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Conserved domains on  [gi|283947834|gb|ADB50578|]
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thioesterase superfamily protein [Conexibacter woesei DSM 14684]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-127 4.12e-34

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 115.43  E-value: 4.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   1 MAISPFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNrAVAAEGMVGLGQSNNCSFLRPV 80
Cdd:COG2050   12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAVTIELNINFLRPA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 283947834  81 SAGA-VHATARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAVRPLRP 127
Cdd:COG2050   91 RLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-127 4.12e-34

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 115.43  E-value: 4.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   1 MAISPFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNrAVAAEGMVGLGQSNNCSFLRPV 80
Cdd:COG2050   12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAVTIELNINFLRPA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 283947834  81 SAGA-VHATARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAVRPLRP 127
Cdd:COG2050   91 RLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 9-122 1.53e-29

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: 103.02  E-value: 1.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   9 HLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNRAVAaEGMVGLGQSNNCSFLRPVSAGAVHAT 88
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 283947834  89 ARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 5-122 7.30e-24

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: 88.56  E-value: 7.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834    5 PFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNrAVAAEGMVGLGQSNNCSFLRPVSAGA 84
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY-LCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 283947834   85 VHATARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
9-122 2.99e-17

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 72.33  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   9 HLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGtNRAVAAEGMVGLGQSNNCSFLRPVSAGAVHAT 88
Cdd:PRK10254  23 HLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMA-GFLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 283947834  89 ARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAV 135
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 37-114 1.71e-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: 63.81  E-value: 1.71e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283947834   37 GIVHGGVYAAIAEAIASLGTNRAVAAEGMVgLGQSNNCSFLRPVSAG-AVHATARVRHRGRTSQVWDVELCDDDGRLCA 114
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQQVV-VVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-127 4.12e-34

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 115.43  E-value: 4.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   1 MAISPFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNrAVAAEGMVGLGQSNNCSFLRPV 80
Cdd:COG2050   12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAVTIELNINFLRPA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 283947834  81 SAGA-VHATARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAVRPLRP 127
Cdd:COG2050   91 RLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 9-122 1.53e-29

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: 103.02  E-value: 1.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   9 HLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNRAVAaEGMVGLGQSNNCSFLRPVSAGAVHAT 88
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALP-PGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 283947834  89 ARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 5-122 7.30e-24

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: 88.56  E-value: 7.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834    5 PFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNrAVAAEGMVGLGQSNNCSFLRPVSAGA 84
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY-LCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 283947834   85 VHATARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
9-122 2.99e-17

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 72.33  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   9 HLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGtNRAVAAEGMVGLGQSNNCSFLRPVSAGAVHAT 88
Cdd:PRK10254  23 HLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMA-GFLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 283947834  89 ARVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAV 135
PLN02322 PLN02322
acyl-CoA thioesterase
 2-105 2.59e-15

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 67.78  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834   2 AISPFDHHLGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNRAVAAEGMVGLGQSNNcsFLRPVS 81
Cdd:PLN02322   8 AIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSIN--HLKSAD 85

                         90       100
                 ....*....|....*....|....*
gi 283947834  82 AG-AVHATARVRHRGRTSQVWDVEL 105
Cdd:PLN02322  86 LGdLVFAEATPVSTGKTIQVWEVKL 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 37-114 1.71e-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: 63.81  E-value: 1.71e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283947834   37 GIVHGGVYAAIAEAIASLGTNRAVAAEGMVgLGQSNNCSFLRPVSAG-AVHATARVRHRGRTSQVWDVELCDDDGRLCA 114
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQQVV-VVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 22-121 1.26e-13

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: 62.11  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834  22 VTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNRAVAAEGMVGLGqSNNCSFLRPVSAGA-VHATARVRHRGRTSQV 100
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTL-SLDVRFLRPVRPGDtLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|.
gi 283947834 101 WDVELCDDDGRLCAMARVTVA 121
Cdd:cd03440   80 VEVEVRNEDGKLVATATATFV 100
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
10-122 1.96e-13

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 62.72  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834  10 LGLELLHCDEQLVTARVPVRPQLTQPIGIVHGGVYAAIAEAIASLGTNRAVAAEGMVgLGQSNNCSFLRPVSAGAVHATA 89
Cdd:PRK10293  24 LDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKV-VGLEINANHVRSAREGRVRGVC 102

                         90       100       110
                 ....*....|....*....|....*....|...
gi 283947834  90 RVRHRGRTSQVWDVELCDDDGRLCAMARVTVAV 122
Cdd:PRK10293 103 KPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAI 135
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 22-121 3.91e-06

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 43.35  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834  22 VTARVPVRPQLTQPIGIVHGGVYA-----AIAEAIASLGTN-RAVAAEGMVGLGQSNNCSFLRPVSAG-AVHATARVRHR 94
Cdd:COG0824    6 FETPIRVRFGDTDAMGHVNNANYLryfeeARTEFLRALGLSyAELEEEGIGLVVVEAEIDYLRPARYGdELTVETRVVRL 85

                         90       100
                 ....*....|....*....|....*...
gi 283947834  95 GRTSQVWDVEL-CDDDGRLCAMARVTVA 121
Cdd:COG0824   86 GGSSLTFEYEIfRADDGELLATGETVLV 113
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 25-121 7.39e-06

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 41.82  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834  25 RVPVRPQLTQPIGIVHGGVYA-----AIAEAIASLGTNRAVAAEGmvGLG---QSNNCSFLRPVSAGA-VHATARVRHRG 95
Cdd:cd00586    4 EIRVRFGDTDAAGHVNNARYLryfeeAREEFLRELGLGYDELEEQ--GLGlvvVELEIDYLRPLRLGDrLTVETRVLRLG 81

                         90       100
                 ....*....|....*....|....*.
gi 283947834  96 RTSQVWDVELCDDDGRLCAMARVTVA 121
Cdd:cd00586   82 RKSFTFEQEIFREDGELLATAETVLV 107
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 74-124 5.93e-05

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 40.78  E-value: 5.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 283947834   74 CSFLRPVSAGAVHATARVRHRGRTSQVWDVELcDDDGRLCAMARVTVAVRP 124
Cdd:pfam13622  38 VDFLRPVPPGPVTIRVEVVRDGRSFSTRRVEL-SQDGRVVVTATATFGRLR 87
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
22-132 4.18e-04

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 37.85  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283947834  22 VTARVPVRPQLTQPIGIVHGG-VYAAIAEAIASLGTNRA------VAAEGMvglgqsnncSFLRPVSAG-AVHATARVRH 93
Cdd:COG1607    7 LTLRELVMPEDTNHHGTLFGGwLLSWMDEAAAIAAARHArgrvvtASVDSV---------DFLRPVRVGdIVELYARVVR 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 283947834  94 RGRTS-----QVWDVELCDDDGRLCAMARVT-VAV------RPLRPAAAAT 132
Cdd:COG1607   78 VGRTSmevgvEVWAEDLRTGERRLVTEAYFTfVAVdedgkpRPVPPLIPET 128
PRK11688 PRK11688
thioesterase family protein;
5-54 1.55e-03

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 36.36  E-value: 1.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 283947834   5 PFDHHLGLELLHCDEQLVTARVPVRPQLtqpIG-----IVHGGVYAAIAEAIASL 54
Cdd:PRK11688  22 PFNRLLGLELERLEPDFVELSFKMQPEL---VGniaqsILHGGVIASVLDVAGGL 73
 
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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