NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|727438034|ref|XP_010500355|]
View 

PREDICTED: 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1 [Camelina sativa]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 3-156 3.71e-101

acyl-CoA thioesterase


:

Pssm-ID: 177956  Cd Length: 154  Bit Score: 286.96  E-value: 3.71e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034   3 SASSKTKAVDPALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727438034  83 LKSADLGDLVFAEASPVTKGRTIQVWEVKLWKTTEKDKLNKILISSSRVTLICNLPIPDNAKDAADALKMVAKL 156
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 3-156 3.71e-101

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 286.96  E-value: 3.71e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034   3 SASSKTKAVDPALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727438034  83 LKSADLGDLVFAEASPVTKGRTIQVWEVKLWKTTEKDKLNKILISSSRVTLICNLPIPDNAKDAADALKMVAKL 156
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-135 3.17e-26

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 96.17  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  12 DPALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKRVA-GIQLSINHLKSADLGD 90
Cdd:COG2050   15 NPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAvTIELNINFLRPARLGD 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 727438034  91 LVFAEASPVTKGRTIQVWEVKLWKTTEKdklnkiLISSSRVTLIC 135
Cdd:COG2050   95 RLTAEARVVRRGRRLAVVEVEVTDEDGK------LVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 19-134 5.30e-26

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: 94.93  E-value: 5.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  19 GFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASG-FKRVAGIQLSINHLKSADLGDLVfAEAS 97
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGDLT-ARAR 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 727438034  98 PVTKGRTIQVWEVKLWKTTEKdklnkiLISSSRVTLI 134
Cdd:cd03443   82 VVKLGRRLAVVEVEVTDEDGK------LVATARGTFA 112
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 13-133 4.72e-16

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: 69.68  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034   13 PALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASM-GAHMASGFKRVAGIQLSINHLKSADLGDL 91
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAaGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 727438034   92 VfAEASPVTKGRTIQVWEVKLwkTTEKDKlnkiLISSSRVTL 133
Cdd:TIGR00369  81 R-AIAQVVHLGRQTGVAEIEI--VDEQGR----LCALSRGTT 115
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-114 2.21e-14

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: 64.20  E-value: 2.21e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727438034   44 FKVLHGGVSALIAESLASMGAHMASGFKR-VAGIQLSINHLKSADLGDLVFAEASPVTKGRTIQVWEVKLWK 114
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 3-156 3.71e-101

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 286.96  E-value: 3.71e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034   3 SASSKTKAVDPALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKRVAGIQLSINH 82
Cdd:PLN02322   1 SASSNTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727438034  83 LKSADLGDLVFAEASPVTKGRTIQVWEVKLWKTTEKDKLNKILISSSRVTLICNLPIPDNAKDAADALKMVAKL 156
Cdd:PLN02322  81 LKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-135 3.17e-26

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 96.17  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  12 DPALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKRVA-GIQLSINHLKSADLGD 90
Cdd:COG2050   15 NPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAvTIELNINFLRPARLGD 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 727438034  91 LVFAEASPVTKGRTIQVWEVKLWKTTEKdklnkiLISSSRVTLIC 135
Cdd:COG2050   95 RLTAEARVVRRGRRLAVVEVEVTDEDGK------LVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 19-134 5.30e-26

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: 94.93  E-value: 5.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  19 GFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASG-FKRVAGIQLSINHLKSADLGDLVfAEAS 97
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGDLT-ARAR 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 727438034  98 PVTKGRTIQVWEVKLWKTTEKdklnkiLISSSRVTLI 134
Cdd:cd03443   82 VVKLGRRLAVVEVEVTDEDGK------LVATARGTFA 112
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 13-133 4.72e-16

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: 69.68  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034   13 PALHMFGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASM-GAHMASGFKRVAGIQLSINHLKSADLGDL 91
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAaGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 727438034   92 VfAEASPVTKGRTIQVWEVKLwkTTEKDKlnkiLISSSRVTL 133
Cdd:TIGR00369  81 R-AIAQVVHLGRQTGVAEIEI--VDEQGR----LCALSRGTT 115
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-114 2.21e-14

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: 64.20  E-value: 2.21e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727438034   44 FKVLHGGVSALIAESLASMGAHMASGFKR-VAGIQLSINHLKSADLGDLVFAEASPVTKGRTIQVWEVKLWK 114
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
16-132 7.68e-10

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 53.86  E-value: 7.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  16 HMFGF---EFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMAS-GFKRVAGIQLSINHLKSADLGDl 91
Cdd:PRK10293  19 NMVGLldiRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTeGEQKVVGLEINANHVRSAREGR- 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 727438034  92 VFAEASPVTKGRTIQVWEVKLWKTTEKdklnkiLISSSRVT 132
Cdd:PRK10293  98 VRGVCKPLHLGSRHQVWQIEIFDEKGR------LCCSSRLT 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-134 1.02e-09

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: 52.48  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  30 ITGHLPVSPNCCQAFKVLHGGVSALIAESLASMGAHMASGFKR-VAGIQLSINHLKSADLGDLVFAEASPVTKGRTIQVW 108
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|....*.
gi 727438034 109 EVKLWKTTEKdklnkiLISSSRVTLI 134
Cdd:cd03440   81 EVEVRNEDGK------LVATATATFV 100
PRK10254 PRK10254
proofreading thioesterase EntH;
18-110 4.00e-09

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 51.91  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727438034  18 FGFEFDELSPTRITGHLPVSPNCCQAFKVLHGGVSALIAESLASM-GAHMASGFKRVAGIQLSINHLKSADLGDlVFAEA 96
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMaGFLMTRDGQCVVGTELNATHHRPVSEGK-VRGVC 102

                         90
                 ....*....|....
gi 727438034  97 SPVTKGRTIQVWEV 110
Cdd:PRK10254 103 QPLHLGRQNQSWEI 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH