|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
35-309 |
4.10e-134 |
|
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: 381.70 E-value: 4.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 35 EPLDEDLFRGRHYWVPA---KRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRS 111
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRqflNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 112 VKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEElldcetlidQYLRDPNLQKRYPLALNRIAAQEVP----IEI 187
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATKYPATLPRFLKHVVPferpFEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 188 KPVNPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMV-SLDHSMWFHAPFR 266
Cdd:TIGR00189 151 RPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAaSLDHSIWFHRPFR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 34577075 267 ADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIR 309
Cdd:TIGR00189 229 ADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
30-311 |
1.26e-103 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 304.49 E-value: 1.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 30 TVLNLEPLDEDLFRGR-HYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFS 108
Cdd:COG1946 7 DLLDLERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 109 VRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNLQKRYPLalnRIAAQEVPIEIK 188
Cdd:COG1946 87 TRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLIAGVLPL---RFFAFLRPFDIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 189 PVNPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTALLphQWQHKVHFMVSLDHSMWFHAPFRAD 268
Cdd:COG1946 155 PVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALL--SWLGPPLPAASLDHAMWFHRPFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 34577075 269 HWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVK 311
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
27-308 |
4.09e-98 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 295.48 E-value: 4.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 27 LVTTVLNLEPLDEDLFRG------RHYWvpakRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVER 100
Cdd:PLN02868 131 LVERILHLEPLEVDIFRGitlpdaPTFG----KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 101 TRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDPNLQKRYPlalNRIA 179
Cdd:PLN02868 207 IRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPRLPRSYR---NKVA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 180 AQEV---PIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLD 256
Cdd:PLN02868 283 AKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAALSLD 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 34577075 257 HSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:PLN02868 362 HSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-308 |
1.31e-57 |
|
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: 186.00 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 48 WVPAKRLFGGQIVGQALVAAAKSVSEDVhVHSLHCYFVRAGDPKlPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQAS 127
Cdd:pfam13622 5 WSPGRAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 128 FQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRYPLALNRIAAQEV-PIEIKPVNPSPLSQlQRMEPKQ 205
Cdd:pfam13622 83 FGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEAPFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 206 MFWVRARgyigEGDMKMHCCVAAYISDyAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRG 285
Cdd:pfam13622 149 RLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRG 223
|
250 260
....*....|....*....|...
gi 34577075 286 LVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:pfam13622 224 DVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
205-308 |
1.54e-46 |
|
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: 152.79 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 205 QMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVH-FMVSLDHSMWFHAPFRADHWMLYECESPWAGGS 283
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 34577075 284 RGLVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
35-309 |
4.10e-134 |
|
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: 381.70 E-value: 4.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 35 EPLDEDLFRGRHYWVPA---KRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRS 111
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRqflNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 112 VKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEElldcetlidQYLRDPNLQKRYPLALNRIAAQEVP----IEI 187
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATKYPATLPRFLKHVVPferpFEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 188 KPVNPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMV-SLDHSMWFHAPFR 266
Cdd:TIGR00189 151 RPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAaSLDHSIWFHRPFR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 34577075 267 ADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIR 309
Cdd:TIGR00189 229 ADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
30-311 |
1.26e-103 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 304.49 E-value: 1.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 30 TVLNLEPLDEDLFRGR-HYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFS 108
Cdd:COG1946 7 DLLDLERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 109 VRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNLQKRYPLalnRIAAQEVPIEIK 188
Cdd:COG1946 87 TRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLIAGVLPL---RFFAFLRPFDIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 189 PVNPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTALLphQWQHKVHFMVSLDHSMWFHAPFRAD 268
Cdd:COG1946 155 PVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALL--SWLGPPLPAASLDHAMWFHRPFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 34577075 269 HWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVK 311
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
27-308 |
4.09e-98 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 295.48 E-value: 4.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 27 LVTTVLNLEPLDEDLFRG------RHYWvpakRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVER 100
Cdd:PLN02868 131 LVERILHLEPLEVDIFRGitlpdaPTFG----KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 101 TRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDPNLQKRYPlalNRIA 179
Cdd:PLN02868 207 IRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPRLPRSYR---NKVA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 180 AQEV---PIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLD 256
Cdd:PLN02868 283 AKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAALSLD 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 34577075 257 HSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:PLN02868 362 HSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
30-312 |
3.33e-82 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 250.44 E-value: 3.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 30 TVLNLEPLDEDLFRGRHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSV 109
Cdd:PRK10526 10 TLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 110 RSVKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEELLDcETLIDQylrdpNLQKRYPLALNRIAAQEVPIEIKP 189
Cdd:PRK10526 90 RRVAAIQNGKPIFYMTASF-QAPEAGFEHQKTMPSAPAPDGLPS-ETDIAQ-----SLAHLLPPVLKDKFICDRPLEIRP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 190 VN-PSPLsQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPhqwqHKVHFM------VSLDHSMWFH 262
Cdd:PRK10526 163 VEfHNPL-KGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQP----HGIGFLepgmqiATIDHSMWFH 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 34577075 263 APFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKP 312
Cdd:PRK10526 237 RPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-308 |
1.31e-57 |
|
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: 186.00 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 48 WVPAKRLFGGQIVGQALVAAAKSVSEDVhVHSLHCYFVRAGDPKlPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQAS 127
Cdd:pfam13622 5 WSPGRAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 128 FQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRYPLALNRIAAQEV-PIEIKPVNPSPLSQlQRMEPKQ 205
Cdd:pfam13622 83 FGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEAPFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 206 MFWVRARgyigEGDMKMHCCVAAYISDyAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRG 285
Cdd:pfam13622 149 RLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRG 223
|
250 260
....*....|....*....|...
gi 34577075 286 LVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:pfam13622 224 DVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
205-308 |
1.54e-46 |
|
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: 152.79 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 205 QMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKVH-FMVSLDHSMWFHAPFRADHWMLYECESPWAGGS 283
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 34577075 284 RGLVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
40-130 |
4.56e-43 |
|
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: 143.53 E-value: 4.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 40 DLFRGRHYWVP---AKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQ 116
Cdd:cd03445 1 DRFRGVSPPVPpgqGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 34577075 117 HGKPIFICQASFQQ 130
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
205-308 |
2.75e-35 |
|
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: 123.22 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 205 QMFWVRARGYIGeGDMKMHCCVAAYISDYAFLGTALLPHqwqhKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSR 284
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPH----GASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 34577075 285 GLVHGRLWRQDGVLAVTCAQEGVI 308
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
190-307 |
8.53e-25 |
|
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: 96.93 E-value: 8.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 190 VNPSPLSQL---QRMEPKQMfWVRARGYIGEgDMKMHCCVAAYISDYAFLGTALLPHQWQHKvHFMVSLDHSMWFHAPFR 266
Cdd:pfam02551 14 VRPGELRRTfggQVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGFLCD-GIQVSLDHSIYFHRPGD 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 34577075 267 ADHWMLYECESPWAGGSRGLVHGRLWR-QDGVLAVTCAQEGV 307
Cdd:pfam02551 91 LNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
40-129 |
7.16e-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: 93.56 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 40 DLFRGRHYWVP--AKRLFGGQIVGQALVAAAKSVSE-----DVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSV 112
Cdd:cd00556 1 DRFWGRAPGPLpdDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRG 80
|
90
....*....|....*...
gi 34577075 113 KAVQH-GKPIFICQASFQ 129
Cdd:cd00556 81 RAYQRdGKLVASATQSFL 98
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
207-307 |
1.92e-10 |
|
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: 57.10 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 207 FWVRARGYIGEGDMKMHCCVAAYISDYAFLGTALLPHqwqHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGL 286
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG---GRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79
|
90 100
....*....|....*....|.
gi 34577075 287 VHGRLWRQDGVLAVTCAQEGV 307
Cdd:cd03440 80 VEVEVRNEDGKLVATATATFV 100
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
37-122 |
2.42e-05 |
|
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: 43.39 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34577075 37 LDEDLFRGRHYW----VPAKRLFGGQIVG--QALVAAAKSVSEDVHVHS--------LHC-------------------- 82
Cdd:pfam02551 1 VANDLFRGEYPVavrpGELRRTFGGQVVAhqQSWVAALGTVPDDPRLHScalaylsdLTLlltalyphgflcdgiqvsld 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 34577075 83 ---YFVRAGDPKLPVLYQVERTRTGSSFSVRSVK--AVQHGKPIF 122
Cdd:pfam02551 81 hsiYFHRPGDLNKWILYDVESPSASGGRGLRQGRnfSTQSGKLIA 125
|
|
| |
