|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
2-274 |
9.31e-84 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 252.88 E-value: 9.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 2 TVGTISEVLALEgTQEADVFSGPAIPSQ-IERTFGGQVAAQALAAAQRTVD-NKQVHSLHGYFVGPGDTKKPLELRVERL 79
Cdd:COG1946 1 ALMELLDLLDLE-RLEDGLFRGEISPDQgLRRVFGGQVAAQALRAARRTVPeDRPPHSLHAYFLRPGDPDGPIEYEVERL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 80 RDGRSFASRQVRVIQDGRLVFILLASFHRDGDtGPEHQDVAPQVLSPDEA-----ARRGGGAPystRIILKEWTDWDIRL 154
Cdd:COG1946 80 RDGRSFSTRRVTAIQGGRVIFTATASFGVPEE-GLEHQAPMPDVPPPEDLpslpeLLIAGVLP---LRFFAFLRPFDIRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 155 VPDegrDDAAAEVTGAGYRHIWFRNTGELGSDPAfHRAALTYMSDMTLIRSALIPHQGEKIQLASLDHAVWFLRPFRVDE 234
Cdd:COG1946 156 VEG---PLPFAPPSGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAASLDHAMWFHRPFRADD 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1181172035 235 WLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGLTR 274
Cdd:COG1946 232 WLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
22-274 |
4.20e-71 |
|
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: 220.31 E-value: 4.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 22 SGPAIPSQI-ERTFGGQVAAQALAAAQRTVD-NKQVHSLHGYFVGPGDTKKPLELRVERLRDGRSFASRQVRVIQDGRLV 99
Cdd:TIGR00189 11 SHLSKGRQFlNRTFGGQVVGQALAAASKTVPeEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 100 FILLASFHRDGDtGPEHQDVAPQVLSPDEAARRGG----GAPYSTRIILKE--WTDWDIRLVP-DEGRDDAAAEVTGAgy 172
Cdd:TIGR00189 91 FTLQASFQAEKS-GIEHQSTMPKVPPPESELPRENqlatKYPATLPRFLKHvvPFERPFEIRPvNLLNYLGGKEDPPQ-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 173 rHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHQGE---KIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGT 249
Cdd:TIGR00189 168 -YVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAgfcHSMAASLDHSIWFHRPFRADDWLLYKCSSPSAGGSR 246
|
250 260
....*....|....*....|....*
gi 1181172035 250 AIARGKLFTEQGELVALVNQEGLTR 274
Cdd:TIGR00189 247 GLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
3-272 |
1.67e-62 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 202.64 E-value: 1.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 3 VGTISEVLALEgTQEADVFSG---PAIPSqIERTFGGQVAAQALAAAQRTVDN-KQVHSLHGYFVGPGDTKKPLELRVER 78
Cdd:PLN02868 129 CSLVERILHLE-PLEVDIFRGitlPDAPT-FGKVFGGQLVGQALAAASKTVDPlKLVHSLHAYFLLVGDINLPIIYQVER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 79 LRDGRSFASRQVRVIQDGRLVFILLASFHRDGDtGPEHQDV----AP---QVLSPDEAARRGGGAPYSTRIILKEWT--- 148
Cdd:PLN02868 207 IRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQ-GFEHQEStmphVPppeTLLSREELRERRLTDPRLPRSYRNKVAakp 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 149 --DW--DIRLVpdEGRDDAAAEVTGAGYRhIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPH--QGEKIQLASLDH 222
Cdd:PLN02868 286 fvPWpiEIRFC--EPNNSTNQTKSPPRLR-YWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHrtKGLKFAALSLDH 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1181172035 223 AVWFLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGL 272
Cdd:PLN02868 363 SMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-272 |
9.82e-44 |
|
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: 149.40 E-value: 9.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 48 RTVDNKQVHSLHGYFVGPGDTKkPLELRVERLRDGRSFASRQVRVIQDGRLVFILLASFHRDGDTGPEHQD-VAPQVLSP 126
Cdd:pfam13622 26 RTVPPDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWELTPaAPPPLPPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 127 DEAARRGGGAPYSTRIILKEWTD-WDIRLVPDEGRDDAAaevtGAGYRHIWFRNTGElgsDPAFHRAALTYMSDM-TLIR 204
Cdd:pfam13622 105 EDCPLAADEAPFPLFRRVPGFLDpFEPRFARGGGPFSPG----GPGRVRLWVRLRDG---GEPDPLAALAYLADAfPPRV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181172035 205 SALIPHQGEKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGL 272
Cdd:pfam13622 178 LSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVL 245
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
173-272 |
3.81e-37 |
|
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: 127.75 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 173 RHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHQG---EKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGT 249
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLplfDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80
|
90 100
....*....|....*....|...
gi 1181172035 250 AIARGKLFTEQGELVALVNQEGL 272
Cdd:cd03444 81 GLVEGRIFTRDGELVASVAQEGL 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
2-274 |
9.31e-84 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 252.88 E-value: 9.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 2 TVGTISEVLALEgTQEADVFSGPAIPSQ-IERTFGGQVAAQALAAAQRTVD-NKQVHSLHGYFVGPGDTKKPLELRVERL 79
Cdd:COG1946 1 ALMELLDLLDLE-RLEDGLFRGEISPDQgLRRVFGGQVAAQALRAARRTVPeDRPPHSLHAYFLRPGDPDGPIEYEVERL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 80 RDGRSFASRQVRVIQDGRLVFILLASFHRDGDtGPEHQDVAPQVLSPDEA-----ARRGGGAPystRIILKEWTDWDIRL 154
Cdd:COG1946 80 RDGRSFSTRRVTAIQGGRVIFTATASFGVPEE-GLEHQAPMPDVPPPEDLpslpeLLIAGVLP---LRFFAFLRPFDIRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 155 VPDegrDDAAAEVTGAGYRHIWFRNTGELGSDPAfHRAALTYMSDMTLIRSALIPHQGEKIQLASLDHAVWFLRPFRVDE 234
Cdd:COG1946 156 VEG---PLPFAPPSGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAASLDHAMWFHRPFRADD 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1181172035 235 WLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGLTR 274
Cdd:COG1946 232 WLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
22-274 |
4.20e-71 |
|
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: 220.31 E-value: 4.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 22 SGPAIPSQI-ERTFGGQVAAQALAAAQRTVD-NKQVHSLHGYFVGPGDTKKPLELRVERLRDGRSFASRQVRVIQDGRLV 99
Cdd:TIGR00189 11 SHLSKGRQFlNRTFGGQVVGQALAAASKTVPeEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRRVKAVQHGKTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 100 FILLASFHRDGDtGPEHQDVAPQVLSPDEAARRGG----GAPYSTRIILKE--WTDWDIRLVP-DEGRDDAAAEVTGAgy 172
Cdd:TIGR00189 91 FTLQASFQAEKS-GIEHQSTMPKVPPPESELPRENqlatKYPATLPRFLKHvvPFERPFEIRPvNLLNYLGGKEDPPQ-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 173 rHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHQGE---KIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGT 249
Cdd:TIGR00189 168 -YVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAgfcHSMAASLDHSIWFHRPFRADDWLLYKCSSPSAGGSR 246
|
250 260
....*....|....*....|....*
gi 1181172035 250 AIARGKLFTEQGELVALVNQEGLTR 274
Cdd:TIGR00189 247 GLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
3-272 |
1.67e-62 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 202.64 E-value: 1.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 3 VGTISEVLALEgTQEADVFSG---PAIPSqIERTFGGQVAAQALAAAQRTVDN-KQVHSLHGYFVGPGDTKKPLELRVER 78
Cdd:PLN02868 129 CSLVERILHLE-PLEVDIFRGitlPDAPT-FGKVFGGQLVGQALAAASKTVDPlKLVHSLHAYFLLVGDINLPIIYQVER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 79 LRDGRSFASRQVRVIQDGRLVFILLASFHRDGDtGPEHQDV----AP---QVLSPDEAARRGGGAPYSTRIILKEWT--- 148
Cdd:PLN02868 207 IRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQ-GFEHQEStmphVPppeTLLSREELRERRLTDPRLPRSYRNKVAakp 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 149 --DW--DIRLVpdEGRDDAAAEVTGAGYRhIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPH--QGEKIQLASLDH 222
Cdd:PLN02868 286 fvPWpiEIRFC--EPNNSTNQTKSPPRLR-YWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHrtKGLKFAALSLDH 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1181172035 223 AVWFLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGL 272
Cdd:PLN02868 363 SMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
9-274 |
2.38e-50 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 167.62 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 9 VLALEGTQEAdVFSGPAIPSQIERTFGGQVAAQALAAAQRTVD-NKQVHSLHGYFVGPGDTKKPLELRVERLRDGRSFAS 87
Cdd:PRK10526 11 LLNLEKIEEG-LFRGQSEDLGLRQVFGGQVVGQALYAAKETVPeERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 88 RQVRVIQDGRLVFILLASFhRDGDTGPEHQDVAPQVLSPDeaarrggGAPYSTRIILKEwtdwdIRLVPDEGRD----DA 163
Cdd:PRK10526 90 RRVAAIQNGKPIFYMTASF-QAPEAGFEHQKTMPSAPAPD-------GLPSETDIAQSL-----AHLLPPVLKDkficDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 164 AAEV------------TGAGYRHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPH------QGekIQLASLDHAVW 225
Cdd:PRK10526 157 PLEIrpvefhnplkghVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHgigflePG--MQIATIDHSMW 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1181172035 226 FLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGLTR 274
Cdd:PRK10526 235 FHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
48-272 |
9.82e-44 |
|
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: 149.40 E-value: 9.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 48 RTVDNKQVHSLHGYFVGPGDTKkPLELRVERLRDGRSFASRQVRVIQDGRLVFILLASFHRDGDTGPEHQD-VAPQVLSP 126
Cdd:pfam13622 26 RTVPPDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSEWELTPaAPPPLPPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 127 DEAARRGGGAPYSTRIILKEWTD-WDIRLVPDEGRDDAAaevtGAGYRHIWFRNTGElgsDPAFHRAALTYMSDM-TLIR 204
Cdd:pfam13622 105 EDCPLAADEAPFPLFRRVPGFLDpFEPRFARGGGPFSPG----GPGRVRLWVRLRDG---GEPDPLAALAYLADAfPPRV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181172035 205 SALIPHQGEKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQGELVALVNQEGL 272
Cdd:pfam13622 178 LSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARLWDEDGRLVATSRQEVL 245
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
173-272 |
3.81e-37 |
|
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: 127.75 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 173 RHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHQG---EKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGT 249
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLplfDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGR 80
|
90 100
....*....|....*....|...
gi 1181172035 250 AIARGKLFTEQGELVALVNQEGL 272
Cdd:cd03444 81 GLVEGRIFTRDGELVASVAQEGL 103
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
19-108 |
9.76e-29 |
|
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: 105.40 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 19 DVFSG---PAIPSQIERTFGGQVAAQALAAAQRTV-DNKQVHSLHGYFVGPGDTKKPLELRVERLRDGRSFASRQVRVIQ 94
Cdd:cd03445 1 DRFRGvspPVPPGQGRGVFGGQVLAQALVAAARTVpDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 1181172035 95 DGRLVFILLASFHR 108
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
173-272 |
3.98e-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: 238311 [Multi-domain] Cd Length: 99 Bit Score: 103.96 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 173 RHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHqgEKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGTAIA 252
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPH--GASGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALR 78
|
90 100
....*....|....*....|
gi 1181172035 253 RGKLFTEQGELVALVNQEGL 272
Cdd:cd00556 79 RGRAYQRDGKLVASATQSFL 98
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
148-272 |
7.98e-27 |
|
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: 101.94 E-value: 7.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 148 TDWDIRLVPDEGRDDAAAEVtgAGYRHIWFRNTGELGSDPAFHRAALTYMSDMTLIRSALIPHQ-GEKIQLASLDHAVWF 226
Cdd:pfam02551 8 GEYPVAVRPGELRRTFGGQV--VAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHGfLCDGIQVSLDHSIYF 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1181172035 227 LRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQ-GELVALVNQEGL 272
Cdd:pfam02551 86 HRPGDLNKWILYDVESPSASGGRGLRQGRNFSTQsGKLIASVQQEGL 132
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
55-108 |
3.26e-16 |
|
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: 72.38 E-value: 3.26e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1181172035 55 VHSLHGYFVGPGDTKKPLELRVERLRDGRSFASRQVRVIQ-DGRLVFILLASFHR 108
Cdd:cd00556 45 SLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQrDGKLVASATQSFLV 99
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
181-272 |
2.40e-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: 39.38 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181172035 181 GELGSDPAFHRAALTYMSDMTLIRsALIPHQGEKIQLASLDHAVWFLRPFRVDEWLLYEQVSPTASQGTAIARGKLFTEQ 260
Cdd:cd03440 10 EDIDGGGIVHGGLLLALADEAAGA-AAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNED 88
|
90
....*....|..
gi 1181172035 261 GELVALVNQEGL 272
Cdd:cd03440 89 GKLVATATATFV 100
|
|
| |
