|
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: 605.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 1 MSQALNNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPDELKSETDIARALAHLLPPQVKEKFLCDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 161 RPVEFHNPMKGHTAEPKRQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLEKGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504643785 241 MNDWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNRG 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
3.18e-131 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 373.06 E-value: 3.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 94 AIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPDELKSETDIarALAHLLPPQvkeKFLCDKPLEIRPVEFHNPMKGHT 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPEL--LIAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 174 AEPKRQVWIRANGTVPEDfRVHQYLLGYASDFNFLPVALQPhgvgFLEKGMQVATIDHSMWFHRPFNMNDWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 504643785 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
2.91e-124 |
|
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: 355.51 E-value: 2.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 92 VAAIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPD-ELKSETDIARALAHLLPPQVKEKFLCDKPLEIRPVEFHNPMK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 171 GHTAEPKRqVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLeKGMQVATIDHSMWFHRPFNMNDWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 504643785 251 STSASSARGFVRGEFYTQDGVLVASTVQEGVMR 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 |
1.73e-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: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 148 VKEKFLCDKPLEIRPVEFHNPMKGHTAePKRQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGvgFLEKGMQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504643785 228 TIDHSMWFHRPFNMNDWLLYSVESTSASSARGFVRGEFY-TQDGVLVASTVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
8.94e-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: 147.01 E-value: 8.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 178 RQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLEKGMqVATIDHSMWFHRPFNMNDWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 504643785 258 RGFVRGEFYTQDGVLVASTVQEGVM 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: 605.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 1 MSQALNNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEV 80
Cdd:PRK10526 1 MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPDELKSETDIARALAHLLPPQVKEKFLCDKPLEI 160
Cdd:PRK10526 81 LRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 161 RPVEFHNPMKGHTAEPKRQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLEKGMQVATIDHSMWFHRPFN 240
Cdd:PRK10526 161 RPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504643785 241 MNDWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNRG 286
Cdd:PRK10526 241 LNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
15-283 |
3.18e-131 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 373.06 E-value: 3.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 15 EKIEEGLFRGQ-SEDLGLRQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARRVA 93
Cdd:COG1946 12 ERLEDGLFRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 94 AIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPDELKSETDIarALAHLLPPQvkeKFLCDKPLEIRPVEFHNPMKGHT 173
Cdd:COG1946 92 AIQGGRVIFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPEL--LIAGVLPLR---FFAFLRPFDIRPVEGPLPFAPPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 174 AEPKRQVWIRANGTVPEDfRVHQYLLGYASDFNFLPVALQPhgvgFLEKGMQVATIDHSMWFHRPFNMNDWLLYSVESTS 253
Cdd:COG1946 167 GEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALLS----WLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPS 241
|
250 260 270
....*....|....*....|....*....|
gi 504643785 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:COG1946 242 ASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
15-283 |
2.91e-124 |
|
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: 355.51 E-value: 2.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 15 EKIEEGLFRGQSEDLGLR---QVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARR 91
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 92 VAAIQNGKPIFYMTASFQAPEPGYEHQKAMPAAPSPD-ELKSETDIARALAHLLPPQVKEKFLCDKPLEIRPVEFHNPMK 170
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPEsELPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 171 GHTAEPKRqVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLeKGMQVATIDHSMWFHRPFNMNDWLLYSVE 250
Cdd:TIGR00189 161 GKEDPPQY-VWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGF-CHSMAASLDHSIWFHRPFRADDWLLYKCS 238
|
250 260 270
....*....|....*....|....*....|...
gi 504643785 251 STSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
Cdd:TIGR00189 239 SPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
15-282 |
1.38e-87 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 266.97 E-value: 1.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 15 EKIEEGLFRG----QSEDLGlrQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSAR 90
Cdd:PLN02868 139 EPLEVDIFRGitlpDAPTFG--KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 91 RVAAIQNGKPIFYMTASFQAPEPGYEHQKA-MPAAPSPDELKSETDI--ARALAHLLPPQVKEKFLCDK----PLEIRPV 163
Cdd:PLN02868 217 RVDAIQKGKVIFTLFASFQKEEQGFEHQEStMPHVPPPETLLSREELreRRLTDPRLPRSYRNKVAAKPfvpwPIEIRFC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 164 EFHNPMKGHTAEPKRQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGvgflEKGMQVA--TIDHSMWFHRPFNM 241
Cdd:PLN02868 297 EPNNSTNQTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHR----TKGLKFAalSLDHSMWFHRPFRA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 504643785 242 NDWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVM 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 |
1.73e-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: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 148 VKEKFLCDKPLEIRPVEFHNPMKGHTAePKRQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGvgFLEKGMQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504643785 228 TIDHSMWFHRPFNMNDWLLYSVESTSASSARGFVRGEFY-TQDGVLVASTVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFsTQSGKLIASVQQEGL 132
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
3.05e-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: 173.67 E-value: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 32 RQVFGGQVVGQALYAAKETVPADRLvHSFHSYFLRPGDSAkPIVYDVEVLRDGNSFSARRVAAIQNGKPIFYMTASFQAP 111
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDPL-HSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 112 EPG--YEHQKAMPAAPSPDELKSETDIAralAHLLPPQVKEKFlcdKPLEIRPVEFHNPMKGHtAEPKRQVWIRANGTVP 189
Cdd:pfam13622 87 RSSewELTPAAPPPLPPPEDCPLAADEA---PFPLFRRVPGFL---DPFEPRFARGGGPFSPG-GPGRVRLWVRLRDGGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 190 edfRVHQYLLGYASDFnFLPVALqPHGVGFLEKGMqVATIDHSMWFHRPFNMNDWLLYSVESTSASSARGFVRGEFYTQD 269
Cdd:pfam13622 160 ---PDPLAALAYLADA-FPPRVL-SLRLDPPASGW-FPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 504643785 270 GVLVASTVQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
8.94e-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: 147.01 E-value: 8.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 178 RQVWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFLEKGMqVATIDHSMWFHRPFNMNDWLLYSVESTSASSA 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASA-SASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 504643785 258 RGFVRGEFYTQDGVLVASTVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
21-109 |
3.74e-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: 140.06 E-value: 3.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 21 LFRGQS---EDLGLRQVFGGQVVGQALYAAKETVPADRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARRVAAIQN 97
Cdd:cd03445 2 RFRGVSppvPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQN 81
|
90
....*....|..
gi 504643785 98 GKPIFYMTASFQ 109
Cdd:cd03445 82 GKVIFTATASFQ 93
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
180-282 |
7.10e-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: 110.90 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 180 VWIRANGTVPEDFRVHQYLLGYASDFNFLPVALQPHGVGFlekgmqVATIDHSMWFHRPFNMNDWLLYSVESTSASSARG 259
Cdd:cd00556 3 FWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASG------FASLDHHIYFHRPGDADEWLLYEVESLRDGRSRA 76
|
90 100
....*....|....*....|...
gi 504643785 260 FVRGEFYTQDGVLVASTVQEGVM 282
Cdd:cd00556 77 LRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
32-109 |
1.37e-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: 92.02 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 32 RQVFGGQVVGQALYAAKETVPA-----DRLVHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARRVAAIQN-GKPIFYMT 105
Cdd:cd00556 15 RRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94
|
....
gi 504643785 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 |
5.55e-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: 61.88 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 17 IEEGLFRGQ---SEDLG-LRQVFGGQVVG--QALYAAKETVPADRLVHSF------------------------------ 60
Cdd:pfam02551 1 VANDLFRGEypvAVRPGeLRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsld 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504643785 61 HS-YFLRPGDSAKPIVYDVE--------VLRDGNSFSarrvaaIQNGKPIFY 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 |
2.33e-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: 50.94 E-value: 2.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504643785 205 FNFLPVALQPHGVGFLEKGMQVATIDHSMWFHRPFNMNDWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGV 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 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643785 34 VFGGQVVGQALYAAKETVPADRL------VHSFHSYFLRPGDSAKPIVYDVEVLRDGNSFSARRVAAI-QNGKPIFYMTA 106
Cdd:cd03440 18 VHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVATATA 97
|
..
gi 504643785 107 SF 108
Cdd:cd03440 98 TF 99
|
|
| |
