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Conserved domains on  [gi|472255763|gb|AGI30294|]
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hypothetical protein I653_15250 [Bacillus subtilis subsp. subtilis str. BAB-1]

Protein Classification

hotdog fold thioesterase( domain architecture ID 10794535)

hotdog fold thioesterase similar to Bacillus subtilis putative esterase ComA2 and to thioesterase PaaI that functions in the aerobic phenylacetate degradation pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 6-123 3.20e-50

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: 155.20  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763    6 TLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVKEGT 85
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 472255763   86 VKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAV 123
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 6-123 3.20e-50

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: 155.20  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763    6 TLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVKEGT 85
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 472255763   86 VKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAV 123
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-126 1.85e-35

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 118.51  E-value: 1.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   4 KHTLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQNLIDHStQACVGLEINANHLKSVKE 83
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPG-RRAVTIELNINFLRPARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 472255763  84 G-TVKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAVIKK 126
Cdd:COG2050   93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 10-123 1.19e-32

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: 110.73  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763  10 ALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQNLIDHStQACVGLEINANHLKSVKEGTVKAV 89
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPG-ALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 472255763  90 AEPVHIGRTTIVYHIHIYDEQERLICISRCTLAV 123
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10254 PRK10254
proofreading thioesterase EntH;
3-124 1.44e-29

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 103.91  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   3 TKHTLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVK 82
Cdd:PRK10254  16 SDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSM-AGFLMTRDGQCVVGTELNATHHRPVS 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 472255763  83 EGTVKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAVI 124
Cdd:PRK10254  95 EGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 37-115 7.25e-17

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: 69.59  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   37 FGYLHGGASVALAETAASAGAQNLIDhSTQACVGLEINANHLKSVKEG-TVKAVAEPVHIGRTTIVYHIHIYDEQERLIC 115
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 6-123 3.20e-50

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: 155.20  E-value: 3.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763    6 TLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVKEGT 85
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 472255763   86 VKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAV 123
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-126 1.85e-35

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 118.51  E-value: 1.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   4 KHTLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQNLIDHStQACVGLEINANHLKSVKE 83
Cdd:COG2050   14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPG-RRAVTIELNINFLRPARL 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 472255763  84 G-TVKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAVIKK 126
Cdd:COG2050   93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 10-123 1.19e-32

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: 110.73  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763  10 ALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQNLIDHStQACVGLEINANHLKSVKEGTVKAV 89
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPG-ALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 472255763  90 AEPVHIGRTTIVYHIHIYDEQERLICISRCTLAV 123
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10254 PRK10254
proofreading thioesterase EntH;
3-124 1.44e-29

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 103.91  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   3 TKHTLLEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVK 82
Cdd:PRK10254  16 SDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSM-AGFLMTRDGQCVVGTELNATHHRPVS 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 472255763  83 EGTVKAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAVI 124
Cdd:PRK10254  95 EGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
25-124 3.50e-29

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 102.78  E-value: 3.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763  25 AVMPVDHRTVQPFGYLHGGASVALAETAASAgAQNLIDHSTQACVGLEINANHLKSVKEGTVKAVAEPVHIGRTTIVYHI 104
Cdd:PRK10293  38 ATMPVDSRTKQPFGLLHGGASVVLAESIGSV-AGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQI 116

                         90       100
                 ....*....|....*....|
gi 472255763 105 HIYDEQERLICISRCTLAVI 124
Cdd:PRK10293 117 EIFDEKGRLCCSSRLTTAIL 136
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 37-115 7.25e-17

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: 69.59  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   37 FGYLHGGASVALAETAASAGAQNLIDhSTQACVGLEINANHLKSVKEG-TVKAVAEPVHIGRTTIVYHIHIYDEQERLIC 115
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 8-121 5.84e-16

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 69.32  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763   8 LEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQnlIDHSTQACVGLEINANHLKSVKEGT-V 86
Cdd:PLN02322  13 LHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAH--MASGFKRVAGIQLSINHLKSADLGDlV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 472255763  87 KAVAEPVHIGRTTIVYHIHIY-----DEQER-LICISRCTL 121
Cdd:PLN02322  91 FAEATPVSTGKTIQVWEVKLWkttdkDKANKiLISSSRVTL 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 23-122 2.59e-11

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: 55.94  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763  23 CIAVMPVDHRTVQPFGYLHGGASVALAETAASAGAQNLIDHSTqACVGLEINANHLKSVKEG-TVKAVAEPVHIGRTTIV 101
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL-GAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|.
gi 472255763 102 YHIHIYDEQERLICISRCTLA 122
Cdd:cd03440   80 VEVEVRNEDGKLVATATATFV 100
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 8-124 3.74e-09

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 50.50  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472255763    8 LEALGIEIVENTAERCIAVMPVDHRTVQPFGYLHGGASVALAETAAsAGAQNLIDhstQACVGLEINANHLKSVKEG-TV 86
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAF-AYACNSYG---DAAVAAQCTIDFLRPGRAGeRL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 472255763   87 KAVAEPVHIGRTTIVYHIHIYDEQERLICISRCTLAVI 124
Cdd:TIGR02286  77 EAEAVEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
 
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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