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Conserved domains on  [gi|589533610|gb|EXI13383|]
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hypothetical protein J604_0892 [Acinetobacter sp. 694762]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
25-156 9.97e-32

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member pfam14539:

Pssm-ID: 469797  Cd Length: 131  Bit Score: 110.42  E-value: 9.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610   25 LWSKAFGRIVPMVGTANIRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVD 104
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589533610  105 YLKVVEGGLTATATLSAEQQKyiadhEKGELVIPVTVIDDAGNEPIQCQMLW 156
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEDWG-----EKGDLPVPVEVRDDAGTEVVRATITL 129
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
25-156 9.97e-32

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: 110.42  E-value: 9.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610   25 LWSKAFGRIVPMVGTANIRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVD 104
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589533610  105 YLKVVEGGLTATATLSAEQQKyiadhEKGELVIPVTVIDDAGNEPIQCQMLW 156
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEDWG-----EKGDLPVPVEVRDDAGTEVVRATITL 129
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
28-163 7.55e-19

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 77.68  E-value: 7.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610  28 KAFGRIVPMVGTANIRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVDYLK 107
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLR 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 589533610 108 VVEGG--LTATATLsaeqqkyiaDHEKGEL-VIPVTVIDDAGNEPIQCQMLWAWLPKRK 163
Cdd:COG2050   89 PARLGdrLTAEARV---------VRRGRRLaVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
42-136 2.80e-15

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: 67.58  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610  42 IRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVDYLKVVEGG-LTATAT-L 119
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARvV 83
                         90       100
                 ....*....|....*....|.
gi 589533610 120 SAEQQKYIAD----HEKGELV 136
Cdd:cd03443   84 KLGRRLAVVEvevtDEDGKLV 104
 
Name Accession Description Interval E-value
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
25-156 9.97e-32

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: 110.42  E-value: 9.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610   25 LWSKAFGRIVPMVGTANIRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVD 104
Cdd:pfam14539   3 LFSRAVCRKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 589533610  105 YLKVVEGGLTATATLSAEQQKyiadhEKGELVIPVTVIDDAGNEPIQCQMLW 156
Cdd:pfam14539  83 YLAKATGDLTAVAELDPEDWG-----EKGDLPVPVEVRDDAGTEVVRATITL 129
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
28-163 7.55e-19

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 77.68  E-value: 7.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610  28 KAFGRIVPMVGTANIRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVDYLK 107
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLR 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 589533610 108 VVEGG--LTATATLsaeqqkyiaDHEKGEL-VIPVTVIDDAGNEPIQCQMLWAWLPKRK 163
Cdd:COG2050   89 PARLGdrLTAEARV---------VRRGRRLaVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
42-136 2.80e-15

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: 67.58  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610  42 IRYLEVDVNHVTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVDYLKVVEGG-LTATAT-L 119
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGdLTARARvV 83
                         90       100
                 ....*....|....*....|.
gi 589533610 120 SAEQQKYIAD----HEKGELV 136
Cdd:cd03443   84 KLGRRLAVVEvevtDEDGKLV 104
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
52-136 7.25e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 34.37  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533610  52 VTVRLENQKNMQNHIKGVHAAAMALLAETATGFLTGLHIPDNRILLIKSLHVDYLKVVEGG--LTATATLSAEQQKYI-- 127
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGdtLTVEAEVVRVGRSSVtv 80
                         90
                 ....*....|..
gi 589533610 128 ---ADHEKGELV 136
Cdd:cd03440   81 eveVRNEDGKLV 92
 
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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