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Conserved domains on  [gi|1087789978|gb|AOX99733|]
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DUF4442 domain-containing protein [Jeongeupia sp. USM3]

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 ...
 21-152 9.04e-73

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: 214.04  E-value: 9.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  21 RWLFSRLVCFKAPYFGSISPRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQ 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1087789978 101 VGYLKKAETGLRAVATVTQPPvWSDGQDLPVNVDVTDAAGQVVVRATITMWV 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPED-WGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-152 9.04e-73

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: 214.04  E-value: 9.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  21 RWLFSRLVCFKAPYFGSISPRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQ 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1087789978 101 VGYLKKAETGLRAVATVTQPPvWSDGQDLPVNVDVTDAAGQVVVRATITMWV 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPED-WGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-157 8.40e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.99  E-value: 8.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  31 KAPYFGSISPRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG 110
Cdd:COG2050    14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1087789978 111 --LRAVATVTQppvwSDGQDLPVNVDVTDAAGQVVVRATITMWVSAKKR 157
Cdd:COG2050    94 drLTAEARVVR----RGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 40-150 1.09e-16

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: 71.05  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  40 PRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG-LRAVATVT 118
Cdd:cd03443     4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARVV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1087789978 119 QppvwSDGQDLPVNVDVTDAAGQVVVRATITM 150
Cdd:cd03443    84 K----LGRRLAVVEVEVTDEDGKLVATARGTF 111
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 41-117 4.21e-03

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 35.01  E-value: 4.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1087789978  41 RFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG-LRAVATV 117
Cdd:TIGR00369   9 EIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGkVRAIAQV 86
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-152 9.04e-73

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: 214.04  E-value: 9.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  21 RWLFSRLVCFKAPYFGSISPRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQ 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1087789978 101 VGYLKKAETGLRAVATVTQPPvWSDGQDLPVNVDVTDAAGQVVVRATITMWV 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDPED-WGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-157 8.40e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.99  E-value: 8.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  31 KAPYFGSISPRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG 110
Cdd:COG2050    14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1087789978 111 --LRAVATVTQppvwSDGQDLPVNVDVTDAAGQVVVRATITMWVSAKKR 157
Cdd:COG2050    94 drLTAEARVVR----RGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 40-150 1.09e-16

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: 71.05  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1087789978  40 PRFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG-LRAVATVT 118
Cdd:cd03443     4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARVV 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1087789978 119 QppvwSDGQDLPVNVDVTDAAGQVVVRATITM 150
Cdd:cd03443    84 K----LGRRLAVVEVEVTDEDGKLVATARGTF 111
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 41-117 4.21e-03

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 35.01  E-value: 4.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1087789978  41 RFERLEPGRCELTIAKRRKVLNHIGTVHAIAMCNMAELAAGTMTDVTIPASHRWIPKGMQVGYLKKAETG-LRAVATV 117
Cdd:TIGR00369   9 EIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGkVRAIAQV 86
 
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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