|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
35-281 |
8.39e-112 |
|
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: 323.92 E-value: 8.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 35 EPLDEDLFRGRHYWVPA---KRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSVRS 111
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRqflNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 112 VKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEElldcetlidQYLRDPNLQKRYPVALNRIAAQEVP----IEI 187
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATKYPATLPRFLKHVVPferpFEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 188 KPINPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKVHFMV-SLDHSMWFHTPFR 266
Cdd:TIGR00189 151 RPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAaSLDHSIWFHRPFR 228
|
250
....*....|....*
gi 966966157 267 ADHWMLYECESPWAG 281
Cdd:TIGR00189 229 ADDWLLYKCSSPSAG 243
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
16-281 |
7.64e-89 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 270.44 E-value: 7.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 16 RGDPPRDLRSvLVTTVLNLEPLDEDLFRG------RHYWvpakRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGD 89
Cdd:PLN02868 121 DSDKTPKDCS-LVERILHLEPLEVDIFRGitlpdaPTFG----KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 90 PNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDPNLQ 168
Cdd:PLN02868 196 INLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPRLP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 169 KRYPvalNRIAAQEV---PIEIKPINPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQW 245
Cdd:PLN02868 275 RSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPHRT 350
|
250 260 270
....*....|....*....|....*....|....*.
gi 966966157 246 QHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:PLN02868 351 KGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAH 386
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
30-281 |
1.37e-86 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 259.81 E-value: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 30 TVLNLEPLDEDLFRGR-HYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFS 108
Cdd:COG1946 7 DLLDLERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 109 VRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNLQKRYPValnRIAAQEVPIEIK 188
Cdd:COG1946 87 TRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLIAGVLPL---RFFAFLRPFDIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 189 PINPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTAVLphQWQHKVHFMVSLDHSMWFHTPFRAD 268
Cdd:COG1946 155 PVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALL--SWLGPPLPAASLDHAMWFHRPFRAD 230
|
250
....*....|...
gi 966966157 269 HWMLYECESPWAG 281
Cdd:COG1946 231 DWLLYDADSPSAS 243
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-281 |
3.03e-45 |
|
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: 153.26 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 48 WVPAKRLFGGQIVGQALVAAAKSVSEDVhVHSLHCYFVRAGDPNvPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQAS 127
Cdd:pfam13622 5 WSPGRAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 128 FQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRYPVALNRIAAQEV-PIEIKPINPSPLSQlQRMEPKQ 205
Cdd:pfam13622 83 FGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEAPFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966966157 206 MFWVRARgyigEGDMKMHCCVAAYISDyAFLGTAVLPHQWQHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:pfam13622 149 RLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAG 219
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
40-130 |
2.07e-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: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 40 DLFRGRHYWVP---AKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSVRSVKAVQ 116
Cdd:cd03445 1 DRFRGVSPPVPpgqGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 966966157 117 HGKPIFICQASFQQ 130
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. ... |
35-281 |
8.39e-112 |
|
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: 323.92 E-value: 8.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 35 EPLDEDLFRGRHYWVPA---KRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSVRS 111
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRqflNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 112 VKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEElldcetlidQYLRDPNLQKRYPVALNRIAAQEVP----IEI 187
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASF-QAEKSGIEHQSTMPKVPPPES---------ELPRENQLATKYPATLPRFLKHVVPferpFEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 188 KPINPSPLSQLQRMePKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKVHFMV-SLDHSMWFHTPFR 266
Cdd:TIGR00189 151 RPVNLLNYLGGKED-PPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAaSLDHSIWFHRPFR 228
|
250
....*....|....*
gi 966966157 267 ADHWMLYECESPWAG 281
Cdd:TIGR00189 229 ADDWLLYKCSSPSAG 243
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
16-281 |
7.64e-89 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 270.44 E-value: 7.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 16 RGDPPRDLRSvLVTTVLNLEPLDEDLFRG------RHYWvpakRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGD 89
Cdd:PLN02868 121 DSDKTPKDCS-LVERILHLEPLEVDIFRGitlpdaPTFG----KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 90 PNVPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSpMQHQFS-MPTVPPPEELLDCETLIDQYLRDPNLQ 168
Cdd:PLN02868 196 INLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG-FEHQEStMPHVPPPETLLSREELRERRLTDPRLP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 169 KRYPvalNRIAAQEV---PIEIKPINPSPLSQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQW 245
Cdd:PLN02868 275 RSYR---NKVAAKPFvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGKLSD-DQALHRCVAAYASDLIFLGTSLNPHRT 350
|
250 260 270
....*....|....*....|....*....|....*.
gi 966966157 246 QHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:PLN02868 351 KGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAH 386
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
30-281 |
1.37e-86 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 259.81 E-value: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 30 TVLNLEPLDEDLFRGR-HYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFS 108
Cdd:COG1946 7 DLLDLERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 109 VRSVKAVQHGKPIFICQASFQQAQPSPmQHQFSMPTVPPPEELLDcetlidqyLRDPNLQKRYPValnRIAAQEVPIEIK 188
Cdd:COG1946 87 TRRVTAIQGGRVIFTATASFGVPEEGL-EHQAPMPDVPPPEDLPS--------LPELLIAGVLPL---RFFAFLRPFDIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 189 PINPSPLSQLQRMEPKQMFWVRARGyiGEGDMKMHCCVAAYISDYAFLGTAVLphQWQHKVHFMVSLDHSMWFHTPFRAD 268
Cdd:COG1946 155 PVEGPLPFAPPSGEPRQRVWMRARD--PLPDDPLHAALLAYASDATPPATALL--SWLGPPLPAASLDHAMWFHRPFRAD 230
|
250
....*....|...
gi 966966157 269 HWMLYECESPWAG 281
Cdd:COG1946 231 DWLLYDADSPSAS 243
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
30-286 |
6.32e-67 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 210.38 E-value: 6.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 30 TVLNLEPLDEDLFRGRHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSV 109
Cdd:PRK10526 10 TLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 110 RSVKAVQHGKPIFICQASFqQAQPSPMQHQFSMPTVPPPEELLDcETLIDQylrdpNLQKRYPVALNRIAAQEVPIEIKP 189
Cdd:PRK10526 90 RRVAAIQNGKPIFYMTASF-QAPEAGFEHQKTMPSAPAPDGLPS-ETDIAQ-----SLAHLLPPVLKDKFICDRPLEIRP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 190 IN-PSPLsQLQRMEPKQMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPhqwqHKVHFM------VSLDHSMWFH 262
Cdd:PRK10526 163 VEfHNPL-KGHVAEPVRQVWIRANGSVPD-DLRVHQYLLGYASDLNFLPVALQP----HGIGFLepgmqiATIDHSMWFH 236
|
250 260
....*....|....*....|....*
gi 966966157 263 TPFRADHWMLYECESPWA-GFRIFI 286
Cdd:PRK10526 237 RPFNLNEWLLYSVESTSAsSARGFV 261
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-281 |
3.03e-45 |
|
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: 153.26 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 48 WVPAKRLFGGQIVGQALVAAAKSVSEDVhVHSLHCYFVRAGDPNvPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQAS 127
Cdd:pfam13622 5 WSPGRAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 128 FQQAQPSPMQ-HQFSMPTVPPPEElldcetlidqylrDPNLQKRYPVALNRIAAQEV-PIEIKPINPSPLSQlQRMEPKQ 205
Cdd:pfam13622 83 FGRLRSSEWElTPAAPPPLPPPED-------------CPLAADEAPFPLFRRVPGFLdPFEPRFARGGGPFS-PGGPGRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966966157 206 MFWVRARgyigEGDMKMHCCVAAYISDyAFLGTAVLPHQWQHKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:pfam13622 149 RLWVRLR----DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAG 219
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
40-130 |
2.07e-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: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 40 DLFRGRHYWVP---AKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSVRSVKAVQ 116
Cdd:cd03445 1 DRFRGVSPPVPpgqGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 966966157 117 HGKPIFICQASFQQ 130
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
205-281 |
4.72e-30 |
|
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: 109.26 E-value: 4.72e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966966157 205 QMFWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKVH-FMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsASASLDHAIWFHRPFRADDWLLYEQRSPRAG 77
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
40-129 |
1.38e-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: 94.72 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 40 DLFRGRHYWVP--AKRLFGGQIVGQALVAAAKSVSE-----DVHVHSLHCYFVRAGDPNVPVLYQVERTRTGSSFSVRSV 112
Cdd:cd00556 1 DRFWGRAPGPLpdDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRG 80
|
90
....*....|....*...
gi 966966157 113 KAVQH-GKPIFICQASFQ 129
Cdd:cd00556 81 RAYQRdGKLVASATQSFL 98
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
205-281 |
6.30e-22 |
|
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: 87.78 E-value: 6.30e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966966157 205 QMFWVRARGYIGeGDMKMHCCVAAYISDYAFLGTAVLPHqwqhKVHFMVSLDHSMWFHTPFRADHWMLYECESPWAG 281
Cdd:cd00556 1 DRFWGRAPGPLP-DDRRVFGGQLAAQSDLAALRTVPRPH----GASGFASLDHHIYFHRPGDADEWLLYEVESLRDG 72
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
199-280 |
3.01e-16 |
|
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: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 199 QRMEPKQMfWVRARGYIGEgDMKMHCCVAAYISDYAFLGTAVLPHQWQHKvHFMVSLDHSMWFHTPFRADHWMLYECESP 278
Cdd:pfam02551 26 QVVAHQQS-WVAALGTVPD-DPRLHSCALAYLSDLTLLLTALYPHGFLCD-GIQVSLDHSIYFHRPGDLNKWILYDVESP 102
|
..
gi 966966157 279 WA 280
Cdd:pfam02551 103 SA 104
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
37-122 |
9.25e-06 |
|
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: 44.54 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966966157 37 LDEDLFRGRHYW----VPAKRLFGGQIVG--QALVAAAKSVSEDVHVHS--------LHC-------------------- 82
Cdd:pfam02551 1 VANDLFRGEYPVavrpGELRRTFGGQVVAhqQSWVAALGTVPDDPRLHScalaylsdLTLlltalyphgflcdgiqvsld 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 966966157 83 ---YFVRAGDPNVPVLYQVERTRTGSSFSVRSVK--AVQHGKPIF 122
Cdd:pfam02551 81 hsiYFHRPGDLNKWILYDVESPSASGGRGLRQGRnfSTQSGKLIA 125
|
|
| |
