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Conserved domains on  [gi|704200684|ref|XP_010142067|]
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PREDICTED: acyl-coenzyme A thioesterase 8, partial [Buceros rhinoceros silvestris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tesB super family cl36601
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 2-121 1.55e-38

acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]


The actual alignment was detected with superfamily member TIGR00189:

Pssm-ID: 272951 [Multi-domain]  Cd Length: 271  Bit Score: 130.17  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684    2 QKFLQNPNLAERYRKQLTRIQAEDVP----IDIKPVNPPDQFCSEpQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYA 77
Cdd:TIGR00189 118 SELPRENQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGK-EDPPQYVWRRARGSLPD-DPRLHQCALAYLSDLT 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 704200684   78 FLGTALLPHRQ--HRVVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:TIGR00189 196 LLPTALNPHNKagFCHSMAASLDHSIWFHRPFRADDWLLYKCSSPS 241
 
Name Accession Description Interval E-value
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 2-121 1.55e-38

acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272951 [Multi-domain]  Cd Length: 271  Bit Score: 130.17  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684    2 QKFLQNPNLAERYRKQLTRIQAEDVP----IDIKPVNPPDQFCSEpQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYA 77
Cdd:TIGR00189 118 SELPRENQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGK-EDPPQYVWRRARGSLPD-DPRLHQCALAYLSDLT 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 704200684   78 FLGTALLPHRQ--HRVVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:TIGR00189 196 LLPTALNPHNKagFCHSMAASLDHSIWFHRPFRADDWLLYKCSSPS 241
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 2-120 1.87e-36

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 127.91  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684   2 QKFLQNPNLAERYRKQLTRIQAEDVPIDIKPVNPPDQFCSEPQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGT 81
Cdd:PLN02868 265 ERRLTDPRLPRSYRNKVAAKPFVPWPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGT 343

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 704200684  82 ALLPHRQHRVVFMA-SLDHAMWFHAPFRADHWMLYECESP 120
Cdd:PLN02868 344 SLNPHRTKGLKFAAlSLDHSMWFHRPFRADDWLLFVIVSP 383
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
27-121 4.10e-33

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 116.52  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684  27 PIDIKPVNPPDQFCSEPQEPKQLFWVRARGDIGETDmkVHCCVAAYISDYAFLGTALLPHRQHRVvFMASLDHAMWFHAP 106
Cdd:COG1946  150 PFDIRPVEGPLPFAPPSGEPRQRVWMRARDPLPDDP--LHAALLAYASDATPPATALLSWLGPPL-PAASLDHAMWFHRP 226

                         90
                 ....*....|....*
gi 704200684 107 FRADHWMLYECESPW 121
Cdd:COG1946  227 FRADDWLLYDADSPS 241
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 48-121 8.33e-31

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: 239528 [Multi-domain]  Cd Length: 104  Bit Score: 105.41  E-value: 8.33e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704200684  48 QLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHR--QHRVVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:cd03444    1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGlpLFDASASASLDHAIWFHRPFRADDWLLYEQRSPR 75
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 51-120 4.95e-18

Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this domain are found in a number of acyl-CoA thioesterases.


Pssm-ID: 396894  Cd Length: 132  Bit Score: 73.82  E-value: 4.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684   51 WVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHRQHRVVFMASLDHAMWFHAPFRADHWMLYECESP 120
Cdd:pfam02551  34 WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQVSLDHSIYFHRPGDLNKWILYDVESP 102
 
Name Accession Description Interval E-value
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 2-121 1.55e-38

acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272951 [Multi-domain]  Cd Length: 271  Bit Score: 130.17  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684    2 QKFLQNPNLAERYRKQLTRIQAEDVP----IDIKPVNPPDQFCSEpQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYA 77
Cdd:TIGR00189 118 SELPRENQLATKYPATLPRFLKHVVPferpFEIRPVNLLNYLGGK-EDPPQYVWRRARGSLPD-DPRLHQCALAYLSDLT 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 704200684   78 FLGTALLPHRQ--HRVVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:TIGR00189 196 LLPTALNPHNKagFCHSMAASLDHSIWFHRPFRADDWLLYKCSSPS 241
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 2-120 1.87e-36

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 127.91  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684   2 QKFLQNPNLAERYRKQLTRIQAEDVPIDIKPVNPPDQFCSEPQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGT 81
Cdd:PLN02868 265 ERRLTDPRLPRSYRNKVAAKPFVPWPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGT 343

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 704200684  82 ALLPHRQHRVVFMA-SLDHAMWFHAPFRADHWMLYECESP 120
Cdd:PLN02868 344 SLNPHRTKGLKFAAlSLDHSMWFHRPFRADDWLLFVIVSP 383
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
27-121 4.10e-33

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 116.52  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684  27 PIDIKPVNPPDQFCSEPQEPKQLFWVRARGDIGETDmkVHCCVAAYISDYAFLGTALLPHRQHRVvFMASLDHAMWFHAP 106
Cdd:COG1946  150 PFDIRPVEGPLPFAPPSGEPRQRVWMRARDPLPDDP--LHAALLAYASDATPPATALLSWLGPPL-PAASLDHAMWFHRP 226

                         90
                 ....*....|....*
gi 704200684 107 FRADHWMLYECESPW 121
Cdd:COG1946  227 FRADDWLLYDADSPS 241
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 48-121 8.33e-31

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: 239528 [Multi-domain]  Cd Length: 104  Bit Score: 105.41  E-value: 8.33e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704200684  48 QLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHR--QHRVVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:cd03444    1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGlpLFDASASASLDHAIWFHRPFRADDWLLYEQRSPR 75
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 48-121 4.47e-24

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: 88.17  E-value: 4.47e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704200684  48 QLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHRQhrvVFMASLDHAMWFHAPFRADHWMLYECESPW 121
Cdd:cd00556    1 DRFWGRAPGPLPD-DRRVFGGQLAAQSDLAALRTVPRPHGA---SGFASLDHHIYFHRPGDADEWLLYEVESLR 70
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 10-120 8.35e-21

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 84.42  E-value: 8.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684  10 LAERYRKQLTRiqaeDVPIDIKPVNPPDQFCSEPQEPKQLFWVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHRQ- 88
Cdd:PRK10526 144 LPPVLKDKFIC----DRPLEIRPVEFHNPLKGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQPHGIg 218

                         90       100       110
                 ....*....|....*....|....*....|....
gi 704200684  89 --HRVVFMASLDHAMWFHAPFRADHWMLYECESP 120
Cdd:PRK10526 219 flEPGMQIATIDHSMWFHRPFNLNEWLLYSVEST 252
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 51-120 4.95e-18

Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this domain are found in a number of acyl-CoA thioesterases.


Pssm-ID: 396894  Cd Length: 132  Bit Score: 73.82  E-value: 4.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684   51 WVRARGDIGEtDMKVHCCVAAYISDYAFLGTALLPHRQHRVVFMASLDHAMWFHAPFRADHWMLYECESP 120
Cdd:pfam02551  34 WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQVSLDHSIYFHRPGDLNKWILYDVESP 102
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 27-121 3.35e-13

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: 63.50  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704200684   27 PIDIKPVnPPDQFCSEPQEPKQLFWVRARgdigETDMKVHCCVAAYISDYAFLGTALLPHRQHRVVFMASLDHAMWFHAP 106
Cdd:pfam13622 128 PFEPRFA-RGGGPFSPGGPGRVRLWVRLR----DGGEPDPLAALAYLADAFPPRVLSLRLDPPASGWFPTLDLTVYFHRR 202

                          90
                  ....*....|....*
gi 704200684  107 FRADHWMLYECESPW 121
Cdd:pfam13622 203 PPPGEWLLLRAETPV 217
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 50-122 6.95e-03

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: 33.60  E-value: 6.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704200684  50 FWVRARGDIGETDMKVHCCVAAYISDYAFLGTALLPHRQHRVVFMASLDhaMWFHAPFRADHWMLYECESPWT 122
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLD--VRFLRPVRPGDTLTVEAEVVRV 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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