|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
1-285 |
1.39e-172 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 478.09 E-value: 1.39e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 1 MSQVLDDLLSLLSLEEIEQGLYRGQSQDLGFRAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVET 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 81 IRDGKSFSTRRVSAIQYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSLEFYQENAHHIPEVIRNKFIREMPIEM 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 161 RPVTFHNPFKPEVIEPVKHIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFMQPNMQVATIDHAMWFHRPFR 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490726174 241 MDDWILYTIDSPSASSGRGLVRGQFFDRQGNLVASTIQEGVMRQR 285
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNH 285
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
17-285 |
3.75e-135 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 383.07 E-value: 3.75e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 17 IEQGLYRGQ-SQDLGFRAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAI 95
Cdd:COG1946 14 LEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 96 QYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSLEFYqeNAHHIPeviRNKFIREMPIEMRPVTFHNPFKPEVIE 175
Cdd:COG1946 94 QGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 176 PVKHIWIKANGDMPDDQRiHNYLLAYASDFEFLPTALQphgvSFMQPNMQVATIDHAMWFHRPFRMDDWILYTIDSPSAS 255
Cdd:COG1946 169 PRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPSAS 243
|
250 260 270
....*....|....*....|....*....|
gi 490726174 256 SGRGLVRGQFFDRQGNLVASTIQEGVMRQR 285
Cdd:COG1946 244 GGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
17-283 |
6.03e-117 |
|
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: 336.64 E-value: 6.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 17 IEQGLYRGQSQDLGFR---AVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVS 93
Cdd:TIGR00189 3 IDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 94 AIQYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSL-EFYQENAHHIPEVIRNKFIREMPIEMRPVTFHNPFkPE 172
Cdd:TIGR00189 83 AVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPREnQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYL-GG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 173 VIEPVKHIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFmQPNMQVATIDHAMWFHRPFRMDDWILYTIDSP 252
Cdd:TIGR00189 162 KEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAG-FCHSMAASLDHSIWFHRPFRADDWLLYKCSSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 490726174 253 SASSGRGLVRGQFFDRQGNLVASTIQEGVMR 283
Cdd:TIGR00189 241 SAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
4.05e-58 |
|
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: 4.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 32 RAVFGGQVMGQALSAAKETLPkGRVVHSLHSYFLRPGDAAkPIVYDVETIRDGKSFSTRRVSAIQYGKPIFYMTASFQ-- 109
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVP-PDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 110 GEEEGLSHQATMPNVPPPEELRssLEFYQENAHHIPEVIRnkFIRemPIEMRPVTFHNPFKPEViEPVKHIWIKANgdmP 189
Cdd:pfam13622 87 RSSEWELTPAAPPPLPPPEDCP--LAADEAPFPLFRRVPG--FLD--PFEPRFARGGGPFSPGG-PGRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 190 DDQRIHNYLLAYASDFefLPTALQPHGVSFMQPNMqVATIDHAMWFHRPFRMDDWILYTIDSPSASSGRGLVRGQFFDRQ 269
Cdd:pfam13622 157 GGEPDPLAALAYLADA--FPPRVLSLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 490726174 270 GNLVASTIQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
179-282 |
7.30e-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: 149.71 E-value: 7.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 179 HIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFmQPNMQVATIDHAMWFHRPFRMDDWILYTIDSPSASSGR 258
Cdd:cd03444 2 RVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPL-FDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80
|
90 100
....*....|....*....|....
gi 490726174 259 GLVRGQFFDRQGNLVASTIQEGVM 282
Cdd:cd03444 81 GLVEGRIFTRDGELVASVAQEGLL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
1-285 |
1.39e-172 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 478.09 E-value: 1.39e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 1 MSQVLDDLLSLLSLEEIEQGLYRGQSQDLGFRAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVET 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 81 IRDGKSFSTRRVSAIQYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSLEFYQENAHHIPEVIRNKFIREMPIEM 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 161 RPVTFHNPFKPEVIEPVKHIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFMQPNMQVATIDHAMWFHRPFR 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490726174 241 MDDWILYTIDSPSASSGRGLVRGQFFDRQGNLVASTIQEGVMRQR 285
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNH 285
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
17-285 |
3.75e-135 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 383.07 E-value: 3.75e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 17 IEQGLYRGQ-SQDLGFRAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAI 95
Cdd:COG1946 14 LEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 96 QYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSLEFYqeNAHHIPeviRNKFIREMPIEMRPVTFHNPFKPEVIE 175
Cdd:COG1946 94 QGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 176 PVKHIWIKANGDMPDDQRiHNYLLAYASDFEFLPTALQphgvSFMQPNMQVATIDHAMWFHRPFRMDDWILYTIDSPSAS 255
Cdd:COG1946 169 PRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPSAS 243
|
250 260 270
....*....|....*....|....*....|
gi 490726174 256 SGRGLVRGQFFDRQGNLVASTIQEGVMRQR 285
Cdd:COG1946 244 GGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
17-283 |
6.03e-117 |
|
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: 336.64 E-value: 6.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 17 IEQGLYRGQSQDLGFR---AVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVS 93
Cdd:TIGR00189 3 IDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 94 AIQYGKPIFYMTASFQGEEEGLSHQATMPNVPPPEELRSSL-EFYQENAHHIPEVIRNKFIREMPIEMRPVTFHNPFkPE 172
Cdd:TIGR00189 83 AVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPREnQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYL-GG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 173 VIEPVKHIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFmQPNMQVATIDHAMWFHRPFRMDDWILYTIDSP 252
Cdd:TIGR00189 162 KEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAG-FCHSMAASLDHSIWFHRPFRADDWLLYKCSSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 490726174 253 SASSGRGLVRGQFFDRQGNLVASTIQEGVMR 283
Cdd:TIGR00189 241 SAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
31-282 |
1.64e-95 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 287.39 E-value: 1.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 31 FRAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAIQYGKPIFYMTASFQG 110
Cdd:PLN02868 157 FGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 111 EEEGLSHQ-ATMPNVPPPEELRSSLEFYQE--NAHHIPEVIRNKFIREM----PIEMRPVTFHNPFKPEVIEPVKHIWIK 183
Cdd:PLN02868 237 EEQGFEHQeSTMPHVPPPETLLSREELRERrlTDPRLPRSYRNKVAAKPfvpwPIEIRFCEPNNSTNQTKSPPRLRYWFR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 184 ANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFMQPnmQVATIDHAMWFHRPFRMDDWILYTIDSPSASSGRGLVRG 263
Cdd:PLN02868 317 AKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKF--AALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATG 394
|
250
....*....|....*....
gi 490726174 264 QFFDRQGNLVASTIQEGVM 282
Cdd:PLN02868 395 HMFNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
4.05e-58 |
|
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: 4.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 32 RAVFGGQVMGQALSAAKETLPkGRVVHSLHSYFLRPGDAAkPIVYDVETIRDGKSFSTRRVSAIQYGKPIFYMTASFQ-- 109
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVP-PDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 110 GEEEGLSHQATMPNVPPPEELRssLEFYQENAHHIPEVIRnkFIRemPIEMRPVTFHNPFKPEViEPVKHIWIKANgdmP 189
Cdd:pfam13622 87 RSSEWELTPAAPPPLPPPEDCP--LAADEAPFPLFRRVPG--FLD--PFEPRFARGGGPFSPGG-PGRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 190 DDQRIHNYLLAYASDFefLPTALQPHGVSFMQPNMqVATIDHAMWFHRPFRMDDWILYTIDSPSASSGRGLVRGQFFDRQ 269
Cdd:pfam13622 157 GGEPDPLAALAYLADA--FPPRVLSLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 490726174 270 GNLVASTIQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
179-282 |
7.30e-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: 149.71 E-value: 7.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 179 HIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFmQPNMQVATIDHAMWFHRPFRMDDWILYTIDSPSASSGR 258
Cdd:cd03444 2 RVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPL-FDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80
|
90 100
....*....|....*....|....
gi 490726174 259 GLVRGQFFDRQGNLVASTIQEGVM 282
Cdd:cd03444 81 GLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
147-281 |
2.14e-44 |
|
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: 147.01 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 147 VIRNKFIREMPIEMRPVTFHNPFKPEVIePVKHIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGvsFMQPNMQV 226
Cdd:pfam02551 1 VANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490726174 227 aTIDHAMWFHRPFRMDDWILYTIDSPSASSGRGLVRGQFFDRQ-GNLVASTIQEGV 281
Cdd:pfam02551 78 -SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFSTQsGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
21-109 |
2.49e-42 |
|
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: 140.45 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 21 LYRGQSQDLGF---RAVFGGQVMGQALSAAKETLPKGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAIQY 97
Cdd:cd03445 2 RFRGVSPPVPPgqgRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81
|
90
....*....|..
gi 490726174 98 GKPIFYMTASFQ 109
Cdd:cd03445 82 GKVIFTATASFQ 93
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
179-282 |
3.16e-32 |
|
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: 114.75 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 179 HIWIKANGDMPDDQRIHNYLLAYASDFEFLPTALQPHGVSFMqpnmqvATIDHAMWFHRPFRMDDWILYTIDSPSASSGR 258
Cdd:cd00556 2 RFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGF------ASLDHHIYFHRPGDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 490726174 259 GLVRGQFFDRQGNLVASTIQEGVM 282
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
32-109 |
1.04e-23 |
|
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: 92.41 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 32 RAVFGGQVMGQALSAAKETLP-----KGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAIQ-YGKPIFYMT 105
Cdd:cd00556 15 RRVFGGQLAAQSDLAALRTVPrphgaSGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQrDGKLVASAT 94
|
....
gi 490726174 106 ASFQ 109
Cdd:cd00556 95 QSFL 98
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
179-281 |
5.41e-08 |
|
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: 49.78 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 179 HIWIKANGDMPDDQRI-HNYLLAYASDfeflpTALQPHGVSFMQPNMQVATIDHAMWFHRPFRMDDWILYTIDSPSASSG 257
Cdd:cd03440 2 VLRLTVTPEDIDGGGIvHGGLLLALAD-----EAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS 76
|
90 100
....*....|....*....|....
gi 490726174 258 RGLVRGQFFDRQGNLVASTIQEGV 281
Cdd:cd03440 77 SVTVEVEVRNEDGKLVATATATFV 100
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
31-103 |
6.82e-08 |
|
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: 50.32 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 31 FRAVFGGQVMG--QALSAAKETLPKGRVVHSL------------------------------HS-YFLRPGDAAKPIVYD 77
Cdd:pfam02551 19 LRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsldHSiYFHRPGDLNKWILYD 98
|
90 100 110
....*....|....*....|....*....|....
gi 490726174 78 VET--------IRDGKSFSTrrvsaiQYGKPIFY 103
Cdd:pfam02551 99 VESpsasggrgLRQGRNFST------QSGKLIAS 126
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
30-108 |
6.99e-06 |
|
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: 44.00 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726174 30 GFRAVFGGQVMGQALSAAKETLP------KGRVVHSLHSYFLRPGDAAKPIVYDVETIRDGKSFSTRRVSAI-QYGKPIF 102
Cdd:cd03440 14 GGGIVHGGLLLALADEAAGAAAArlggrgLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVA 93
|
....*.
gi 490726174 103 YMTASF 108
Cdd:cd03440 94 TATATF 99
|
|
| |
