|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
1-286 |
0e+00 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 600.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 1 MSQALTNLLALLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 81 LRDGNSFSARRVAAIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPEGLPSETDIARKLAHLLPPQAKEKFLSDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 161 RPVEFHNPLKGHVAEPTRQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1709425733 241 INEWLLYSVESTSASSARGFVRGEFYTQDGILVASTVQEGVMRNRN 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
4.93e-132 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 374.98 E-value: 4.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 94 AIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPEGLPSETDIArkLAHLLPPQakeKFLSDKPLEIRPVEFHNPLKGHV 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 174 AEPTRQVWIRANGVVPDDiRVHQSLLGYASDFNFLPVALQPhgvgFLEPGMQVATIDHSMWFHRPFNINEWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 1709425733 254 ASSARGFVRGEFYTQDGILVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
9.16e-127 |
|
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: 361.67 E-value: 9.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 92 VAAIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPE-GLPSETDIARKLAHLLPPQAKEKFLSDKPLEIRPVEFHNPLK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 171 GHVAEPTRqVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLePGMQVATIDHSMWFHRPFNINEWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 1709425733 251 STSASSARGFVRGEFYTQDGILVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
5.58e-53 |
|
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: 172.90 E-value: 5.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 32 RQVFGGQVVGQALYAAKETVPEERLiHSFHSYFLRPGDSQkPIVYDVEVLRDGNSFSARRVAAIQHGKPIFYMTASFQAP 111
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 112 EPG--YEHQKAMPSAPSPEGLPSETDIArklAHLLPPQAKEKFlsdKPLEIRPVEFHNPLKGHvAEPTRQVWIRANgvvP 189
Cdd:pfam13622 87 RSSewELTPAAPPPLPPPEDCPLAADEA---PFPLFRRVPGFL---DPFEPRFARGGGPFSPG-GPGRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 190 DDIRVHQSLLGYASDFnFLPVALqPHGVGFLEPGMqVATIDHSMWFHRPFNINEWLLYSVESTSASSARGFVRGEFYTQD 269
Cdd:pfam13622 157 GGEPDPLAALAYLADA-FPPRVL-SLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 1709425733 270 GILVASTVQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
1.55e-45 |
|
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: 148.94 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 178 RQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLEPGMqVATIDHSMWFHRPFNINEWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 1709425733 258 RGFVRGEFYTQDGILVASTVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
1-286 |
0e+00 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 600.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 1 MSQALTNLLALLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 81 LRDGNSFSARRVAAIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPEGLPSETDIARKLAHLLPPQAKEKFLSDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 161 RPVEFHNPLKGHVAEPTRQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1709425733 241 INEWLLYSVESTSASSARGFVRGEFYTQDGILVASTVQEGVMRNRN 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
4.93e-132 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 374.98 E-value: 4.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 94 AIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPEGLPSETDIArkLAHLLPPQakeKFLSDKPLEIRPVEFHNPLKGHV 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 174 AEPTRQVWIRANGVVPDDiRVHQSLLGYASDFNFLPVALQPhgvgFLEPGMQVATIDHSMWFHRPFNINEWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 1709425733 254 ASSARGFVRGEFYTQDGILVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
9.16e-127 |
|
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: 361.67 E-value: 9.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 92 VAAIQHGKPIFYMTASFQAPEPGYEHQKAMPSAPSPE-GLPSETDIARKLAHLLPPQAKEKFLSDKPLEIRPVEFHNPLK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 171 GHVAEPTRqVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLePGMQVATIDHSMWFHRPFNINEWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 1709425733 251 STSASSARGFVRGEFYTQDGILVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
15-282 |
1.66e-86 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 264.27 E-value: 1.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 15 EKIEEGLFRG----QSEDLGlrQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSAR 90
Cdd:PLN02868 139 EPLEVDIFRGitlpDAPTFG--KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 91 RVAAIQHGKPIFYMTASFQAPEPGYEHQKA-MPSAPSPEGLPSETDIARKLAH--LLPPQAKEKFLSDK----PLEIRPV 163
Cdd:PLN02868 217 RVDAIQKGKVIFTLFASFQKEEQGFEHQEStMPHVPPPETLLSREELRERRLTdpRLPRSYRNKVAAKPfvpwPIEIRFC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 164 EFHNPLKGHVAEPTRQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGvgflEPGMQVA--TIDHSMWFHRPFNI 241
Cdd:PLN02868 297 EPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR----TKGLKFAalSLDHSMWFHRPFRA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1709425733 242 NEWLLYSVESTSASSARGFVRGEFYTQDGILVASTVQEGVM 282
Cdd:PLN02868 373 DDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
5.58e-53 |
|
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: 172.90 E-value: 5.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 32 RQVFGGQVVGQALYAAKETVPEERLiHSFHSYFLRPGDSQkPIVYDVEVLRDGNSFSARRVAAIQHGKPIFYMTASFQAP 111
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 112 EPG--YEHQKAMPSAPSPEGLPSETDIArklAHLLPPQAKEKFlsdKPLEIRPVEFHNPLKGHvAEPTRQVWIRANgvvP 189
Cdd:pfam13622 87 RSSewELTPAAPPPLPPPEDCPLAADEA---PFPLFRRVPGFL---DPFEPRFARGGGPFSPG-GPGRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 190 DDIRVHQSLLGYASDFnFLPVALqPHGVGFLEPGMqVATIDHSMWFHRPFNINEWLLYSVESTSASSARGFVRGEFYTQD 269
Cdd:pfam13622 157 GGEPDPLAALAYLADA-FPPRVL-SLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 1709425733 270 GILVASTVQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
148-281 |
4.18e-52 |
|
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: 167.04 E-value: 4.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 148 AKEKFLSDKPLEIRPVEFHNPLKGHVAePTRQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGvgFLEPGMQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1709425733 228 TIDHSMWFHRPFNINEWLLYSVESTSASSARGFVRGEFY-TQDGILVASTVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
1.55e-45 |
|
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: 148.94 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 178 RQVWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFLEPGMqVATIDHSMWFHRPFNINEWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 1709425733 258 RGFVRGEFYTQDGILVASTVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
21-109 |
2.43e-41 |
|
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: 137.75 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 21 LFRGQS---EDLGLRQVFGGQVVGQALYAAKETVPEERLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARRVAAIQH 97
Cdd:cd03445 2 RFRGVSppvPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81
|
90
....*....|..
gi 1709425733 98 GKPIFYMTASFQ 109
Cdd:cd03445 82 GKVIFTATASFQ 93
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
180-282 |
1.17e-31 |
|
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: 113.21 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 180 VWIRANGVVPDDIRVHQSLLGYASDFNFLPVALQPHGVGFlepgmqVATIDHSMWFHRPFNINEWLLYSVESTSASSARG 259
Cdd:cd00556 3 FWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASG------FASLDHHIYFHRPGDADEWLLYEVESLRDGRSRA 76
|
90 100
....*....|....*....|...
gi 1709425733 260 FVRGEFYTQDGILVASTVQEGVM 282
Cdd:cd00556 77 LRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
32-109 |
6.89e-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: 90.10 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 32 RQVFGGQVVGQALYAAKETVPEE-----RLIHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARRVAAIQH-GKPIFYMT 105
Cdd:cd00556 15 RRVFGGQLAAQSDLAALRTVPRPhgasgFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94
|
....
gi 1709425733 106 ASFQ 109
Cdd:cd00556 95 QSFL 98
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
17-103 |
4.23e-12 |
|
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: 62.26 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 17 IEEGLFRGQ---SEDLG-LRQVFGGQVVG--QALYAAKETVPEERLIHSF------------------------------ 60
Cdd:pfam02551 1 VANDLFRGEypvAVRPGeLRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsld 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1709425733 61 HS-YFLRPGDSQKPIVYDVE--------VLRDGNSFSarrvaaIQHGKPIFY 103
Cdd:pfam02551 81 HSiYFHRPGDLNKWILYDVEspsasggrGLRQGRNFS------TQSGKLIAS 126
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
205-281 |
4.45e-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: 50.17 E-value: 4.45e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709425733 205 FNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFNINEWLLYSVESTSASSARGFVRGEFYTQDGILVASTVQEGV 281
Cdd:cd03440 24 LALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
34-108 |
1.79e-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: 37.07 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709425733 34 VFGGQVVGQALYAAKETVPEERL------IHSFHSYFLRPGDSQKPIVYDVEVLRDGNSFSARRVAAI-QHGKPIFYMTA 106
Cdd:cd03440 18 VHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVATATA 97
|
..
gi 1709425733 107 SF 108
Cdd:cd03440 98 TF 99
|
|
| |
