWPLASVEYdESTVGGDLANMLGLPEALEEDRLpDESKPplqarridd 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  97 -------------ATVNTKIKSDKKILVIGDSYSDEMLSILRQYFAEAQTVNIWSFEPSLLDEYKPDIVVWEHAERYTDR 163
Cdd:cd14440   221 dtatlpfpldkpkLTTNSPAGNNKSALVFRDSFGEALSPYLAETFSRVVYLWSPEIDQALIEAEKPDVVVLEIVERVLRQ 300


                  .
gi 2125645018 164 F 164
Cdd:cd14440   301 L 301
ALGX pfam16822
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
 22-158 6.77e-06

SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.


Pssm-ID: 435599  Cd Length: 267  Bit Score: 44.64  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  22 KSEKKQQVYYKSDTHFNQIGAFVTVQALKDKI---------DGKTDKLKDVkfgkITNHYSGDLARLCDMQDTFNND--- 89
Cdd:pfam16822  99 AEADGKPVFLRTDTHWTPAGAEAAARAVAAAIratpgfaglPPQAFTTETV----GTLPRPGDLANLAGLDCLGNRLgpr 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  90 ---TQYQLDPATVNTKIKS------DKKILVIGDSYSDE----MLSILRQYFAeAQTVNIW----SFEPSLLdEY----- 147
Cdd:pfam16822 175 dqvPRRETTPVSASDDADGlfgdapAPRVALVGTSYSANpywnFVGFLQQALG-RDVLNVAleggGPSGAML-EYlasea 252

                         170
                  ....*....|....*
gi 2125645018 148 ----KPDIVVWEHAE 158
Cdd:pfam16822 253 fqnaPPQLVIWEFPE 267
 
Name Accession Description Interval E-value
AlgX_N_like_3 cd14440
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
 28-164 6.53e-20

Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. Members of this uncharacterized protein family resemble AlgX_N.


Pssm-ID: 270206 [Multi-domain]  Cd Length: 315  Bit Score: 84.33  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  28 QVYYKSDTHFNQIGAFVTVQALKDKIDGKTDKLKDVKFGKI-TNHYSGDLARLCDMQDTFNNDTQ-YQLDP--------- 96
Cdd:cd14440   141 PVYYKTDTHWNFYGAYVAYRAIAEALGPGVPALWPLASVEYdESTVGGDLANMLGLPEALEEDRLpDESKPplqarridd 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  97 -------------ATVNTKIKSDKKILVIGDSYSDEMLSILRQYFAEAQTVNIWSFEPSLLDEYKPDIVVWEHAERYTDR 163
Cdd:cd14440   221 dtatlpfpldkpkLTTNSPAGNNKSALVFRDSFGEALSPYLAETFSRVVYLWSPEIDQALIEAEKPDVVVLEIVERVLRQ 300


                  .
gi 2125645018 164 F 164
Cdd:cd14440   301 L 301
AlgX_N_like cd14439
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
 24-170 5.04e-09

N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The alginate biosynthesis protein AlgX appears to be directly involved in the O-acetylation of alginate, an exopolysaccharide that is associated with the formation of persistent biofilms, such as those by mucoid strains of Pseudomonas aeruginosa that affect patients suffering from cystic fibrosis. Its N-terminal catalytic domain resembles SGNH hydrolases, though with a permuted topology. The active site matches that of the SGNH hydrolases, is well conserved, and has been verified experimentally. This wider family includes AlgX, AlgJ, AlgV, and a number of uncharacterized families, some of which may have been mis-annotated in sequence databases.


Pssm-ID: 270205 [Multi-domain]  Cd Length: 316  Bit Score: 54.00  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  24 EKKQQVYYKSDTHFNQIGAFVTVQALKDKIDGKTDKLKDVKF-----GKITNHYSGDLARLCDMQDTFNNDTQYQ----L 94
Cdd:cd14439   138 KEGEQLFYRTDHHWTPLGARLAAQQVAEALKKKPGYEVPPEKydtskVEESRSRLGDLAKRLGLDELLKEDLIYLervvL 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  95 DPATVNTKIKSDK---KILVIGDSYS----------DEMLSILRQYFAeAQTVNIWS-----------FEPSLLDEYKPD 150
Cdd:cd14439   218 NAGSPQSALFSDSgapKVVLLGDSFSnvfilellikDGFAQHLAPALG-RPVDEIAKngggsgsrrdyLAREEFKGPPKK 296

                         170       180
                  ....*....|....*....|
gi 2125645018 151 IVVWEHAERYTDRFNWISLF 170
Cdd:cd14439   297 VVIWEFAEREAADNAWRQVD 316
ALGX pfam16822
SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The ...
 22-158 6.77e-06

SGNH hydrolase-like domain, acetyltransferase AlgX; ALGX is a family found in bacteria. The domain demonstrates catalytic activity similar to that of the SGNH hydrolase-like domain, with the typical Ser-His-Asp triad found in this enzyme. Alginate is an exopolysaccharide that contributes to biofilm formation. ALGX is secreted into the biofilm and is responsible for the acetylation of biofilm polymers that help protect them from host destruction.


Pssm-ID: 435599  Cd Length: 267  Bit Score: 44.64  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  22 KSEKKQQVYYKSDTHFNQIGAFVTVQALKDKI---------DGKTDKLKDVkfgkITNHYSGDLARLCDMQDTFNND--- 89
Cdd:pfam16822  99 AEADGKPVFLRTDTHWTPAGAEAAARAVAAAIratpgfaglPPQAFTTETV----GTLPRPGDLANLAGLDCLGNRLgpr 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125645018  90 ---TQYQLDPATVNTKIKS------DKKILVIGDSYSDE----MLSILRQYFAeAQTVNIW----SFEPSLLdEY----- 147
Cdd:pfam16822 175 dqvPRRETTPVSASDDADGlfgdapAPRVALVGTSYSANpywnFVGFLQQALG-RDVLNVAleggGPSGAML-EYlasea 252

                         170
                  ....*....|....*
gi 2125645018 148 ----KPDIVVWEHAE 158
Cdd:pfam16822 253 fqnaPPQLVIWEFPE 267
 
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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