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Conserved domains on  [gi|503554062|ref|WP_013788138|]
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MULTISPECIES: transcription factor FapR [Thermoanaerobacterium]

Protein Classification

transcription factor FapR( domain architecture ID 11480274)

transcription factor FapR regulates membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04424 PRK04424
transcription factor FapR;
4-187 1.75e-110

transcription factor FapR;


:

Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 313.30  E-value: 1.75e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062   4 KLSKRDRLKKLKIEIEKYPFYTDDELADLFSVSVQTIRLDRMELGIPELRERIKNVAEKNYNKVKAIVGSEIVGELIDLE 83
Cdd:PRK04424   2 KLSKKERQKALQELIEENPFITDEELAEKFGVSIQTIRLDRMELGIPELRERIKHVAEKNYDKVKSLPEEEVVGELIDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062  84 LGKSGISVFEPTPEMAFLKTKIIRGHYIYSQAESLAISVIDAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFV 163
Cdd:PRK04424  82 LGRSAISILEITEEMVFSKTGIARGHHLFAQANSLAVAVIDAELALTGVANIRFKRPVKLGERVVAKAEVVRKKGNKYIV 161

                        170       180
                 ....*....|....*....|....
gi 503554062 164 WVMIKVKDREVFRGKFILVSLESD 187
Cdd:PRK04424 162 EVKSYVGDELVFRGKFIMYRSSEE 185
 
Name Accession Description Interval E-value
PRK04424 PRK04424
transcription factor FapR;
4-187 1.75e-110

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 313.30  E-value: 1.75e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062   4 KLSKRDRLKKLKIEIEKYPFYTDDELADLFSVSVQTIRLDRMELGIPELRERIKNVAEKNYNKVKAIVGSEIVGELIDLE 83
Cdd:PRK04424   2 KLSKKERQKALQELIEENPFITDEELAEKFGVSIQTIRLDRMELGIPELRERIKHVAEKNYDKVKSLPEEEVVGELIDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062  84 LGKSGISVFEPTPEMAFLKTKIIRGHYIYSQAESLAISVIDAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFV 163
Cdd:PRK04424  82 LGRSAISILEITEEMVFSKTGIARGHHLFAQANSLAVAVIDAELALTGVANIRFKRPVKLGERVVAKAEVVRKKGNKYIV 161

                        170       180
                 ....*....|....*....|....
gi 503554062 164 WVMIKVKDREVFRGKFILVSLESD 187
Cdd:PRK04424 162 EVKSYVGDELVFRGKFIMYRSSEE 185
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 105-183 5.03e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 49.94  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062 105 IIRGHYIYSQAESL----AISVIDAEAALIGV-ANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKVKDREV---FR 176
Cdd:COG2050   49 TVHGGALAALADSAaglaANSALPPGRRAVTIeLNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLvatAT 128


                 ....*..
gi 503554062 177 GKFILVS 183
Cdd:COG2050  129 GTFAVLP 135
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 105-182 2.39e-04

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: 39.00  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062 105 IIRGHYIYSQAESLAI-----SVIDAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKVKDRE-VFRGK 178
Cdd:cd03440   17 IVHGGLLLALADEAAGaaaarLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKlVATAT 96


                 ....
gi 503554062 179 FILV 182
Cdd:cd03440   97 ATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 106-174 5.91e-04

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 37.23  E-value: 5.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062  106 IRGHYIYSQAESLAISVIdaeaaliGVANIKYKYPVKIGDRLVAKAEVTRkRGNKYFVW-VMIKVKDREV 174
Cdd:pfam03061  16 AAGAAARRLGGSQQVVVV-------VELSIDFLRPARLGDRLTVEARVVR-LGRTSAVVeVEVRDEDGRL 77
 
Name Accession Description Interval E-value
PRK04424 PRK04424
transcription factor FapR;
4-187 1.75e-110

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 313.30  E-value: 1.75e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062   4 KLSKRDRLKKLKIEIEKYPFYTDDELADLFSVSVQTIRLDRMELGIPELRERIKNVAEKNYNKVKAIVGSEIVGELIDLE 83
Cdd:PRK04424   2 KLSKKERQKALQELIEENPFITDEELAEKFGVSIQTIRLDRMELGIPELRERIKHVAEKNYDKVKSLPEEEVVGELIDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062  84 LGKSGISVFEPTPEMAFLKTKIIRGHYIYSQAESLAISVIDAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFV 163
Cdd:PRK04424  82 LGRSAISILEITEEMVFSKTGIARGHHLFAQANSLAVAVIDAELALTGVANIRFKRPVKLGERVVAKAEVVRKKGNKYIV 161

                        170       180
                 ....*....|....*....|....
gi 503554062 164 WVMIKVKDREVFRGKFILVSLESD 187
Cdd:PRK04424 162 EVKSYVGDELVFRGKFIMYRSSEE 185
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 105-183 5.03e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 49.94  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062 105 IIRGHYIYSQAESL----AISVIDAEAALIGV-ANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKVKDREV---FR 176
Cdd:COG2050   49 TVHGGALAALADSAaglaANSALPPGRRAVTIeLNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLvatAT 128


                 ....*..
gi 503554062 177 GKFILVS 183
Cdd:COG2050  129 GTFAVLP 135
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 129-182 2.22e-04

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 39.79  E-value: 2.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503554062 129 LIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKVKDREVFRGKFILV 182
Cdd:COG0764   84 FLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFA 137
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 105-182 2.39e-04

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: 39.00  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062 105 IIRGHYIYSQAESLAI-----SVIDAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKVKDRE-VFRGK 178
Cdd:cd03440   17 IVHGGLLLALADEAAGaaaarLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKlVATAT 96


                 ....
gi 503554062 179 FILV 182
Cdd:cd03440   97 ATFV 100
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 134-181 5.27e-04

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 38.29  E-value: 5.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503554062 134 NIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKV---KDREVFRGKFIL 181
Cdd:cd03449   76 SLRFLRPVFIGDTVTATVTVTEKREDKKRVTLETVCtnqNGEVVIEGEAVV 126
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 106-174 5.91e-04

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 37.23  E-value: 5.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503554062  106 IRGHYIYSQAESLAISVIdaeaaliGVANIKYKYPVKIGDRLVAKAEVTRkRGNKYFVW-VMIKVKDREV 174
Cdd:pfam03061  16 AAGAAARRLGGSQQVVVV-------VELSIDFLRPARLGDRLTVEARVVR-LGRTSAVVeVEVRDEDGRL 77
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
124-182 1.72e-03

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503554062 124 DAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNK-----YFVWVMIKVKDREVFRGKFILV 182
Cdd:COG2030   72 GTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKRESKsrgivTLRTTVTNQDGEVVLTGEATVL 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 124-169 8.71e-03

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 34.93  E-value: 8.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 503554062 124 DAEAALIGVANIKYKYPVKIGDRLVAKAEVTRKRGNKYFVWVMIKV 169
Cdd:cd03441   64 GTDGANLGSQSVRFLAPVFPGDTLRVEVEVLGKRPSKGRGVVTVRT 109
 
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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