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Conserved domains on  [gi|658755466|ref|WP_029773430|]
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MULTISPECIES: hotdog fold domain-containing protein [Pseudoalteromonas]

Protein Classification

hotdog fold domain-containing protein( domain architecture ID 10629414)

hotdog fold domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases, similar to PaaI family thioesterases

CATH:  3.10.129.10
PubMed:  15307895
SCOP:  3000149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-153 1.18e-68

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


:

Pssm-ID: 434027  Cd Length: 131  Bit Score: 203.64  E-value: 1.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466   21 NWLFSKAVCIKAPYFGSMKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGM 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP-DTHRWIPKGM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 658755466  101 TVHYLAKVDTDVTAIAEIDlPRQWVDKEDLVVPVKLYNTRNELVFTADITMYI 153
Cdd:pfam14539  80 TVDYLAKATGDLTAVAELD-PEDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-153 1.18e-68

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 203.64  E-value: 1.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466   21 NWLFSKAVCIKAPYFGSMKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGM 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP-DTHRWIPKGM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 658755466  101 TVHYLAKVDTDVTAIAEIDlPRQWVDKEDLVVPVKLYNTRNELVFTADITMYI 153
Cdd:pfam14539  80 TVDYLAKATGDLTAVAELD-PEDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-157 7.99e-17

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 72.28  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466  31 KAPYFGSMKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGMTVHYL--AKV 108
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLrpARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 658755466 109 DTDVTAIAEIDlprqWVDKEDLVVPVKLYNTRNELVFTADITMYITEKK 157
Cdd:COG2050   93 GDRLTAEARVV----RRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 38-153 7.28e-13

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 61.03  E-value: 7.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466  38 MKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGMTVHYLAKV-DTDVTAIA 116
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPArGGDLTARA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 658755466 117 EIDlpRQWvdKEDLVVPVKLYNTRNELVFTADITMYI 153
Cdd:cd03443   81 RVV--KLG--RRLAVVEVEVTDEDGKLVATARGTFAV 113
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-153 1.18e-68

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 203.64  E-value: 1.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466   21 NWLFSKAVCIKAPYFGSMKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGM 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLP-DTHRWIPKGM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 658755466  101 TVHYLAKVDTDVTAIAEIDlPRQWVDKEDLVVPVKLYNTRNELVFTADITMYI 153
Cdd:pfam14539  80 TVDYLAKATGDLTAVAELD-PEDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-157 7.99e-17

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 72.28  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466  31 KAPYFGSMKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGMTVHYL--AKV 108
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLrpARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 658755466 109 DTDVTAIAEIDlprqWVDKEDLVVPVKLYNTRNELVFTADITMYITEKK 157
Cdd:COG2050   93 GDRLTAEARVV----RRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 38-153 7.28e-13

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 61.03  E-value: 7.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755466  38 MKPYVLDLREGHCSAVVKNRRSVHNHIGTIHAIAQCNLAELCAGVMVDATVPyKTHRWIPKGMTVHYLAKV-DTDVTAIA 116
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPArGGDLTARA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 658755466 117 EIDlpRQWvdKEDLVVPVKLYNTRNELVFTADITMYI 153
Cdd:cd03443   81 RVV--KLG--RRLAVVEVEVTDEDGKLVATARGTFAV 113
 
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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