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Conserved domains on  [gi|1377620536|gb|PTU32275|]
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DUF4442 domain-containing protein [Stenotrophobium rhamnosiphilum]

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 7.62e-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: 214.43  E-value: 7.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  21 KWFFSLLISRRAPYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMT 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1377620536 101 VEYLKKGETSLRAIAELDPmPTFGAATELPVTVNVYDTQKQLVFRAVINMWI 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDP-EDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 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 7.62e-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: 214.43  E-value: 7.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  21 KWFFSLLISRRAPYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMT 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1377620536 101 VEYLKKGETSLRAIAELDPmPTFGAATELPVTVNVYDTQKQLVFRAVINMWI 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDP-EDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 30-156 5.96e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 74.98  E-value: 5.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  30 RRAPYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKGET 109
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1377620536 110 SLRAIAEldpmptfgaATEL-------PVTVNVYDTQKQLVFRAVINMWISPKK 156
Cdd:COG2050    93 GDRLTAE---------ARVVrrgrrlaVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 41-146 2.11e-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: 62.58  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  41 TFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKG-ETSLRAIAELDP 119
Cdd:cd03443     5 RVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVVK 84

                          90       100
                  ....*....|....*....|....*..
gi 1377620536 120 MptfgAATELPVTVNVYDTQKQLVFRA 146
Cdd:cd03443    85 L----GRRLAVVEVEVTDEDGKLVATA 107
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 33-116 1.59e-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: 36.17  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  33 PYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKG-ETSL 111
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPArEGKV 80


                  ....*
gi 1377620536 112 RAIAE 116
Cdd:TIGR00369  81 RAIAQ 85
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 21-152 7.62e-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: 214.43  E-value: 7.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  21 KWFFSLLISRRAPYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMT 100
Cdd:pfam14539   1 KRLFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1377620536 101 VEYLKKGETSLRAIAELDPmPTFGAATELPVTVNVYDTQKQLVFRAVINMWI 152
Cdd:pfam14539  81 VDYLAKATGDLTAVAELDP-EDWGEKGDLPVPVEVRDDAGTEVVRATITLWV 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 30-156 5.96e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 74.98  E-value: 5.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  30 RRAPYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKGET 109
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1377620536 110 SLRAIAEldpmptfgaATEL-------PVTVNVYDTQKQLVFRAVINMWISPKK 156
Cdd:COG2050    93 GDRLTAE---------ARVVrrgrrlaVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 41-146 2.11e-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: 62.58  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  41 TFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKG-ETSLRAIAELDP 119
Cdd:cd03443     5 RVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPArGGDLTARARVVK 84

                          90       100
                  ....*....|....*....|....*..
gi 1377620536 120 MptfgAATELPVTVNVYDTQKQLVFRA 146
Cdd:cd03443    85 L----GRRLAVVEVEVTDEDGKLVATA 107
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 33-116 1.59e-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: 36.17  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377620536  33 PYFSSIRATFEELRPGYCEVTAPKRRAVTNHIGTFHAIAMCNMAELAGGMMTEVSVPSTHRWIPKGMTVEYLKKG-ETSL 111
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPArEGKV 80


                  ....*
gi 1377620536 112 RAIAE 116
Cdd:TIGR00369  81 RAIAQ 85
 
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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