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Conserved domains on  [gi|489521226|ref|WP_003426017|]
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DHHW family protein [Clostridioides difficile]

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 ...
62-348 4.83e-13

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: 69.31  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226  62 FSDQFPFREELSEIYSKV-----------QIVLGKNK---IKNYYLLDDnWIMPTPsksMSEKELKDAANEINELSKIAS 127
Cdd:cd14440    1 FSDHFGFRDQLISADSALlysllgessnpRVIIGKDGwlfLGEDYMLED-YCGRDP---LSEEDLRRWVALLERRRDWLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 128 DSNKKVYYVSTPNKESMLAHLYPKYVDGLKNdiSNKNAFKSYLDLET-INVIDVDEHFLKEfnESQREDLYFKTDHHWNG 206
Cdd:cd14440   77 ARGIPFVVVVAPNKHTIYPEHLPSWYPGKSP--TRLDQLLALLLSAAgVGVVDLRPALLEA--KATGAPVYYKTDTHWNF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 207 IGAYEGFKCIIEDMN-IVNNISWDSYTQTMYDEGYflgsynKNLNKLvkedetipyVHLKEKPNYEYYKFDGKTetkcke 285
Cdd:cd14440  153 YGAYVAYRAIAEALGpGVPALWPLASVEYDESTVG------GDLANM---------LGLPEALEEDRLPDESKP------ 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489521226 286 eDVIATRKNEKEILYGGAYMFGNAcsilkIRNEDALSDKKILIIRDSYQAPTSWLFADIFSEV 348
Cdd:cd14440  212 -PLQARRIDDDTATLPFPLDKPKL-----TTNSPAGNNKSALVFRDSFGEALSPYLAETFSRV 268
 
Name Accession Description Interval E-value
AlgX_N_like_3 cd14440
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
62-348 4.83e-13

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: 69.31  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226  62 FSDQFPFREELSEIYSKV-----------QIVLGKNK---IKNYYLLDDnWIMPTPsksMSEKELKDAANEINELSKIAS 127
Cdd:cd14440    1 FSDHFGFRDQLISADSALlysllgessnpRVIIGKDGwlfLGEDYMLED-YCGRDP---LSEEDLRRWVALLERRRDWLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 128 DSNKKVYYVSTPNKESMLAHLYPKYVDGLKNdiSNKNAFKSYLDLET-INVIDVDEHFLKEfnESQREDLYFKTDHHWNG 206
Cdd:cd14440   77 ARGIPFVVVVAPNKHTIYPEHLPSWYPGKSP--TRLDQLLALLLSAAgVGVVDLRPALLEA--KATGAPVYYKTDTHWNF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 207 IGAYEGFKCIIEDMN-IVNNISWDSYTQTMYDEGYflgsynKNLNKLvkedetipyVHLKEKPNYEYYKFDGKTetkcke 285
Cdd:cd14440  153 YGAYVAYRAIAEALGpGVPALWPLASVEYDESTVG------GDLANM---------LGLPEALEEDRLPDESKP------ 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489521226 286 eDVIATRKNEKEILYGGAYMFGNAcsilkIRNEDALSDKKILIIRDSYQAPTSWLFADIFSEV 348
Cdd:cd14440  212 -PLQARRIDDDTATLPFPLDKPKL-----TTNSPAGNNKSALVFRDSFGEALSPYLAETFSRV 268
DHHW pfam14286
DHHW protein; This family of proteins is found in bacteria. Proteins in this family are ...
194-245 1.05e-04

DHHW protein; This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 404 amino acids in length. There is a conserved DHHW motif. There is some distant homology to the Lipase_GDSL_2 family.


Pssm-ID: 405044 [Multi-domain]  Cd Length: 385  Bit Score: 43.92  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489521226  194 EDLYFKTDHHWNGIGAYEGFKCIIEDMNiVNNISWDSYTQtmYDEGYFLGSY 245
Cdd:pfam14286 233 EYIYFRTDHHWTALGAYYAYEAFAAAKG-KKALPLDKFEE--HDFGDFLGSF 281
 
Name Accession Description Interval E-value
AlgX_N_like_3 cd14440
Uncharacterized proteins similar to putative alginate O-acetyltransferase; The alginate ...
62-348 4.83e-13

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: 69.31  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226  62 FSDQFPFREELSEIYSKV-----------QIVLGKNK---IKNYYLLDDnWIMPTPsksMSEKELKDAANEINELSKIAS 127
Cdd:cd14440    1 FSDHFGFRDQLISADSALlysllgessnpRVIIGKDGwlfLGEDYMLED-YCGRDP---LSEEDLRRWVALLERRRDWLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 128 DSNKKVYYVSTPNKESMLAHLYPKYVDGLKNdiSNKNAFKSYLDLET-INVIDVDEHFLKEfnESQREDLYFKTDHHWNG 206
Cdd:cd14440   77 ARGIPFVVVVAPNKHTIYPEHLPSWYPGKSP--TRLDQLLALLLSAAgVGVVDLRPALLEA--KATGAPVYYKTDTHWNF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 207 IGAYEGFKCIIEDMN-IVNNISWDSYTQTMYDEGYflgsynKNLNKLvkedetipyVHLKEKPNYEYYKFDGKTetkcke 285
Cdd:cd14440  153 YGAYVAYRAIAEALGpGVPALWPLASVEYDESTVG------GDLANM---------LGLPEALEEDRLPDESKP------ 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489521226 286 eDVIATRKNEKEILYGGAYMFGNAcsilkIRNEDALSDKKILIIRDSYQAPTSWLFADIFSEV 348
Cdd:cd14440  212 -PLQARRIDDDTATLPFPLDKPKL-----TTNSPAGNNKSALVFRDSFGEALSPYLAETFSRV 268
AlgX_N_like cd14439
N-terminal catalytic domain of putative alginate O-acetyltranferase and similar proteins; The ...
57-261 2.40e-08

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: 55.15  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226  57 EFESYFSDQFPFREELSEIYSKVqiVLGKNKIKNYYLLDDNWIMPTPSKSMSEKELKDAAN---EINELSKIASDSNKKV 133
Cdd:cd14439    6 VLASLLADQNSLRDFWRAQSLLL--LAGNRGSGGVLIGKDGWLFLKPDLYDARTDLDAPAEnveAIAEFRKQLDKRGIRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 134 YYVSTPNKesmlAHLYPKYVDGLK--NDISNKN--AFKSYLDLETINVIDVDEHFLKEfneSQREDLYFKTDHHWNGIGA 209
Cdd:cd14439   84 LVLPVPAK----AKIYPERLPAYVtpPDAVNPNyrAFLSRLRKAGVDVLDLRPVLAQA---KEGEQLFYRTDHHWTPLGA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489521226 210 YEGFKCIIEDMNIVNNISWDSYTQTMYDEGYfLGSYNKNLNKLVKEDETIPY 261
Cdd:cd14439  157 RLAAQQVAEALKKKPGYEVPPEKYDTSKVEE-SRSRLGDLAKRLGLDELLKE 207
DHHW pfam14286
DHHW protein; This family of proteins is found in bacteria. Proteins in this family are ...
194-245 1.05e-04

DHHW protein; This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 404 amino acids in length. There is a conserved DHHW motif. There is some distant homology to the Lipase_GDSL_2 family.


Pssm-ID: 405044 [Multi-domain]  Cd Length: 385  Bit Score: 43.92  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489521226  194 EDLYFKTDHHWNGIGAYEGFKCIIEDMNiVNNISWDSYTQtmYDEGYFLGSY 245
Cdd:pfam14286 233 EYIYFRTDHHWTALGAYYAYEAFAAAKG-KKALPLDKFEE--HDFGDFLGSF 281
AlgX_N cd14441
N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; The alginate ...
95-272 1.52e-03

N-terminal catalytic domain of the putative alginate O-acetyltranferase AlgX; 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. This 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. AlgX contains a C-terminal carbohydrate binding domain that belongs to the wider family of CBM6-CBM35-CBM36_like domains.


Pssm-ID: 270207  Cd Length: 310  Bit Score: 40.37  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226  95 DDNWIMPTPSKSMSEKELKD-AANEINELSKIASDSNKKVYYVSTPNKESMLA-HLYPKYVDGLKNDISNKNAFKSYLD- 171
Cdd:cd14441   28 KDGWLFRSNADLRSQFGLSPeTLAALAALSDALKARGTELVLVPQPTRGLVHAeKLPPAAYAYGFDAAVARQSYRATLAr 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489521226 172 LETINVIDVDEHFLKEFNESqREDLYFKTDHHWNGIGAYEGFKCI---IEDMNIVNNISWDSY-TQTMYDEGyFLGSYNK 247
Cdd:cd14441  108 LRDAGILVPDLLPLMDTKAG-GEPFFFKRDHHWTPEGARASAKAVaetIRGLPAYADLPKQAFeTEPGGLLP-KSGSLGK 185
                        170       180
                 ....*....|....*....|....*
gi 489521226 248 NLNKLVkeDETIPYVHLkekPNYEY 272
Cdd:cd14441  186 ALQAIC--GQKYPTEYV---DRYET 205
 
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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