|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
33-329 |
2.48e-56 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 183.93 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 33 DSFTNIFQQWQPPasRGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQ 112
Cdd:COG1946 17 GLFRGEISPDQGL--RRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 113 QGRSIATVMVSFA-RQSSVEVkqlqhsTFPMGDLK----------PPDEVVEEEPEWTRTEPFQRRAIDARDQLV-SSIH 180
Cdd:COG1946 95 GGRVIFTATASFGvPEEGLEH------QAPMPDVPppedlpslpeLLIAGVLPLRFFAFLRPFDIRPVEGPLPFApPSGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 PHQRIfrqWIRYKGVIPsaDGPsAHLHALAFVTDSYFILTAARVHrlwrlpfepedvpflqkevrsqvqkvseceslgss 260
Cdd:COG1946 169 PRQRV---WMRARDPLP--DDP-LHAALLAYASDATPPATALLSW----------------------------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 587731504 261 vdewveLQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQEV 329
Cdd:COG1946 208 ------LGPPLPAASLDHAMWFHRPFR--ADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEG 268
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
42-329 |
1.40e-52 |
|
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: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 42 WQPPasRGIYGGALIALCLSAAQKTVSGDFhIHSCHCFFLLAGSIDiRVIFHVERIRDGTTFATRRVEARQQGRSIATVM 121
Cdd:pfam13622 5 WSPG--RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 122 VSFARQSSVEVKQLQHSTFPM-----GDLKPPDEVVEEEPEWT-RTEPFQRRAIDARDQLVSSihpHQRIFRQWIRykgv 195
Cdd:pfam13622 81 ATFGRLRSSEWELTPAAPPPLpppedCPLAADEAPFPLFRRVPgFLDPFEPRFARGGGPFSPG---GPGRVRLWVR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 196 iPSADGPSAHLHALAFVTDSYFiltaARVHRLWRLPfepedvpflqkevrsqvqkvseceslgssvdewvelQRLAMVAS 275
Cdd:pfam13622 154 -LRDGGEPDPLAALAYLADAFP----PRVLSLRLDP------------------------------------PASGWFPT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 587731504 276 LDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQEV 329
Cdd:pfam13622 193 LDLTVYFHRRPP--PGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEV 244
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
36-328 |
8.89e-51 |
|
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: 169.46 E-value: 8.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 36 TNIFQQWQPPASRGI----YGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEAR 111
Cdd:TIGR00189 5 ENLFRGSHLSKGRQFlnrtFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 112 QQGRSIATVMVSFARQSSVEVKQLQ-------HSTFP----MGDLKPPDEVVEEEPEWTRTEPFQRRAIDARDQLVSSIH 180
Cdd:TIGR00189 85 QHGKTIFTLQASFQAEKSGIEHQSTmpkvpppESELPrenqLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGKED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 PHQRIfrqWIRYKGVIPsaDGPSAHLHALAFVTDSYFILTAARVHRLwrlpfepedvpflqkevrsqvqkvseceslgss 260
Cdd:TIGR00189 165 PPQYV---WRRARGSLP--DDPRLHQCALAYLSDLTLLPTALNPHNK--------------------------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 587731504 261 vdewvELQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQE 328
Cdd:TIGR00189 207 -----AGFCHSMAASLDHSIWFHRPFR--ADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQE 267
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
37-328 |
1.12e-40 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 146.79 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 37 NIFQQWQPPAS---RGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQQ 113
Cdd:PLN02868 144 DIFRGITLPDAptfGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 114 GRSIATVMVSFARqssvEVKQLQHSTFPMGDLKPPDEVVeeepewTRTEPFQRRAIDA------RDQLVSSIH------- 180
Cdd:PLN02868 224 GKVIFTLFASFQK----EEQGFEHQESTMPHVPPPETLL------SREELRERRLTDPrlprsyRNKVAAKPFvpwpiei 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 ---------------PHQRIfrqWIRYKGVIpsADGPSAHLHALAFVTDSYFILTAARVHRLWRLPFEpedvpflqkevr 245
Cdd:PLN02868 294 rfcepnnstnqtkspPRLRY---WFRAKGKL--SDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFA------------ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 246 sqvqkvseceslgssvdewvelqrlamVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATC 325
Cdd:PLN02868 357 ---------------------------ALSLDHSMWFHRPFR--ADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSL 407
|
...
gi 587731504 326 SQE 328
Cdd:PLN02868 408 TQE 410
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
33-126 |
2.68e-34 |
|
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: 121.19 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 33 DSFTNIFQQWQPPASRGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQ 112
Cdd:cd03445 1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 587731504 113 QGRSIATVMVSFAR 126
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
33-329 |
2.48e-56 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 183.93 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 33 DSFTNIFQQWQPPasRGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQ 112
Cdd:COG1946 17 GLFRGEISPDQGL--RRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 113 QGRSIATVMVSFA-RQSSVEVkqlqhsTFPMGDLK----------PPDEVVEEEPEWTRTEPFQRRAIDARDQLV-SSIH 180
Cdd:COG1946 95 GGRVIFTATASFGvPEEGLEH------QAPMPDVPppedlpslpeLLIAGVLPLRFFAFLRPFDIRPVEGPLPFApPSGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 PHQRIfrqWIRYKGVIPsaDGPsAHLHALAFVTDSYFILTAARVHrlwrlpfepedvpflqkevrsqvqkvseceslgss 260
Cdd:COG1946 169 PRQRV---WMRARDPLP--DDP-LHAALLAYASDATPPATALLSW----------------------------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 587731504 261 vdewveLQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQEV 329
Cdd:COG1946 208 ------LGPPLPAASLDHAMWFHRPFR--ADDWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEG 268
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
42-329 |
1.40e-52 |
|
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: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 42 WQPPasRGIYGGALIALCLSAAQKTVSGDFhIHSCHCFFLLAGSIDiRVIFHVERIRDGTTFATRRVEARQQGRSIATVM 121
Cdd:pfam13622 5 WSPG--RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 122 VSFARQSSVEVKQLQHSTFPM-----GDLKPPDEVVEEEPEWT-RTEPFQRRAIDARDQLVSSihpHQRIFRQWIRykgv 195
Cdd:pfam13622 81 ATFGRLRSSEWELTPAAPPPLpppedCPLAADEAPFPLFRRVPgFLDPFEPRFARGGGPFSPG---GPGRVRLWVR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 196 iPSADGPSAHLHALAFVTDSYFiltaARVHRLWRLPfepedvpflqkevrsqvqkvseceslgssvdewvelQRLAMVAS 275
Cdd:pfam13622 154 -LRDGGEPDPLAALAYLADAFP----PRVLSLRLDP------------------------------------PASGWFPT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 587731504 276 LDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQEV 329
Cdd:pfam13622 193 LDLTVYFHRRPP--PGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEV 244
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
36-328 |
8.89e-51 |
|
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: 169.46 E-value: 8.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 36 TNIFQQWQPPASRGI----YGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEAR 111
Cdd:TIGR00189 5 ENLFRGSHLSKGRQFlnrtFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 112 QQGRSIATVMVSFARQSSVEVKQLQ-------HSTFP----MGDLKPPDEVVEEEPEWTRTEPFQRRAIDARDQLVSSIH 180
Cdd:TIGR00189 85 QHGKTIFTLQASFQAEKSGIEHQSTmpkvpppESELPrenqLATKYPATLPRFLKHVVPFERPFEIRPVNLLNYLGGKED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 PHQRIfrqWIRYKGVIPsaDGPSAHLHALAFVTDSYFILTAARVHRLwrlpfepedvpflqkevrsqvqkvseceslgss 260
Cdd:TIGR00189 165 PPQYV---WRRARGSLP--DDPRLHQCALAYLSDLTLLPTALNPHNK--------------------------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 587731504 261 vdewvELQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQE 328
Cdd:TIGR00189 207 -----AGFCHSMAASLDHSIWFHRPFR--ADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQE 267
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
37-328 |
1.12e-40 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 146.79 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 37 NIFQQWQPPAS---RGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQQ 113
Cdd:PLN02868 144 DIFRGITLPDAptfGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 114 GRSIATVMVSFARqssvEVKQLQHSTFPMGDLKPPDEVVeeepewTRTEPFQRRAIDA------RDQLVSSIH------- 180
Cdd:PLN02868 224 GKVIFTLFASFQK----EEQGFEHQESTMPHVPPPETLL------SREELRERRLTDPrlprsyRNKVAAKPFvpwpiei 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 181 ---------------PHQRIfrqWIRYKGVIpsADGPSAHLHALAFVTDSYFILTAARVHRLWRLPFEpedvpflqkevr 245
Cdd:PLN02868 294 rfcepnnstnqtkspPRLRY---WFRAKGKL--SDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFA------------ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 246 sqvqkvseceslgssvdewvelqrlamVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATC 325
Cdd:PLN02868 357 ---------------------------ALSLDHSMWFHRPFR--ADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSL 407
|
...
gi 587731504 326 SQE 328
Cdd:PLN02868 408 TQE 410
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
33-126 |
2.68e-34 |
|
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: 121.19 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 33 DSFTNIFQQWQPPASRGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQ 112
Cdd:cd03445 1 DRFRGVSPPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 587731504 113 QGRSIATVMVSFAR 126
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
187-328 |
1.02e-30 |
|
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.
Pssm-ID: 239528 [Multi-domain] Cd Length: 104 Bit Score: 111.96 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 187 RQWIRYKGVIPsaDGPSAHLHALAFVTDSYFILTAARVHRLWrlpfepedvpflqkevrsqvqkvseceslgssvdewve 266
Cdd:cd03444 2 RVWVRARGPLP--DDPRLHAAALAYLSDSLLLGTALRPHGLP-------------------------------------- 41
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 587731504 267 LQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQE 328
Cdd:cd03444 42 LFDASASASLDHAIWFHRPFR--ADDWLLYEQRSPRAGNGRGLVEGRIFTRDGELVASVAQE 101
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
48-328 |
7.83e-30 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 115.23 E-value: 7.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 48 RGIYGGALIALCLSAAQKTVSGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQQGRSIATVMVSF-AR 126
Cdd:PRK10526 32 RQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFqAP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 127 QSSVEVKQLQHSTFPMGDLKPPDEVVEEEP---------EWTRTEPFQRRAIDARDQLVSSIHPHQRifRQWIRYKGVIP 197
Cdd:PRK10526 112 EAGFEHQKTMPSAPAPDGLPSETDIAQSLAhllppvlkdKFICDRPLEIRPVEFHNPLKGHVAEPVR--QVWIRANGSVP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 198 saDGPSAHLHALAFVTDSYFILTAarvhrlwrlpFEPEDVPFLQKEVRsqvqkvseceslgssvdewvelqrlamVASLD 277
Cdd:PRK10526 190 --DDLRVHQYLLGYASDLNFLPVA----------LQPHGIGFLEPGMQ---------------------------IATID 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 587731504 278 HTIYFHEPLRIkaDDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQE 328
Cdd:PRK10526 231 HSMWFHRPFNL--NEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQE 279
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
187-328 |
1.69e-17 |
|
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: 76.61 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 187 RQWIRYKGVIPsaDGPSAHLHALAFVTDSYFILTAARVHRLwrlpfepedvpflqkevrsqvqkvseceslgssvdewve 266
Cdd:cd00556 2 RFWGRAPGPLP--DDRRVFGGQLAAQSDLAALRTVPRPHGA--------------------------------------- 40
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 587731504 267 lqrlAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQE 328
Cdd:cd00556 41 ----SGFASLDHHIYFHRPGD--ADEWLLYEVESLRDGRSRALRRGRAYQRDGKLVASATQS 96
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
41-124 |
1.71e-17 |
|
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: 76.61 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 41 QWQPPASRGIYGGALIALCLSAAQKTV-----SGDFHIHSCHCFFLLAGSIDIRVIFHVERIRDGTTFATRRVEARQQ-G 114
Cdd:cd00556 8 PGPLPDDRRVFGGQLAAQSDLAALRTVprphgASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRdG 87
|
90
....*....|
gi 587731504 115 RSIATVMVSF 124
Cdd:cd00556 88 KLVASATQSF 97
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
187-328 |
1.88e-09 |
|
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: 55.33 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587731504 187 RQWIRYKGVIPsaDGPSAHLHALAFVTDSYFILTAARVHrlwrlpfepedvpflqkevrsqvqkvseceslgssvdewvE 266
Cdd:pfam02551 32 QSWVAALGTVP--DDPRLHSCALAYLSDLTLLLTALYPH----------------------------------------G 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 587731504 267 LQRLAMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFS-KDGTLLATCSQE 328
Cdd:pfam02551 70 FLCDGIQVSLDHSIYFHRPGD--LNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQE 130
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
271-329 |
5.18e-04 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 39.00 E-value: 5.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 587731504 271 AMVASLDHTIYFHEPLRikADDWMFAEMESPWAAHGRALVVQRIFSKDGTLLATCSQEV 329
Cdd:cd03440 43 LGAVTLSLDVRFLRPVR--PGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATF 99
|
|
| |
