|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
7-288 |
4.27e-68 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 212.82 E-value: 4.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 7 RLKKIDDLTYVGECDSEHPAARVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRY 86
Cdd:COG1946 10 DLERLEDGLFRGEISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 87 VEAVQHGKVIHLAEFSLQKLAsvkDTFSLTPEFPsHVPGPDGLVSnitgrhqkVAEGVDARELRGQVTERMAPsLEIRPA 166
Cdd:COG1946 90 VTAIQGGRVIFTATASFGVPE---EGLEHQAPMP-DVPPPEDLPS--------LPELLIAGVLPLRFFAFLRP-FDIRPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 167 DLNMFLHGTGGVNQkQYLWIRYKIPVDKSDymLRHATIVYLSDLELVTTGALCFDDKmfKLQT-SMDHSAWIHQyEFDIN 245
Cdd:COG1946 157 EGPLPFAPPSGEPR-QRVWMRARDPLPDDP--LHAALLAYASDATPPATALLSWLGP--PLPAaSLDHAMWFHR-PFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 212645202 246 DWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALIYKV 288
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
10-285 |
1.55e-60 |
|
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: 193.34 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 10 KIDDLTYVGEcdSEHPAA----RVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIR 85
Cdd:TIGR00189 2 KIDENLFRGS--HLSKGRqflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 86 YVEAVQHGKVIhlaeFSLQK-LASVKDTFSLTPEFPShVPGPDGLVSNITGRHQKVAEGVDARELRGQVTERMapsLEIR 164
Cdd:TIGR00189 80 RVKAVQHGKTI----FTLQAsFQAEKSGIEHQSTMPK-VPPPESELPRENQLATKYPATLPRFLKHVVPFERP---FEIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 165 PADLNMFLhgTGGVNQKQYLWIRYKIPVDKsDYMLRHATIVYLSDLELVTTgALCFDDKMFKLQT---SMDHSAWIHQyE 241
Cdd:TIGR00189 152 PVNLLNYL--GGKEDPPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPT-ALNPHNKAGFCHSmaaSLDHSIWFHR-P 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 212645202 242 FDINDWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:TIGR00189 227 FRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLV 270
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
7-285 |
1.08e-41 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 145.28 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 7 RLKKIDDLTYVGEcdSEHPAAR-VFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIR 85
Cdd:PRK10526 13 NLEKIEEGLFRGQ--SEDLGLRqVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 86 YVEAVQHGKVIHLAEFSLQklaSVKDTFSLTPEFPsHVPGPDGLVSnitgrhqkvaEGVDARELRGQVTERM------AP 159
Cdd:PRK10526 91 RVAAIQNGKPIFYMTASFQ---APEAGFEHQKTMP-SAPAPDGLPS----------ETDIAQSLAHLLPPVLkdkficDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 160 SLEIRPADLNMFLHGTGGvNQKQYLWIRY--KIPVDKS--DYMLRhativYLSDLELVTTG----ALCFDDKMFKLQTsM 231
Cdd:PRK10526 157 PLEIRPVEFHNPLKGHVA-EPVRQVWIRAngSVPDDLRvhQYLLG-----YASDLNFLPVAlqphGIGFLEPGMQIAT-I 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 212645202 232 DHSAWIHQyEFDINDWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:PRK10526 230 DHSMWFHR-PFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVM 282
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
24-285 |
1.83e-39 |
|
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: 138.23 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 24 HPAARVFGGHVLAQAMSAAYyTAPEGFYVHAVHCYFIRGGEESiPITYNVKIIRDGRNFAIRYVEAVQHGKVIHLAEFSL 103
Cdd:pfam13622 6 SPGRAPHGGYVAALLLRAAE-RTVPPDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 104 QKLASvkDTFSLTPEFPSHVPGPDGLVsnitgrhqkVAEGVDARELRGQVTERMAPsLEIRPADLNMFlhGTGGVNQKQY 183
Cdd:pfam13622 84 GRLRS--SEWELTPAAPPPLPPPEDCP---------LAADEAPFPLFRRVPGFLDP-FEPRFARGGGP--FSPGGPGRVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 184 LWIRYKIPVDKSDYmlrhATIVYLSDLELVTTGALCFDDKMFKLQTSMDHSAWIHQyEFDINDWILYEQECVANSNHRSL 263
Cdd:pfam13622 150 LWVRLRDGGEPDPL----AALAYLADAFPPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETPVAGDGRGD 224
|
250 260
....*....|....*....|..
gi 212645202 264 IHGRLWSRDGKLIMSTSQEALI 285
Cdd:pfam13622 225 VEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
16-105 |
1.83e-39 |
|
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: 133.13 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 16 YVGE--CDSEHPAARVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRYVEAVQHG 93
Cdd:cd03445 3 FRGVspPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQNG 82
|
90
....*....|..
gi 212645202 94 KVIHLAEFSLQK 105
Cdd:cd03445 83 KVIFTATASFQR 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
7-288 |
4.27e-68 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 212.82 E-value: 4.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 7 RLKKIDDLTYVGECDSEHPAARVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRY 86
Cdd:COG1946 10 DLERLEDGLFRGEISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 87 VEAVQHGKVIHLAEFSLQKLAsvkDTFSLTPEFPsHVPGPDGLVSnitgrhqkVAEGVDARELRGQVTERMAPsLEIRPA 166
Cdd:COG1946 90 VTAIQGGRVIFTATASFGVPE---EGLEHQAPMP-DVPPPEDLPS--------LPELLIAGVLPLRFFAFLRP-FDIRPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 167 DLNMFLHGTGGVNQkQYLWIRYKIPVDKSDymLRHATIVYLSDLELVTTGALCFDDKmfKLQT-SMDHSAWIHQyEFDIN 245
Cdd:COG1946 157 EGPLPFAPPSGEPR-QRVWMRARDPLPDDP--LHAALLAYASDATPPATALLSWLGP--PLPAaSLDHAMWFHR-PFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 212645202 246 DWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALIYKV 288
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRGR 273
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
10-285 |
1.55e-60 |
|
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: 193.34 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 10 KIDDLTYVGEcdSEHPAA----RVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIR 85
Cdd:TIGR00189 2 KIDENLFRGS--HLSKGRqflnRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 86 YVEAVQHGKVIhlaeFSLQK-LASVKDTFSLTPEFPShVPGPDGLVSNITGRHQKVAEGVDARELRGQVTERMapsLEIR 164
Cdd:TIGR00189 80 RVKAVQHGKTI----FTLQAsFQAEKSGIEHQSTMPK-VPPPESELPRENQLATKYPATLPRFLKHVVPFERP---FEIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 165 PADLNMFLhgTGGVNQKQYLWIRYKIPVDKsDYMLRHATIVYLSDLELVTTgALCFDDKMFKLQT---SMDHSAWIHQyE 241
Cdd:TIGR00189 152 PVNLLNYL--GGKEDPPQYVWRRARGSLPD-DPRLHQCALAYLSDLTLLPT-ALNPHNKAGFCHSmaaSLDHSIWFHR-P 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 212645202 242 FDINDWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:TIGR00189 227 FRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLV 270
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
7-285 |
1.08e-41 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 145.28 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 7 RLKKIDDLTYVGEcdSEHPAAR-VFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIR 85
Cdd:PRK10526 13 NLEKIEEGLFRGQ--SEDLGLRqVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 86 YVEAVQHGKVIHLAEFSLQklaSVKDTFSLTPEFPsHVPGPDGLVSnitgrhqkvaEGVDARELRGQVTERM------AP 159
Cdd:PRK10526 91 RVAAIQNGKPIFYMTASFQ---APEAGFEHQKTMP-SAPAPDGLPS----------ETDIAQSLAHLLPPVLkdkficDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 160 SLEIRPADLNMFLHGTGGvNQKQYLWIRY--KIPVDKS--DYMLRhativYLSDLELVTTG----ALCFDDKMFKLQTsM 231
Cdd:PRK10526 157 PLEIRPVEFHNPLKGHVA-EPVRQVWIRAngSVPDDLRvhQYLLG-----YASDLNFLPVAlqphGIGFLEPGMQIAT-I 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 212645202 232 DHSAWIHQyEFDINDWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:PRK10526 230 DHSMWFHR-PFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVM 282
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
8-285 |
1.51e-39 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 142.55 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 8 LKKIDDLTYVGECDSEHPA-ARVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRY 86
Cdd:PLN02868 138 LEPLEVDIFRGITLPDAPTfGKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 87 VEAVQHGKVIHLAEFSLQKLasvKDTFSLTPEFPSHVPGPDGLVSNITGRHQKVAEGVDARELRGQVT--ERMAPSLEIR 164
Cdd:PLN02868 218 VDAIQKGKVIFTLFASFQKE---EQGFEHQESTMPHVPPPETLLSREELRERRLTDPRLPRSYRNKVAakPFVPWPIEIR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 165 padlnmFLHGTGGVNQ-----KQYLWIRYKIPVdKSDYMLRHATIVYLSDLELVTTGALCFDDKMFKLQT-SMDHSAWIH 238
Cdd:PLN02868 295 ------FCEPNNSTNQtksppRLRYWFRAKGKL-SDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAAlSLDHSMWFH 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 212645202 239 QyEFDINDWILYEQECVANSNHRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:PLN02868 368 R-PFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEALL 413
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
24-285 |
1.83e-39 |
|
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: 138.23 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 24 HPAARVFGGHVLAQAMSAAYyTAPEGFYVHAVHCYFIRGGEESiPITYNVKIIRDGRNFAIRYVEAVQHGKVIHLAEFSL 103
Cdd:pfam13622 6 SPGRAPHGGYVAALLLRAAE-RTVPPDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 104 QKLASvkDTFSLTPEFPSHVPGPDGLVsnitgrhqkVAEGVDARELRGQVTERMAPsLEIRPADLNMFlhGTGGVNQKQY 183
Cdd:pfam13622 84 GRLRS--SEWELTPAAPPPLPPPEDCP---------LAADEAPFPLFRRVPGFLDP-FEPRFARGGGP--FSPGGPGRVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 184 LWIRYKIPVDKSDYmlrhATIVYLSDLELVTTGALCFDDKMFKLQTSMDHSAWIHQyEFDINDWILYEQECVANSNHRSL 263
Cdd:pfam13622 150 LWVRLRDGGEPDPL----AALAYLADAFPPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETPVAGDGRGD 224
|
250 260
....*....|....*....|..
gi 212645202 264 IHGRLWSRDGKLIMSTSQEALI 285
Cdd:pfam13622 225 VEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
16-105 |
1.83e-39 |
|
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: 133.13 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 16 YVGE--CDSEHPAARVFGGHVLAQAMSAAYYTAPEGFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRYVEAVQHG 93
Cdd:cd03445 3 FRGVspPVPPGQGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQNG 82
|
90
....*....|..
gi 212645202 94 KVIHLAEFSLQK 105
Cdd:cd03445 83 KVIFTATASFQR 94
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
182-285 |
1.00e-28 |
|
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: 105.79 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 182 QYLWIRYKIPVDKsDYMLRHATIVYLSDLELVTTGALCFDDKMFKL--QTSMDHSAWIHQYEFDiNDWILYEQECVANSN 259
Cdd:cd03444 1 LRVWVRARGPLPD-DPRLHAAALAYLSDSLLLGTALRPHGLPLFDAsaSASLDHAIWFHRPFRA-DDWLLYEQRSPRAGN 78
|
90 100
....*....|....*....|....*.
gi 212645202 260 HRSLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:cd03444 79 GRGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
182-285 |
6.56e-20 |
|
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: 82.39 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 182 QYLWIRYKIPVDKsDYMLRHATIVYLSDLELVTTGALCFDDKMFklqTSMDHSAWIHQYeFDINDWILYEQECVANSNHR 261
Cdd:cd00556 1 DRFWGRAPGPLPD-DRRVFGGQLAAQSDLAALRTVPRPHGASGF---ASLDHHIYFHRP-GDADEWLLYEVESLRDGRSR 75
|
90 100
....*....|....*....|....
gi 212645202 262 SLIHGRLWSRDGKLIMSTSQEALI 285
Cdd:cd00556 76 ALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
13-105 |
7.85e-19 |
|
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: 79.70 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 13 DLTYVGECDSEHPAARVFGGHVLAQAMSAAYYTAPE-----GFYVHAVHCYFIRGGEESIPITYNVKIIRDGRNFAIRYV 87
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRG 80
|
90
....*....|....*....
gi 212645202 88 EAVQH-GKVIHLAEFSLQK 105
Cdd:cd00556 81 RAYQRdGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
161-284 |
1.06e-13 |
|
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: 66.88 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645202 161 LEIRPADLNMFLHGTggVNQKQYLWIRYKIPVdKSDYMLRHATIVYLSDLELVTTGALCFDDKMFKLQTSMDHSAWIHQy 240
Cdd:pfam02551 12 VAVRPGELRRTFGGQ--VVAHQQSWVAALGTV-PDDPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQVSLDHSIYFHR- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 212645202 241 EFDINDWILYEQECVANSNHRSLIHGRLWS-RDGKLIMSTSQEAL 284
Cdd:pfam02551 88 PGDLNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| |
