|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
22-283 |
4.57e-151 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 423.78 E-value: 4.57e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQSENLGLPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNGRPI 101
Cdd:PRK10526 22 FRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 102 FYLTASYHGDAPGFEHQISMPDIPGPENFASETELASHIAEFLPEKLRKTFCGEKPIEMRPVTVVNPLKPKKTEAKQYLW 181
Cdd:PRK10526 102 FYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVAEPVRQVW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 182 VRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLV 261
Cdd:PRK10526 182 IRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFV 261
|
250 260
....*....|....*....|..
gi 656278386 262 RGEIFNQKGELVATAVQEGVMR 283
Cdd:PRK10526 262 RGEFYTQDGVLVASTVQEGVMR 283
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
22-283 |
8.41e-128 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 364.20 E-value: 8.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQ-SENLGLPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNGRP 100
Cdd:COG1946 19 FRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 101 IFYLTASYHGDAPGFEHQISMPDIPGPENFASETELAshIAEFLPeklRKTFCGEKPIEMRPVTVVNPLKPKKTEAKQYL 180
Cdd:COG1946 99 IFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGEPRQRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 181 WVRANGAMPDNQLiHQYLLAYASDWGFLVTALHphevSIMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGL 260
Cdd:COG1946 174 WMRARDPLPDDPL-HAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGL 248
|
250 260
....*....|....*....|...
gi 656278386 261 VRGEIFNQKGELVATAVQEGVMR 283
Cdd:COG1946 249 ERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
22-283 |
1.51e-108 |
|
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: 315.45 E-value: 1.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQSENLG---LPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNG 98
Cdd:TIGR00189 8 FRGSHLSKGrqfLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 99 RPIFYLTASYHGDAPGFEHQISMPDIPGPEN-FASETELASHIAEFLPEKLRKTFCGEKPIEMRPVTVVNPLKPKKTEaK 177
Cdd:TIGR00189 88 KTIFTLQASFQAEKSGIEHQSTMPKVPPPESeLPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGKEDP-P 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 178 QYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMTPnFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANT 257
Cdd:TIGR00189 167 QYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCH-SMAASLDHSIWFHRPFRADDWLLYKCSSPSAGGS 245
|
250 260
....*....|....*....|....*.
gi 656278386 258 RGLVRGEIFNQKGELVATAVQEGVMR 283
Cdd:TIGR00189 246 RGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
9.80e-56 |
|
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: 180.22 E-value: 9.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 32 PQVYGGQVLGQALSAARYTVQDDrSVHSFHSYFLFPGDPEkPIIYDVENLRDGRSFSTRRVKAIQNGRPIFYLTASYH-- 109
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPD-PLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 110 GDAPGFEHQISMPDIPGPEnfasETELASHIAEFLPEKLRKTFCgeKPIEMRPVTVVNPLKPKKTeAKQYLWVRANgamP 189
Cdd:pfam13622 87 RSSEWELTPAAPPPLPPPE----DCPLAADEAPFPLFRRVPGFL--DPFEPRFARGGGPFSPGGP-GRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 190 DNQLIHQYLLAYASDwgFLVTALHPHEVSIMTPnFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLVRGEIFNQK 269
Cdd:pfam13622 157 GGEPDPLAALAYLAD--AFPPRVLSLRLDPPAS-GWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 656278386 270 GELVATAVQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
2.58e-44 |
|
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: 145.85 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 178 QYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSiMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANT 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 656278386 258 RGLVRGEIFNQKGELVATAVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
22-283 |
4.57e-151 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 423.78 E-value: 4.57e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQSENLGLPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNGRPI 101
Cdd:PRK10526 22 FRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 102 FYLTASYHGDAPGFEHQISMPDIPGPENFASETELASHIAEFLPEKLRKTFCGEKPIEMRPVTVVNPLKPKKTEAKQYLW 181
Cdd:PRK10526 102 FYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETDIAQSLAHLLPPVLKDKFICDRPLEIRPVEFHNPLKGHVAEPVRQVW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 182 VRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLV 261
Cdd:PRK10526 182 IRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFV 261
|
250 260
....*....|....*....|..
gi 656278386 262 RGEIFNQKGELVATAVQEGVMR 283
Cdd:PRK10526 262 RGEFYTQDGVLVASTVQEGVMR 283
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
22-283 |
8.41e-128 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 364.20 E-value: 8.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQ-SENLGLPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNGRP 100
Cdd:COG1946 19 FRGEiSPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 101 IFYLTASYHGDAPGFEHQISMPDIPGPENFASETELAshIAEFLPeklRKTFCGEKPIEMRPVTVVNPLKPKKTEAKQYL 180
Cdd:COG1946 99 IFTATASFGVPEEGLEHQAPMPDVPPPEDLPSLPELL--IAGVLP---LRFFAFLRPFDIRPVEGPLPFAPPSGEPRQRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 181 WVRANGAMPDNQLiHQYLLAYASDWGFLVTALHphevSIMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGL 260
Cdd:COG1946 174 WMRARDPLPDDPL-HAALLAYASDATPPATALL----SWLGPPLPAASLDHAMWFHRPFRADDWLLYDADSPSASGGRGL 248
|
250 260
....*....|....*....|...
gi 656278386 261 VRGEIFNQKGELVATAVQEGVMR 283
Cdd:COG1946 249 ERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
22-283 |
1.51e-108 |
|
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: 315.45 E-value: 1.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQSENLG---LPQVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNG 98
Cdd:TIGR00189 8 FRGSHLSKGrqfLNRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 99 RPIFYLTASYHGDAPGFEHQISMPDIPGPEN-FASETELASHIAEFLPEKLRKTFCGEKPIEMRPVTVVNPLKPKKTEaK 177
Cdd:TIGR00189 88 KTIFTLQASFQAEKSGIEHQSTMPKVPPPESeLPRENQLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGKEDP-P 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 178 QYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMTPnFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANT 257
Cdd:TIGR00189 167 QYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCH-SMAASLDHSIWFHRPFRADDWLLYKCSSPSAGGS 245
|
250 260
....*....|....*....|....*.
gi 656278386 258 RGLVRGEIFNQKGELVATAVQEGVMR 283
Cdd:TIGR00189 246 RGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
33-282 |
4.68e-92 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 278.53 E-value: 4.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 33 QVYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNGRPIFYLTASYHGDA 112
Cdd:PLN02868 159 KVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 113 PGFEHQIS-MPDIPGPENFASETEL-ASHIAE-FLPEKLRKTFCGEK----PIEMRPVTVVNPLKPKKTEAKQYLWVRAN 185
Cdd:PLN02868 239 QGFEHQEStMPHVPPPETLLSREELrERRLTDpRLPRSYRNKVAAKPfvpwPIEIRFCEPNNSTNQTKSPPRLRYWFRAK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 186 GAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMTpnFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLVRGEI 265
Cdd:PLN02868 319 GKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLK--FAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHM 396
|
250
....*....|....*..
gi 656278386 266 FNQKGELVATAVQEGVM 282
Cdd:PLN02868 397 FNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
32-282 |
9.80e-56 |
|
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: 180.22 E-value: 9.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 32 PQVYGGQVLGQALSAARYTVQDDrSVHSFHSYFLFPGDPEkPIIYDVENLRDGRSFSTRRVKAIQNGRPIFYLTASYH-- 109
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPD-PLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 110 GDAPGFEHQISMPDIPGPEnfasETELASHIAEFLPEKLRKTFCgeKPIEMRPVTVVNPLKPKKTeAKQYLWVRANgamP 189
Cdd:pfam13622 87 RSSEWELTPAAPPPLPPPE----DCPLAADEAPFPLFRRVPGFL--DPFEPRFARGGGPFSPGGP-GRVRLWVRLR---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 190 DNQLIHQYLLAYASDwgFLVTALHPHEVSIMTPnFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLVRGEIFNQK 269
Cdd:pfam13622 157 GGEPDPLAALAYLAD--AFPPRVLSLRLDPPAS-GWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDED 233
|
250
....*....|...
gi 656278386 270 GELVATAVQEGVM 282
Cdd:pfam13622 234 GRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
2.58e-44 |
|
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: 145.85 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 178 QYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSiMTPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANT 257
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLP-LFDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 656278386 258 RGLVRGEIFNQKGELVATAVQEGVM 282
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
22-109 |
1.90e-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: 239529 [Multi-domain] Cd Length: 94 Bit Score: 143.15 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 22 FRGQSENLGLPQ---VYGGQVLGQALSAARYTVQDDRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQNG 98
Cdd:cd03445 3 FRGVSPPVPPGQgrgVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQNG 82
|
90
....*....|.
gi 656278386 99 RPIFYLTASYH 109
Cdd:cd03445 83 KVIFTATASFQ 93
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
148-281 |
2.94e-40 |
|
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: 136.61 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 148 LRKTFCGEKPIEMRPVTVVNPLKPKKTeAKQYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEvsIMTPNFQVa 227
Cdd:pfam02551 2 ANDLFRGEYPVAVRPGELRRTFGGQVV-AHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG--FLCDGIQV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 656278386 228 TIDHSIWFHRPFKMDEWLLYAIESPTAANTRGLVRGEIFN-QKGELVATAVQEGV 281
Cdd:pfam02551 78 SLDHSIYFHRPGDLNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
178-282 |
8.38e-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: 113.59 E-value: 8.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 178 QYLWVRANGAMPDNQLIHQYLLAYASDWGFLVTALHPHEVSIMtpnfqvATIDHSIWFHRPFKMDEWLLYAIESPTAANT 257
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGF------ASLDHHIYFHRPGDADEWLLYEVESLRDGRS 74
|
90 100
....*....|....*....|....*
gi 656278386 258 RGLVRGEIFNQKGELVATAVQEGVM 282
Cdd:cd00556 75 RALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
32-109 |
7.20e-25 |
|
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: 95.49 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 32 PQVYGGQVLGQALSAARYTVQD-----DRSVHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAIQN-GRPIFYLT 105
Cdd:cd00556 15 RRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdGKLVASAT 94
|
....
gi 656278386 106 ASYH 109
Cdd:cd00556 95 QSFL 98
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
180-281 |
2.21e-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: 53.63 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 180 LWVRANGAMPDNQLI-HQYLLAYASDWGFLVTALHPHEvsimtPNFQVATIDHSIWFHRPFKMDEWLLYAIESPTAANTR 258
Cdd:cd03440 3 LRLTVTPEDIDGGGIvHGGLLLALADEAAGAAAARLGG-----RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS 77
|
90 100
....*....|....*....|...
gi 656278386 259 GLVRGEIFNQKGELVATAVQEGV 281
Cdd:cd03440 78 VTVEVEVRNEDGKLVATATATFV 100
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
31-103 |
1.06e-07 |
|
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: 49.94 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 31 LPQVYGGQVLG--QALSAARYTVQDDRSVHSF------------------------------HS-YFLFPGDPEKPIIYD 77
Cdd:pfam02551 19 LRRTFGGQVVAhqQSWVAALGTVPDDPRLHSCalaylsdltllltalyphgflcdgiqvsldHSiYFHRPGDLNKWILYD 98
|
90 100 110
....*....|....*....|....*....|....
gi 656278386 78 VEN--------LRDGRSFSTrrvkaiQNGRPIFY 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 |
4.19e-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: 35.91 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656278386 30 GLPQVYGGQVLGQALSAARYTVQDDRS------VHSFHSYFLFPGDPEKPIIYDVENLRDGRSFSTRRVKAI-QNGRPIF 102
Cdd:cd03440 14 GGGIVHGGLLLALADEAAGAAAARLGGrglgavTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRnEDGKLVA 93
|
....*.
gi 656278386 103 YLTASY 108
Cdd:cd03440 94 TATATF 99
|
|
| |
