|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
40-323 |
3.08e-139 |
|
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: 394.80 E-value: 3.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 40 QRIDTNLYIARHLLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRV 119
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 120 VKAVQDGEAIFSCQISFhHKEPDAIKHSSKMPEVTPPEQllpareaalEVLRTKEVDE-VTAGVIQHFLKEIPdaFERVF 198
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATkYPATLPRFLKHVVP--FERPF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 199 DVRPVNPAKYL-LKEDtePMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRNGFIPSMSFSLDHCIWMHEN 277
Cdd:TIGR00189 149 EIRPVNLLNYLgGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSIWFHRP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71988741 278 eFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEALVR 323
Cdd:TIGR00189 227 -FRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
33-325 |
9.71e-90 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 269.44 E-value: 9.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 33 IDTFLNLQRIDTNLYIARhlLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDG 112
Cdd:COG1946 5 LLDLLDLERLEDGLFRGE--ISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 113 RSFCTRVVKAVQDGEAIFSCQISFHHKEPDaIKHSSKMPEVTPPEQLLPAREAAlevlrtkevdevtagvIQHFLKEIPD 192
Cdd:COG1946 83 RSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSLPELL----------------IAGVLPLRFF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 193 AFERVFDVRPVNPAKYLLKEDTEPMSMIWIRARENLGDDhRLHQCVAAYLTDLSMLTTAVRPHiRNGFIPsMSfSLDHCI 272
Cdd:COG1946 146 AFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLSW-LGPPLP-AA-SLDHAM 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71988741 273 WMHEnEFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEALVRAP 325
Cdd:COG1946 222 WFHR-PFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
32-321 |
5.24e-75 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.54 E-value: 5.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 32 LIDTFLNLQRIDTNLYiarhllKGRHSYNA-----VYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMI 106
Cdd:PLN02868 131 LVERILHLEPLEVDIF------RGITLPDAptfgkVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 107 DRIRDGRSFCTRVVKAVQDGEAIFSCQISFHHKEPDAIKHSSKMPEVTPPEQLLPaREAALEVLRT------KEVDEVTA 180
Cdd:PLN02868 205 ERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQESTMPHVPPPETLLS-REELRERRLTdprlprSYRNKVAA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 181 GviqhflKEIPDAfervFDVRPVNPAKYLLKEDTEPMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRNGf 260
Cdd:PLN02868 284 K------PFVPWP----IEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKG- 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988741 261 IPSMSFSLDHCIWMHEnEFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEAL 321
Cdd:PLN02868 353 LKFAALSLDHSMWFHR-PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
61-322 |
5.16e-46 |
|
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: 156.34 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 61 AVYGGQVVGQSLAAAAATVEDCFIpHSLHSYFIKTGSVDkPILYMIDRIRDGRSFCTRVVKAVQDGEAIFSCQISFHHKE 140
Cdd:pfam13622 10 APHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 141 PDAIK-HSSKMPEVTPPEQLLPAREAALEVLRTKevdevtagviqhflkeiPDAFERVFDVRPVNPAkYLLKEDTEPMSM 219
Cdd:pfam13622 88 SSEWElTPAAPPPLPPPEDCPLAADEAPFPLFRR-----------------VPGFLDPFEPRFARGG-GPFSPGGPGRVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 220 IWIRAREnlgDDHRLHQCVAAYLTDlsMLTTAVRPHIRNGFIPSMSFSLDHCIWMHENEFRiDDWMLYETISSKAGGSRA 299
Cdd:pfam13622 150 LWVRLRD---GGEPDPLAALAYLAD--AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPP-GEWLLLRAETPVAGDGRG 223
|
250 260
....*....|....*....|...
gi 71988741 300 FIEGRLWSRDGRLIISTAQEALV 322
Cdd:pfam13622 224 DVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
45-138 |
1.33e-44 |
|
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: 147.38 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 45 NLYIARHLLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRVVKAVQ 124
Cdd:cd03445 1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 71988741 125 DGEAIFSCQISFHH 138
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
40-323 |
3.08e-139 |
|
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: 394.80 E-value: 3.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 40 QRIDTNLYIARHLLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRV 119
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 120 VKAVQDGEAIFSCQISFhHKEPDAIKHSSKMPEVTPPEQllpareaalEVLRTKEVDE-VTAGVIQHFLKEIPdaFERVF 198
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATkYPATLPRFLKHVVP--FERPF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 199 DVRPVNPAKYL-LKEDtePMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRNGFIPSMSFSLDHCIWMHEN 277
Cdd:TIGR00189 149 EIRPVNLLNYLgGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSIWFHRP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 71988741 278 eFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEALVR 323
Cdd:TIGR00189 227 -FRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
33-325 |
9.71e-90 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 269.44 E-value: 9.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 33 IDTFLNLQRIDTNLYIARhlLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDG 112
Cdd:COG1946 5 LLDLLDLERLEDGLFRGE--ISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 113 RSFCTRVVKAVQDGEAIFSCQISFHHKEPDaIKHSSKMPEVTPPEQLLPAREAAlevlrtkevdevtagvIQHFLKEIPD 192
Cdd:COG1946 83 RSFSTRRVTAIQGGRVIFTATASFGVPEEG-LEHQAPMPDVPPPEDLPSLPELL----------------IAGVLPLRFF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 193 AFERVFDVRPVNPAKYLLKEDTEPMSMIWIRARENLGDDhRLHQCVAAYLTDLSMLTTAVRPHiRNGFIPsMSfSLDHCI 272
Cdd:COG1946 146 AFLRPFDIRPVEGPLPFAPPSGEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLSW-LGPPLP-AA-SLDHAM 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 71988741 273 WMHEnEFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEALVRAP 325
Cdd:COG1946 222 WFHR-PFRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
32-321 |
5.24e-75 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 236.54 E-value: 5.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 32 LIDTFLNLQRIDTNLYiarhllKGRHSYNA-----VYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMI 106
Cdd:PLN02868 131 LVERILHLEPLEVDIF------RGITLPDAptfgkVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 107 DRIRDGRSFCTRVVKAVQDGEAIFSCQISFHHKEPDAIKHSSKMPEVTPPEQLLPaREAALEVLRT------KEVDEVTA 180
Cdd:PLN02868 205 ERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQESTMPHVPPPETLLS-REELRERRLTdprlprSYRNKVAA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 181 GviqhflKEIPDAfervFDVRPVNPAKYLLKEDTEPMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRNGf 260
Cdd:PLN02868 284 K------PFVPWP----IEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKG- 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988741 261 IPSMSFSLDHCIWMHEnEFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEAL 321
Cdd:PLN02868 353 LKFAALSLDHSMWFHR-PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
35-323 |
1.85e-65 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 207.68 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 35 TFLNLQRIDTNLYIARHLLKGrhsYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDGRS 114
Cdd:PRK10526 10 TLLNLEKIEEGLFRGQSEDLG---LRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 115 FCTRVVKAVQDGEAIFSCQISFHHKEPdAIKHSSKMPEVTPPEQLLPAREAALEvlrtkevdevtagvIQHFLKE-IPDA 193
Cdd:PRK10526 87 FSARRVAAIQNGKPIFYMTASFQAPEA-GFEHQKTMPSAPAPDGLPSETDIAQS--------------LAHLLPPvLKDK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 194 F--ERVFDVRPV---NPAKyllKEDTEPMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRnGFI-PSMSF- 266
Cdd:PRK10526 152 FicDRPLEIRPVefhNPLK---GHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGI-GFLePGMQIa 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71988741 267 SLDHCIWMHEnEFRIDDWMLYETISSKAGGSRAFIEGRLWSRDGRLIISTAQEALVR 323
Cdd:PRK10526 228 TIDHSMWFHR-PFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
61-322 |
5.16e-46 |
|
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: 156.34 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 61 AVYGGQVVGQSLAAAAATVEDCFIpHSLHSYFIKTGSVDkPILYMIDRIRDGRSFCTRVVKAVQDGEAIFSCQISFHHKE 140
Cdd:pfam13622 10 APHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 141 PDAIK-HSSKMPEVTPPEQLLPAREAALEVLRTKevdevtagviqhflkeiPDAFERVFDVRPVNPAkYLLKEDTEPMSM 219
Cdd:pfam13622 88 SSEWElTPAAPPPLPPPEDCPLAADEAPFPLFRR-----------------VPGFLDPFEPRFARGG-GPFSPGGPGRVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 220 IWIRAREnlgDDHRLHQCVAAYLTDlsMLTTAVRPHIRNGFIPSMSFSLDHCIWMHENEFRiDDWMLYETISSKAGGSRA 299
Cdd:pfam13622 150 LWVRLRD---GGEPDPLAALAYLAD--AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPP-GEWLLLRAETPVAGDGRG 223
|
250 260
....*....|....*....|...
gi 71988741 300 FIEGRLWSRDGRLIISTAQEALV 322
Cdd:pfam13622 224 DVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
45-138 |
1.33e-44 |
|
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: 147.38 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 45 NLYIARHLLKGRHSYNAVYGGQVVGQSLAAAAATVEDCFIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRVVKAVQ 124
Cdd:cd03445 1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 71988741 125 DGEAIFSCQISFHH 138
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
218-322 |
1.43e-44 |
|
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: 147.78 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 218 SMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRNGFIPSMSFSLDHCIWMHENeFRIDDWMLYETISSKAGGS 297
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHRP-FRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 71988741 298 RAFIEGRLWSRDGRLIISTAQEALV 322
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
218-322 |
4.64e-29 |
|
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: 107.43 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 218 SMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHIRngfipSMSFSLDHCIWMHENeFRIDDWMLYETISSKAGGS 297
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGA-----SGFASLDHHIYFHRP-GDADEWLLYEVESLRDGRS 74
|
90 100
....*....|....*....|....*
gi 71988741 298 RAFIEGRLWSRDGRLIISTAQEALV 322
Cdd:cd00556 75 RALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
45-137 |
1.67e-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: 95.49 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 45 NLYIARHLLKGRHSYnAVYGGQVVGQSLAAAAATVEDC-----FIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRV 119
Cdd:cd00556 1 DRFWGRAPGPLPDDR-RVFGGQLAAQSDLAALRTVPRPhgasgFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRR 79
|
90
....*....|....*....
gi 71988741 120 VKAVQ-DGEAIFSCQISFH 137
Cdd:cd00556 80 GRAYQrDGKLVASATQSFL 98
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
195-321 |
4.72e-23 |
|
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: 92.69 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 195 ERVFDVRPvNPAKYLLKEDTEPMSMIWIRARENLGDDHRLHQCVAAYLTDLSMLTTAVRPHirNGFIPSMSFSLDHCIWM 274
Cdd:pfam02551 9 EYPVAVRP-GELRRTFGGQVVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPH--GFLCDGIQVSLDHSIYF 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71988741 275 HeNEFRIDDWMLYETISSKAGGSRAFIEGRLWS-RDGRLIISTAQEAL 321
Cdd:pfam02551 86 H-RPGDLNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
220-321 |
4.23e-05 |
|
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: 41.69 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 220 IWIRARENLGDDHR-LHQCVAAYLTDLSMLTTAVRPHIRNGFIPSMSFSLDHciwmhENEFRIDDWMLYETISSKAGGSR 298
Cdd:cd03440 3 LRLTVTPEDIDGGGiVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRF-----LRPVRPGDTLTVEAEVVRVGRSS 77
|
90 100
....*....|....*....|...
gi 71988741 299 AFIEGRLWSRDGRLIISTAQEAL 321
Cdd:cd03440 78 VTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
59-136 |
9.70e-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: 35.14 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988741 59 YNAVYGGQVVGQSLAAAAATVEDC------FIPHSLHSYFIKTGSVDKPILYMIDRIRDGRSFCTRVVKA-VQDGEAIFS 131
Cdd:cd03440 15 GGIVHGGLLLALADEAAGAAAARLggrglgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVrNEDGKLVAT 94
|
....*
gi 71988741 132 CQISF 136
Cdd:cd03440 95 ATATF 99
|
|
| |
