|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
108-402 |
3.51e-133 |
|
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: 383.25 E-value: 3.51e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 108 ERVDKNLYLARHLLKGRNSLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDGKSFCTRL 187
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 188 VKALQDGEAIFTVQISFHrPEADSIVHQLPMPEVPAPDSledlsdTFERIKKNANIPPAALamIGFKQKEIPpaFFRIFS 267
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPES------ELPRENQLATKYPATL--PRFLKHVVP--FERPFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 268 FRPVDIDSYLCLKKDdhtaghghptdaYRSYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKRGFIPSMALTL 347
Cdd:TIGR00189 150 IRPVNLLNYLGGKED------------PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASL 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17558508 348 DHSIWMHTdNFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALIR 402
Cdd:TIGR00189 218 DHSIWFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
101-402 |
1.12e-90 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 274.83 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 101 IDTFLNLERVDKNLYLARhlLKGRNSLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDG 180
Cdd:COG1946 5 LLDLLDLERLEDGLFRGE--ISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 181 KSFCTRLVKALQDGEAIFTVQISFHRPEaDSIVHQLPMPEVPAPDSLEDLSDTFerikkNANIPPAALAmigfkqkeipp 260
Cdd:COG1946 83 RSFSTRRVTAIQGGRVIFTATASFGVPE-EGLEHQAPMPDVPPPEDLPSLPELL-----IAGVLPLRFF----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 261 AFFRIFSFRPVDIDSYLclkkddhTAGHGHPtdayRSYVWIKANENIGDDPrLHLAAAAYISDATMIETALRPHSKRGFi 340
Cdd:COG1946 146 AFLRPFDIRPVEGPLPF-------APPSGEP----RQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLGPPL- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558508 341 psMALTLDHSIWMHTDnFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALIR 402
Cdd:COG1946 213 --PAASLDHAMWFHRP-FRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
100-401 |
1.10e-69 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 225.75 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 100 LIDTFLNLERVDKNLYlarhllKGrNSLP------VVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQ 173
Cdd:PLN02868 131 LVERILHLEPLEVDIF------RG-ITLPdaptfgKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 174 VDRIRDGKSFCTRLVKALQDGEAIFTVQISFHRPEaDSIVHQLP-MPEVPAPDSLEDLSDTFERIKKNANIPpaalamIG 252
Cdd:PLN02868 204 VERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEE-QGFEHQEStMPHVPPPETLLSREELRERRLTDPRLP------RS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 253 FKQKeippAFFRIFSFRPVDIDsyLCLKKDDHTAGHGHPtdayRSYVWIKANENIGDDPRLHLAAAAYISDATMIETALR 332
Cdd:PLN02868 277 YRNK----VAAKPFVPWPIEIR--FCEPNNSTNQTKSPP----RLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLN 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558508 333 PHSKRGfIPSMALTLDHSIWMHTdNFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:PLN02868 347 PHRTKG-LKFAALSLDHSMWFHR-PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
128-401 |
1.17e-48 |
|
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: 165.58 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 128 PVVYGGQVIGQALSAATATVEVGFVpNSLHSYFVQSGNVErPILYQVDRIRDGKSFCTRLVKALQDGEAIFTVQISFHRP 207
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 208 EADSI-VHQLPMPEVPAPDSLedlsdtferikknanipPAALAMIGFKQKEIPPAFFRIFSFRPVDIdsylclkkddhtA 286
Cdd:pfam13622 87 RSSEWeLTPAAPPPLPPPEDC-----------------PLAADEAPFPLFRRVPGFLDPFEPRFARG------------G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 287 GHGHPTDAYRSYVWIKANEnigDDPRLHLAAAAYISDATMieTALRPHSKRGFIPSMALTLDHSIWMHTDnFRVDDWMLY 366
Cdd:pfam13622 138 GPFSPGGPGRVRLWVRLRD---GGEPDPLAALAYLADAFP--PRVLSLRLDPPASGWFPTLDLTVYFHRR-PPPGEWLLL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 17558508 367 ENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:pfam13622 212 RAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
297-401 |
2.19e-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: 239528 [Multi-domain] Cd Length: 104 Bit Score: 147.01 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 297 SYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKRGFIPSMALTLDHSIWMHtDNFRVDDWMLYENHSTIAGGG 376
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFH-RPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 17558508 377 RSLIEGKLWTRDGRLVFSTTQEALI 401
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. ... |
108-402 |
3.51e-133 |
|
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: 383.25 E-value: 3.51e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 108 ERVDKNLYLARHLLKGRNSLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDGKSFCTRL 187
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 188 VKALQDGEAIFTVQISFHrPEADSIVHQLPMPEVPAPDSledlsdTFERIKKNANIPPAALamIGFKQKEIPpaFFRIFS 267
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPES------ELPRENQLATKYPATL--PRFLKHVVP--FERPFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 268 FRPVDIDSYLCLKKDdhtaghghptdaYRSYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKRGFIPSMALTL 347
Cdd:TIGR00189 150 IRPVNLLNYLGGKED------------PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASL 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17558508 348 DHSIWMHTdNFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALIR 402
Cdd:TIGR00189 218 DHSIWFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
101-402 |
1.12e-90 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 274.83 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 101 IDTFLNLERVDKNLYLARhlLKGRNSLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDG 180
Cdd:COG1946 5 LLDLLDLERLEDGLFRGE--ISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 181 KSFCTRLVKALQDGEAIFTVQISFHRPEaDSIVHQLPMPEVPAPDSLEDLSDTFerikkNANIPPAALAmigfkqkeipp 260
Cdd:COG1946 83 RSFSTRRVTAIQGGRVIFTATASFGVPE-EGLEHQAPMPDVPPPEDLPSLPELL-----IAGVLPLRFF----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 261 AFFRIFSFRPVDIDSYLclkkddhTAGHGHPtdayRSYVWIKANENIGDDPrLHLAAAAYISDATMIETALRPHSKRGFi 340
Cdd:COG1946 146 AFLRPFDIRPVEGPLPF-------APPSGEP----RQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLGPPL- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558508 341 psMALTLDHSIWMHTDnFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALIR 402
Cdd:COG1946 213 --PAASLDHAMWFHRP-FRADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
100-401 |
1.10e-69 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 225.75 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 100 LIDTFLNLERVDKNLYlarhllKGrNSLP------VVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQ 173
Cdd:PLN02868 131 LVERILHLEPLEVDIF------RG-ITLPdaptfgKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 174 VDRIRDGKSFCTRLVKALQDGEAIFTVQISFHRPEaDSIVHQLP-MPEVPAPDSLEDLSDTFERIKKNANIPpaalamIG 252
Cdd:PLN02868 204 VERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEE-QGFEHQEStMPHVPPPETLLSREELRERRLTDPRLP------RS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 253 FKQKeippAFFRIFSFRPVDIDsyLCLKKDDHTAGHGHPtdayRSYVWIKANENIGDDPRLHLAAAAYISDATMIETALR 332
Cdd:PLN02868 277 YRNK----VAAKPFVPWPIEIR--FCEPNNSTNQTKSPP----RLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLN 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558508 333 PHSKRGfIPSMALTLDHSIWMHTdNFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:PLN02868 347 PHRTKG-LKFAALSLDHSMWFHR-PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
103-402 |
1.93e-66 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 213.07 E-value: 1.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 103 TFLNLERVDKNLYLARHLLKGrnsLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDGKS 182
Cdd:PRK10526 10 TLLNLEKIEEGLFRGQSEDLG---LRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 183 FCTRLVKALQDGEAIFTVQISFHRPEAdSIVHQLPMPEVPAPDSLEDLSDTFERIKKnaNIPPAAlamigfKQKEIPPaf 262
Cdd:PRK10526 87 FSARRVAAIQNGKPIFYMTASFQAPEA-GFEHQKTMPSAPAPDGLPSETDIAQSLAH--LLPPVL------KDKFICD-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 263 fRIFSFRPVDIdsylclkkddHTAGHGHPTDAYRsYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKrGFI-P 341
Cdd:PRK10526 156 -RPLEIRPVEF----------HNPLKGHVAEPVR-QVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGI-GFLeP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558508 342 SMAL-TLDHSIWMHTDnFRVDDWMLYENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALIR 402
Cdd:PRK10526 223 GMQIaTIDHSMWFHRP-FNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
128-401 |
1.17e-48 |
|
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: 165.58 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 128 PVVYGGQVIGQALSAATATVEVGFVpNSLHSYFVQSGNVErPILYQVDRIRDGKSFCTRLVKALQDGEAIFTVQISFHRP 207
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 208 EADSI-VHQLPMPEVPAPDSLedlsdtferikknanipPAALAMIGFKQKEIPPAFFRIFSFRPVDIdsylclkkddhtA 286
Cdd:pfam13622 87 RSSEWeLTPAAPPPLPPPEDC-----------------PLAADEAPFPLFRRVPGFLDPFEPRFARG------------G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 287 GHGHPTDAYRSYVWIKANEnigDDPRLHLAAAAYISDATMieTALRPHSKRGFIPSMALTLDHSIWMHTDnFRVDDWMLY 366
Cdd:pfam13622 138 GPFSPGGPGRVRLWVRLRD---GGEPDPLAALAYLADAFP--PRVLSLRLDPPASGWFPTLDLTVYFHRR-PPPGEWLLL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 17558508 367 ENHSTIAGGGRSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:pfam13622 212 RAETPVAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
297-401 |
2.19e-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: 239528 [Multi-domain] Cd Length: 104 Bit Score: 147.01 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 297 SYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKRGFIPSMALTLDHSIWMHtDNFRVDDWMLYENHSTIAGGG 376
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFH-RPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 17558508 377 RSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
113-206 |
1.38e-39 |
|
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: 136.60 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 113 NLYLARHLLKGRNSLPVVYGGQVIGQALSAATATVEVGFVPNSLHSYFVQSGNVERPILYQVDRIRDGKSFCTRLVKALQ 192
Cdd:cd03445 1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 17558508 193 DGEAIFTVQISFHR 206
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
297-401 |
6.51e-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: 238311 [Multi-domain] Cd Length: 99 Bit Score: 111.28 E-value: 6.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 297 SYVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKRGFIPsmaltLDHSIWMHtDNFRVDDWMLYENHSTIAGGG 376
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFAS-----LDHHIYFH-RPGDADEWLLYEVESLRDGRS 74
|
90 100
....*....|....*....|....*
gi 17558508 377 RSLIEGKLWTRDGRLVFSTTQEALI 401
Cdd:cd00556 75 RALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
113-206 |
2.73e-21 |
|
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: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 113 NLYLARHLLKGRNSlPVVYGGQVIGQALSAATATVE-----VGFVPNSLHSYFVQSGNVERPILYQVDRIRDGKSFCTRL 187
Cdd:cd00556 1 DRFWGRAPGPLPDD-RRVFGGQLAAQSDLAALRTVPrphgaSGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRR 79
|
90 100
....*....|....*....|
gi 17558508 188 VKALQ-DGEAIFTVQISFHR 206
Cdd:cd00556 80 GRAYQrDGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
298-400 |
1.83e-20 |
|
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: 86.53 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 298 YVWIKANENIGDDPRLHLAAAAYISDATMIETALRPHSKrgFIPSMALTLDHSIWMHTdNFRVDDWMLYENHSTIAGGGR 377
Cdd:pfam02551 32 QSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHGF--LCDGIQVSLDHSIYFHR-PGDLNKWILYDVESPSASGGR 108
|
90 100
....*....|....*....|....
gi 17558508 378 SLIEGKLW-TRDGRLVFSTTQEAL 400
Cdd:pfam02551 109 GLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
305-400 |
9.81e-04 |
|
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: 38.23 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558508 305 ENIGDDPRLHLAAAAYISDATMIETALRPhskrGFIPSMALTLDHSIWMHTDnFRVDDWMLYENHSTIAGGGRSLIEGKL 384
Cdd:cd03440 10 EDIDGGGIVHGGLLLALADEAAGAAAARL----GGRGLGAVTLSLDVRFLRP-VRPGDTLTVEAEVVRVGRSSVTVEVEV 84
|
90
....*....|....*.
gi 17558508 385 WTRDGRLVFSTTQEAL 400
Cdd:cd03440 85 RNEDGKLVATATATFV 100
|
|
| |
