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Conserved domains on  [gi|491207506|ref|WP_005065839|]
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MULTISPECIES: thioesterase family protein [Acinetobacter]

Protein Classification

thioesterase family protein( domain architecture ID 12150045)

thioesterase family protein similar to Talaromyces wortmannii thioesterase-like protein TwmA, part of the gene cluster that mediates the biosynthesis of wortmanamides A and B, reduced long-chain polyketides amidated with a specific omega-amino acid, 5-aminopentanoic acid (5PA)

CATH:  3.10.129.90

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
18-262 3.72e-48

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: 159.80  E-value: 3.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   18 IPEGWLQGRTVFGGLVAGLLMQKACcnIQDPNKRLLSCSVTFVGPVQQGPAQLTIEILREGKSVTTLETRLWQDGAVQTI 97
Cdd:pfam13622   1 TPPPWSPGRAPHGGYVAALLLRAAE--RTVPPDPLHSLHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQDGRVVVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   98 LVASFGVPRASNIKVRHEPIVPV-----YRQPEELQPIPFARQMPECYQHFDVCWAEGHYPVTGSQYADFGGWSRFNPnk 172
Cdd:pfam13622  79 ATATFGRLRSSEWELTPAAPPPLpppedCPLAADEAPFPLFRRVPGFLDPFEPRFARGGGPFSPGGPGRVRLWVRLRD-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  173 hENRQMTLPDLIVLMDIWPPGVLPMFKQVA---PASSLTWHItYVH--PFQHqlcDWFKYKVVTEYAGEGYSTEYAHLWD 247
Cdd:pfam13622 157 -GGEPDPLAALAYLADAFPPRVLSLRLDPPasgWFPTLDLTV-YFHrrPPPG---EWLLLRAETPVAGDGRGDVEARLWD 231
                         250
                  ....*....|....*
gi 491207506  248 QNDHLIAILRQTVTV 262
Cdd:pfam13622 232 EDGRLVATSRQEVLV 246
 
Name Accession Description Interval E-value
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
18-262 3.72e-48

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: 159.80  E-value: 3.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   18 IPEGWLQGRTVFGGLVAGLLMQKACcnIQDPNKRLLSCSVTFVGPVQQGPAQLTIEILREGKSVTTLETRLWQDGAVQTI 97
Cdd:pfam13622   1 TPPPWSPGRAPHGGYVAALLLRAAE--RTVPPDPLHSLHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQDGRVVVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   98 LVASFGVPRASNIKVRHEPIVPV-----YRQPEELQPIPFARQMPECYQHFDVCWAEGHYPVTGSQYADFGGWSRFNPnk 172
Cdd:pfam13622  79 ATATFGRLRSSEWELTPAAPPPLpppedCPLAADEAPFPLFRRVPGFLDPFEPRFARGGGPFSPGGPGRVRLWVRLRD-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  173 hENRQMTLPDLIVLMDIWPPGVLPMFKQVA---PASSLTWHItYVH--PFQHqlcDWFKYKVVTEYAGEGYSTEYAHLWD 247
Cdd:pfam13622 157 -GGEPDPLAALAYLADAFPPRVLSLRLDPPasgWFPTLDLTV-YFHrrPPPG---EWLLLRAETPVAGDGRGDVEARLWD 231
                         250
                  ....*....|....*
gi 491207506  248 QNDHLIAILRQTVTV 262
Cdd:pfam13622 232 EDGRLVATSRQEVLV 246
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
22-263 5.74e-44

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 149.64  E-value: 5.74e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  22 WLQGRTVFGGLVAGLLMQkACCNIQDPNKRLLSCSVTFVGPVQ-QGPAQLTIEILREGKSVTTLETRLWQDGAVQTILVA 100
Cdd:COG1946   26 DQGLRRVFGGQVAAQALR-AARRTVPEDRPPHSLHAYFLRPGDpDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506 101 SFGVPRASnikVRHEPIVPVYRQPEELQPIP---FARQMPECY----QHFDVCWAEGHYPVTGSQY-ADFGGWSRFNPnk 172
Cdd:COG1946  105 SFGVPEEG---LEHQAPMPDVPPPEDLPSLPellIAGVLPLRFfaflRPFDIRPVEGPLPFAPPSGePRQRVWMRARD-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506 173 henrqmTLPD-------LIVLMDIWPPGV--LPMFKQVAPASSLTWHITYVHPFqhQLCDWFKYKVVTEYAGEGYSTEYA 243
Cdd:COG1946  180 ------PLPDdplhaalLAYASDATPPATalLSWLGPPLPAASLDHAMWFHRPF--RADDWLLYDADSPSASGGRGLERG 251
                        250       260
                 ....*....|....*....|
gi 491207506 244 HLWDQNDHLIAILRQTVTVF 263
Cdd:COG1946  252 RIWDRDGRLVASSRQEGLVR 271
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
19-104 2.80e-15

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 239529 [Multi-domain]  Cd Length: 94  Bit Score: 69.57  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  19 PEGWLQGRTVFGGLVAGLLMQKACcNIQDPNKRLLSCSVTFVGPVQQG-PAQLTIEILREGKSVTTLETRLWQDGAVQTI 97
Cdd:cd03445    9 PVPPGQGRGVFGGQVLAQALVAAA-RTVPDDRVPHSLHSYFLRPGDPDqPIEYEVERLRDGRSFATRRVRAVQNGKVIFT 87

                 ....*..
gi 491207506  98 LVASFGV 104
Cdd:cd03445   88 ATASFQR 94
 
Name Accession Description Interval E-value
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
18-262 3.72e-48

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: 159.80  E-value: 3.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   18 IPEGWLQGRTVFGGLVAGLLMQKACcnIQDPNKRLLSCSVTFVGPVQQGPAQLTIEILREGKSVTTLETRLWQDGAVQTI 97
Cdd:pfam13622   1 TPPPWSPGRAPHGGYVAALLLRAAE--RTVPPDPLHSLHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQDGRVVVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506   98 LVASFGVPRASNIKVRHEPIVPV-----YRQPEELQPIPFARQMPECYQHFDVCWAEGHYPVTGSQYADFGGWSRFNPnk 172
Cdd:pfam13622  79 ATATFGRLRSSEWELTPAAPPPLpppedCPLAADEAPFPLFRRVPGFLDPFEPRFARGGGPFSPGGPGRVRLWVRLRD-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  173 hENRQMTLPDLIVLMDIWPPGVLPMFKQVA---PASSLTWHItYVH--PFQHqlcDWFKYKVVTEYAGEGYSTEYAHLWD 247
Cdd:pfam13622 157 -GGEPDPLAALAYLADAFPPRVLSLRLDPPasgWFPTLDLTV-YFHrrPPPG---EWLLLRAETPVAGDGRGDVEARLWD 231
                         250
                  ....*....|....*
gi 491207506  248 QNDHLIAILRQTVTV 262
Cdd:pfam13622 232 EDGRLVATSRQEVLV 246
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
22-263 5.74e-44

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 149.64  E-value: 5.74e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  22 WLQGRTVFGGLVAGLLMQkACCNIQDPNKRLLSCSVTFVGPVQ-QGPAQLTIEILREGKSVTTLETRLWQDGAVQTILVA 100
Cdd:COG1946   26 DQGLRRVFGGQVAAQALR-AARRTVPEDRPPHSLHAYFLRPGDpDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506 101 SFGVPRASnikVRHEPIVPVYRQPEELQPIP---FARQMPECY----QHFDVCWAEGHYPVTGSQY-ADFGGWSRFNPnk 172
Cdd:COG1946  105 SFGVPEEG---LEHQAPMPDVPPPEDLPSLPellIAGVLPLRFfaflRPFDIRPVEGPLPFAPPSGePRQRVWMRARD-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506 173 henrqmTLPD-------LIVLMDIWPPGV--LPMFKQVAPASSLTWHITYVHPFqhQLCDWFKYKVVTEYAGEGYSTEYA 243
Cdd:COG1946  180 ------PLPDdplhaalLAYASDATPPATalLSWLGPPLPAASLDHAMWFHRPF--RADDWLLYDADSPSASGGRGLERG 251
                        250       260
                 ....*....|....*....|
gi 491207506 244 HLWDQNDHLIAILRQTVTVF 263
Cdd:COG1946  252 RIWDRDGRLVASSRQEGLVR 271
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
19-104 2.80e-15

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 239529 [Multi-domain]  Cd Length: 94  Bit Score: 69.57  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  19 PEGWLQGRTVFGGLVAGLLMQKACcNIQDPNKRLLSCSVTFVGPVQQG-PAQLTIEILREGKSVTTLETRLWQDGAVQTI 97
Cdd:cd03445    9 PVPPGQGRGVFGGQVLAQALVAAA-RTVPDDRVPHSLHSYFLRPGDPDqPIEYEVERLRDGRSFATRRVRAVQNGKVIFT 87

                 ....*..
gi 491207506  98 LVASFGV 104
Cdd:cd03445   88 ATASFQR 94
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
15-104 2.24e-06

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 45.03  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506  15 WIEIPEGWLQGRTVFGGLVAGLLMQKAC----CNIQDPNKRLLSCSVTFVGPVQ-QGPAQLTIEILREGKSVTTLETRLW 89
Cdd:cd00556    4 WGRAPGPLPDDRRVFGGQLAAQSDLAALrtvpRPHGASGFASLDHHIYFHRPGDaDEWLLYEVESLRDGRSRALRRGRAY 83
                         90
                 ....*....|....*.
gi 491207506  90 Q-DGAVQTILVASFGV 104
Cdd:cd00556   84 QrDGKLVASATQSFLV 99
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
165-262 1.33e-04

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 40.02  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207506 165 WSRFNPNKHENRQMTLPDLIVLMDIWPPGVLPMFKQVAPASSLTWHITYVHPFQhqLCDWFKYKVVTEYAGEGYSTEYAH 244
Cdd:cd00556    4 WGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFASLDHHIYFHRPGD--ADEWLLYEVESLRDGRSRALRRGR 81
                         90
                 ....*....|....*...
gi 491207506 245 LWDQNDHLIAILRQTVTV 262
Cdd:cd00556   82 AYQRDGKLVASATQSFLV 99
 
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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