1C8U,1C8U,1TBU


Conserved Protein Domain Family
Thioesterase_II

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cd00556: Thioesterase_II 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 238311
Aligned: 169 rows
Threshold Bit Score: 38.479
Created: 7-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitedimer interface
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1C8U_A; Ser203, His231, and Glu279 form a trypsin-like catalytic triad

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                            #  ##                        #  #          
1C8U_A      177 RQVWIRANgsvpd---------------dlrvHQYLLGYASDLNFLPVAlqphgigf-lepgiqiATIDHSMWFHRPFnl 240 Escherichia coli
1C8U_A       19 GLFRGQSEdlgl-----------------rqvFGGQVVGQALYAAKETVpe------------erLVHSFHSYFLRPGds 69  Escherichia coli
XP_368100    46 DIERIEELcgegkpf----------whaplasFGGHVYAQSGMAAARVVdaeekagpsderqrrrGVHTVHGYFTTFVfs 115 Magnaporthe gris...
ZP_00136199   8 DPSSVVVPaswgq---------------gratFGGLVVALAYEAMLAVVea------------grPLRSIGVSFVGPLap 60  Pseudomonas aeru...
CAG67294     21 DIPQGWSQgr--------------------tiYGGLVAGLLMHKALSVMnd------------esKNLLSTSITFVGPvn 68  Acinetobacter sp...
ZP_00776079   5 DLIDATNHyinsdeqdraqltipkewaqgrtaYGGLTGALVYSAIRQKVsn------------drVLRSFACNFVGPVmt 72  Pseudoalteromona...
CAI89395     17 DDTNNVANtmqfean----------wcqgrtaFGGLSAALLYQAMRAQVns------------erRLLSLSTNFVGPLla 74  Pseudoalteromona...
ABA75761      5 DLIDAVRRqpevtipa--------ewgqgrasFGGLVAALQFEVMRTKVpt------------drPVRSLAITFVGPVep 64  Pseudomonas fluo...
ZP_00819658  31 DVRNNCEVvipsdw------------gqgratFGGLVAALVFEVMASKVad------------drAMRALQVSFVGPVep 86  Marinobacter aqu...
ABB06163     39 GRWRSRRAdpna----------------ngriFGGQLLGQAMAAALDGVpe------------nrTPTMMQALFLHGAlp 90  Burkholderia sp....
Feature 1                                                     #    
1C8U_A      241 neWLLYSVESTSASSARGFVRGEFYTq----------dGVLVASTVQEGVM 281 Escherichia coli
1C8U_A       70 kkPIIYDVETLRDGNSFSARRVAAIQn-----------GKPIFYMTASFQA 109 Escherichia coli
XP_368100   116 drPIFYEVSPITNAQFSFKTYLVTARqptetssrpprhGWDCPGGNNSYRF 166 Magnaporthe grisea 70-15
ZP_00136199  61 eqPASFSARLLREGKAVSQVQVEVRQg-----------EQVVTLVQASFGV 100 Pseudomonas aeruginosa UCBPP-PA14
CAG67294     69 egRVRLTVEILRQGKSVTTIEARLWQd-----------QAVQTILIASFGQ 108 Acinetobacter sp. ADP1
ZP_00776079  73 eaSFDIEVEILREGRNVTQVIGKAIQd-----------GKVCVMVQAAFGV 112 Pseudoalteromonas atlantica T6c
CAI89395     75 dtPFSLSVEILREGKSSTQVLAKAIQn-----------EQVCVIVQACFAS 114 Pseudoalteromonas haloplanktis TAC125
ABA75761     65 evPVSFEVEVLREGKAVSQVLGRAVQn-----------GQVVTMVQGSFGA 104 Pseudomonas fluorescens PfO-1
ZP_00819658  87 dvPARVEAEVLREGKAVSQVQGRILQn-----------GEPRLVCLASFGG 126 Marinobacter aquaeolei VT8
ABB06163     91 gePLEFETSVLQEGKRFSSRRVSAWQp----------gGRAVLDAQVTCAI 131 Burkholderia sp. 383

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