|
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: 590.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 1 MSQALTNLLALLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 81 LRDGNSFSARRVAAVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPAPDALPSETDIARKLAHLLPPQVKEKFLCDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 161 RPVEFHNPLKGHVAEPTRQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2072513100 241 INDWLLYSVESTSASSARGFVRGEFYTQDGTLVASTVQEGVMRNRN 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
2.99e-124 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 355.72 E-value: 2.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 94 AVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPAPDALPSETDIArkLAHLLPPQvkeKFLCDKPLEIRPVEFHNPLKGHV 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 174 AEPTRQVWIRANGAVPEDLRiHQYLLGYASDFNFLPVALQPhgvgFLEPGMQVATIDHSMWFHRPFNINDWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 2072513100 254 ASSARGFVRGEFYTQDGTLVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
6.10e-121 |
|
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: 347.04 E-value: 6.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 92 VAAVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPA-PDALPSETDIARKLAHLLPPQVKEKFLCDKPLEIRPVEFHNPLK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPpESELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 171 GHVAEPTRqVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLePGMQVATIDHSMWFHRPFNINDWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 2072513100 251 STSASSARGFVRGEFYTQDGTLVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
148-281 |
1.97e-53 |
|
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: 170.50 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 148 VKEKFLCDKPLEIRPVEFHNPLKGHVAePTRQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGvgFLEPGMQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2072513100 228 TIDHSMWFHRPFNINDWLLYSVESTSASSARGFVRGEFY-TQDGTLVASTVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
3.21e-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: 148.55 E-value: 3.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 178 RQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLEPGMqVATIDHSMWFHRPFNINDWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 2072513100 258 RGFVRGEFYTQDGTLVASTVQEGVM 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: 590.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 1 MSQALTNLLALLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 81 LRDGNSFSARRVAAVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPAPDALPSETDIARKLAHLLPPQVKEKFLCDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 161 RPVEFHNPLKGHVAEPTRQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2072513100 241 INDWLLYSVESTSASSARGFVRGEFYTQDGTLVASTVQEGVMRNRN 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
2.99e-124 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 355.72 E-value: 2.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 94 AVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPAPDALPSETDIArkLAHLLPPQvkeKFLCDKPLEIRPVEFHNPLKGHV 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 174 AEPTRQVWIRANGAVPEDLRiHQYLLGYASDFNFLPVALQPhgvgFLEPGMQVATIDHSMWFHRPFNINDWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 2072513100 254 ASSARGFVRGEFYTQDGTLVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
6.10e-121 |
|
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: 347.04 E-value: 6.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 92 VAAVQNGKPIFYMTASFQAPEPGYEHQKTMPAAPA-PDALPSETDIARKLAHLLPPQVKEKFLCDKPLEIRPVEFHNPLK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPpESELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 171 GHVAEPTRqVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLePGMQVATIDHSMWFHRPFNINDWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 2072513100 251 STSASSARGFVRGEFYTQDGTLVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
15-282 |
1.32e-78 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 244.24 E-value: 1.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 15 EKIEEGLFRG----QSEDLGlrQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSAR 90
Cdd:PLN02868 139 EPLEVDIFRGitlpDAPTFG--KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 91 RVAAVQNGKPIFYMTASFQAPEPGYEHQK-TMPAAPAPDALPSETDIARKLAH--LLPPQVKEKFLCDK----PLEIRPV 163
Cdd:PLN02868 217 RVDAIQKGKVIFTLFASFQKEEQGFEHQEsTMPHVPPPETLLSREELRERRLTdpRLPRSYRNKVAAKPfvpwPIEIRFC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 164 EFHNPLKGHVAEPTRQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGvgflEPGMQVA--TIDHSMWFHRPFNI 241
Cdd:PLN02868 297 EPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR----TKGLKFAalSLDHSMWFHRPFRA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2072513100 242 NDWLLYSVESTSASSARGFVRGEFYTQDGTLVASTVQEGVM 282
Cdd:PLN02868 373 DDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
148-281 |
1.97e-53 |
|
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: 170.50 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 148 VKEKFLCDKPLEIRPVEFHNPLKGHVAePTRQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGvgFLEPGMQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2072513100 228 TIDHSMWFHRPFNINDWLLYSVESTSASSARGFVRGEFY-TQDGTLVASTVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
3.16e-49 |
|
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: 163.66 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 32 RQVFGGQVVGQALYAAKETVPAERLiHSFHSYFLRPGDSQkPIIYDVEVLRDGNSFSARRVAAVQNGKPIFYMTASFQAP 111
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 112 EPG---YEHQKTMPAAPAPDALPSETDIARKLAHLLPPQVKekflcdkPLEIRPVEFHNPLKGHvAEPTRQVWIRANgav 188
Cdd:pfam13622 87 RSSeweLTPAAPPPLPPPEDCPLAADEAPFPLFRRVPGFLD-------PFEPRFARGGGPFSPG-GPGRVRLWVRLR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 189 PEDLRIHQYLLGYASDFnFLPVALqPHGVGFLEPGMqVATIDHSMWFHRPFNINDWLLYSVESTSASSARGFVRGEFYTQ 268
Cdd:pfam13622 156 DGGEPDPLAALAYLADA-FPPRVL-SLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDE 232
|
250
....*....|....
gi 2072513100 269 DGTLVASTVQEGVM 282
Cdd:pfam13622 233 DGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
3.21e-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: 148.55 E-value: 3.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 178 RQVWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFLEPGMqVATIDHSMWFHRPFNINDWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 2072513100 258 RGFVRGEFYTQDGTLVASTVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
21-109 |
1.88e-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: 138.52 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 21 LFRGQS---EDLGLRQVFGGQVVGQALYAAKETVPAERLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARRVAAVQN 97
Cdd:cd03445 2 RFRGVSppvPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81
|
90
....*....|..
gi 2072513100 98 GKPIFYMTASFQ 109
Cdd:cd03445 82 GKVIFTATASFQ 93
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
180-282 |
6.11e-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: 111.28 E-value: 6.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 180 VWIRANGAVPEDLRIHQYLLGYASDFNFLPVALQPHGVGFlepgmqVATIDHSMWFHRPFNINDWLLYSVESTSASSARG 259
Cdd:cd00556 3 FWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASG------FASLDHHIYFHRPGDADEWLLYEVESLRDGRSRA 76
|
90 100
....*....|....*....|...
gi 2072513100 260 FVRGEFYTQDGTLVASTVQEGVM 282
Cdd:cd00556 77 LRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
32-109 |
2.73e-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: 91.25 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 32 RQVFGGQVVGQALYAAKETVPAE-----RLIHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARRVAAVQN-GKPIFYMT 105
Cdd:cd00556 15 RRVFGGQLAAQSDLAALRTVPRPhgasgFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94
|
....
gi 2072513100 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 |
1.51e-11 |
|
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: 60.72 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 17 IEEGLFRGQ---SEDLG-LRQVFGGQVVG--QALYAAKETVPAERLIHSF------------------------------ 60
Cdd:pfam02551 1 VANDLFRGEypvAVRPGeLRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsld 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2072513100 61 HS-YFLRPGDSQKPIIYDVE--------VLRDGNSFSarrvaaVQNGKPIFY 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 |
5.45e-09 |
|
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: 52.86 E-value: 5.45e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2072513100 205 FNFLPVALQPHGVGFLEPGMQVATIDHSMWFHRPFNINDWLLYSVESTSASSARGFVRGEFYTQDGTLVASTVQEGV 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 |
2.12e-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: 36.68 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072513100 34 VFGGQVVGQALYAAKETVPAERL------IHSFHSYFLRPGDSQKPIIYDVEVLRDGNSFSARRVAA-VQNGKPIFYMTA 106
Cdd:cd03440 18 VHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVrNEDGKLVATATA 97
|
..
gi 2072513100 107 SF 108
Cdd:cd03440 98 TF 99
|
|
| |
