|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
166-456 |
1.18e-135 |
|
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: 391.33 E-value: 1.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 166 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 245
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 246 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 325
Cdd:TIGR00189 80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 326 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 405
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 7496167 406 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 456
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
186-456 |
1.24e-78 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 245.94 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 186 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 265
Cdd:COG1946 29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 266 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 345
Cdd:COG1946 109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 346 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 425
Cdd:COG1946 166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 7496167 426 IASGSRATIEGRIWRRDGVLIASCQQEALVR 456
Cdd:COG1946 241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
187-454 |
2.83e-66 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 218.44 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 187 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 266
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 267 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 342
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 343 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 422
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380
|
250 260 270
....*....|....*....|....*....|..
gi 7496167 423 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 454
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
187-455 |
2.79e-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: 176.37 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 187 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 266
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 267 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 345
Cdd:pfam13622 87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 346 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 425
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216
|
250 260 270
....*....|....*....|....*....|
gi 7496167 426 IASGSRATIEGRIWRRDGVLIASCQQEALV 455
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
351-455 |
7.34e-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: 149.32 E-value: 7.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 351 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 430
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 7496167 431 RATIEGRIWRRDGVLIASCQQEALV 455
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| SPK |
pfam04435 |
Domain of unknown function (DUF545); Family of uncharacterized C. elegans proteins. The region ... |
46-124 |
4.95e-16 |
|
Domain of unknown function (DUF545); Family of uncharacterized C. elegans proteins. The region represented by this family can is found to be repeated up to four time in some proteins.
Pssm-ID: 461308 Cd Length: 104 Bit Score: 73.71 E-value: 4.95e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7496167 46 FVAFVAKRYKDTTTPVPSKELYEGFKNKIKFKKHTDTLRKSIQPFLMGAFKDSDYDDEKKVQMLFVTSTPLkDGMFLEK 124
Cdd:pfam04435 1 LLKFLAEKTKNATEPLSLTQLCREFKEKTGSKLSVSTLRKRFRRILAKIHKLEEYDLETKVRMLFALSAPV-DEDFLKE 78
|
|
| SPK |
smart00583 |
domain in SET and PHD domain containing proteins and protein kinases; |
42-124 |
5.57e-03 |
|
domain in SET and PHD domain containing proteins and protein kinases;
Pssm-ID: 214732 Cd Length: 114 Bit Score: 36.77 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 42 YIEQFVAFVAKRYKDTTTPV----PSKELYEGFKNKIKFKKHTdTLRKSIQPFLMGAFKDSDYDDEKKVQMLFVTSTPLK 117
Cdd:smart00583 1 ELTRFMDFLVEKTKDAIEPLvvplKVFEEFSKLEGNSLLSYET-YYKRFHNKLAPNMIKLNNYSIEERIRMMFALSGKVE 79
|
....*..
gi 7496167 118 DGmFLEK 124
Cdd:smart00583 80 DD-FLER 85
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
166-456 |
1.18e-135 |
|
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: 391.33 E-value: 1.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 166 TELKKDSFSPSTLSNGRQAHhGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITR 245
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFL-NRTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 246 TVEAVQKDKVCFVLQCSFHvEEKSSIIHQSEMPKVPEPEvlmsmrDAVPYMKELVEKgevtpPPAMLARLQSYDSKVysd 325
Cdd:TIGR00189 80 RVKAVQHGKTIFTLQASFQ-AEKSGIEHQSTMPKVPPPE------SELPRENQLATK-----YPATLPRFLKHVVPF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 326 dQDLFEMRCTNLGNYYGFASDkkPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCV 405
Cdd:TIGR00189 145 -ERPFEIRPVNLLNYLGGKED--PPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFCHSMAASLDHSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 7496167 406 WFHRsEVKADEWLLFECKSRIASGSRATIEGRIWRRDGVLIASCQQEALVR 456
Cdd:TIGR00189 222 WFHR-PFRADDWLLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
186-456 |
1.24e-78 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 245.94 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 186 HGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHV 265
Cdd:COG1946 29 LRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 266 EEkSSIIHQSEMPKVPEPEVLMSMRDAVpyMKELVekgevtpPPAMLARLQSydskvysddqdlFEMRCTNLGNYYGfAS 345
Cdd:COG1946 109 PE-EGLEHQAPMPDVPPPEDLPSLPELL--IAGVL-------PLRFFAFLRP------------FDIRPVEGPLPFA-PP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 346 DKKPELYFWMRARGDLSNDERfHRWLIAYNSDSLLVSTAVSPHYTTGFCSSmlfSLDHCVWFHRsEVKADEWLLFECKSR 425
Cdd:COG1946 166 SGEPRQRVWMRARDPLPDDPL-HAALLAYASDATPPATALLSWLGPPLPAA---SLDHAMWFHR-PFRADDWLLYDADSP 240
|
250 260 270
....*....|....*....|....*....|.
gi 7496167 426 IASGSRATIEGRIWRRDGVLIASCQQEALVR 456
Cdd:COG1946 241 SASGGRGLERGRIWDRDGRLVASSRQEGLVR 271
|
|
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
187-454 |
2.83e-66 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 218.44 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 187 GAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 266
Cdd:PLN02868 158 GKVFGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 267 EKsSIIHQ-SEMPKVPEPEVLMSmrdavpyMKELVEKgEVTPPpamlaRL-QSYDSKVYSDDQDLF--EMRCTNLGNYYG 342
Cdd:PLN02868 238 EQ-GFEHQeSTMPHVPPPETLLS-------REELRER-RLTDP-----RLpRSYRNKVAAKPFVPWpiEIRFCEPNNSTN 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 343 fASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFcSSMLFSLDHCVWFHRSeVKADEWLLFEC 422
Cdd:PLN02868 304 -QTKSPPRLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGL-KFAALSLDHSMWFHRP-FRADDWLLFVI 380
|
250 260 270
....*....|....*....|....*....|..
gi 7496167 423 KSRIASGSRATIEGRIWRRDGVLIASCQQEAL 454
Cdd:PLN02868 381 VSPAAHNGRGFATGHMFNRKGELVVSLTQEAL 412
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
190-459 |
1.30e-54 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 183.80 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 190 YGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVEEkS 269
Cdd:PRK10526 35 FGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPE-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 270 SIIHQSEMPKVPEPEVLMSMRDAVPYMKELVekgevtpPPAMlarlqsydSKVYSDDQDlFEMRCTNLGN-YYGFASdkK 348
Cdd:PRK10526 114 GFEHQKTMPSAPAPDGLPSETDIAQSLAHLL-------PPVL--------KDKFICDRP-LEIRPVEFHNpLKGHVA--E 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 349 PELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHyTTGFCSS--MLFSLDHCVWFHRSeVKADEWLLFECKSRI 426
Cdd:PRK10526 176 PVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPH-GIGFLEPgmQIATIDHSMWFHRP-FNLNEWLLYSVESTS 253
|
250 260 270
....*....|....*....|....*....|...
gi 7496167 427 ASGSRATIEGRIWRRDGVLIASCQQEALVRSKS 459
Cdd:PRK10526 254 ASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN 286
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
187-455 |
2.79e-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: 176.37 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 187 GAAYGGLIFSQALAAAEKTVDEQFkPHSMHSYFILNVDTkEPISYNVRRIRDGRSFITRTVEAVQKDKVCFVLQCSFHVE 266
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVPPDP-LHSLHVDFLRPVPP-GPVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 267 EKSSIIHQS-EMPKVPEPEVLMSMRDAVPYmkelvekgevTPPPAMLARLQSydskvysddqdlFEMRCTNLGNyyGFAS 345
Cdd:pfam13622 87 RSSEWELTPaAPPPLPPPEDCPLAADEAPF----------PLFRRVPGFLDP------------FEPRFARGGG--PFSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 346 DKKPELYFWMRARGDlsnDERFHRWLIAYNSDSLlvSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSR 425
Cdd:pfam13622 143 GGPGRVRLWVRLRDG---GEPDPLAALAYLADAF--PPRVLSLRLDPPASGWFPTLDLTVYFHR-RPPPGEWLLLRAETP 216
|
250 260 270
....*....|....*....|....*....|
gi 7496167 426 IASGSRATIEGRIWRRDGVLIASCQQEALV 455
Cdd:pfam13622 217 VAGDGRGDVEARLWDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
351-455 |
7.34e-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: 149.32 E-value: 7.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 351 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGS 430
Cdd:cd03444 1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLFDASASASLDHAIWFHR-PFRADDWLLYEQRSPRAGNG 79
|
90 100
....*....|....*....|....*
gi 7496167 431 RATIEGRIWRRDGVLIASCQQEALV 455
Cdd:cd03444 80 RGLVEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
171-265 |
1.87e-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: 137.37 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 171 DSFSPSTLSNGRQaHHGAAYGGLIFSQALAAAEKTVDEQFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAV 250
Cdd:cd03445 1 DRFRGVSPPVPPG-QGRGVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAV 79
|
90
....*....|....*
gi 7496167 251 QKDKVCFVLQCSFHV 265
Cdd:cd03445 80 QNGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
351-455 |
1.60e-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: 116.29 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 351 LYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHYTTGFCSsmlfsLDHCVWFHRSeVKADEWLLFECKSRIASGS 430
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGFAS-----LDHHIYFHRP-GDADEWLLYEVESLRDGRS 74
|
90 100
....*....|....*....|....*
gi 7496167 431 RATIEGRIWRRDGVLIASCQQEALV 455
Cdd:cd00556 75 RALRRGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
179-265 |
1.02e-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: 86.63 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 179 SNGRQAHHGAAYGGLIFSQALAAAEKTVDE-----QFKPHSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEAVQKD 253
Cdd:cd00556 7 APGPLPDDRRVFGGQLAAQSDLAALRTVPRphgasGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRGRAYQRD 86
|
90
....*....|...
gi 7496167 254 -KVCFVLQCSFHV 265
Cdd:cd00556 87 gKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
343-454 |
3.54e-20 |
|
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: 86.14 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 343 FASDKKPELYFWMRARGDLSNDERFHRWLIAYNSDSLLVSTAVSPHytTGFCSSMLFSLDHCVWFHRSeVKADEWLLFEC 422
Cdd:pfam02551 23 FGGQVVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPH--GFLCDGIQVSLDHSIYFHRP-GDLNKWILYDV 99
|
90 100 110
....*....|....*....|....*....|...
gi 7496167 423 KSRIASGSRATIEGRIWR-RDGVLIASCQQEAL 454
Cdd:pfam02551 100 ESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| SPK |
pfam04435 |
Domain of unknown function (DUF545); Family of uncharacterized C. elegans proteins. The region ... |
46-124 |
4.95e-16 |
|
Domain of unknown function (DUF545); Family of uncharacterized C. elegans proteins. The region represented by this family can is found to be repeated up to four time in some proteins.
Pssm-ID: 461308 Cd Length: 104 Bit Score: 73.71 E-value: 4.95e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7496167 46 FVAFVAKRYKDTTTPVPSKELYEGFKNKIKFKKHTDTLRKSIQPFLMGAFKDSDYDDEKKVQMLFVTSTPLkDGMFLEK 124
Cdd:pfam04435 1 LLKFLAEKTKNATEPLSLTQLCREFKEKTGSKLSVSTLRKRFRRILAKIHKLEEYDLETKVRMLFALSAPV-DEDFLKE 78
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
353-454 |
1.01e-07 |
|
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: 49.78 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 353 FWMRARGDLSNDERF-HRWLIAYNSDSLLVSTAvsphYTTGFCSSMLFSLDHCVWFHRsEVKADEWLLFECKSRIASGSR 431
Cdd:cd03440 3 LRLTVTPEDIDGGGIvHGGLLLALADEAAGAAA----ARLGGRGLGAVTLSLDVRFLR-PVRPGDTLTVEAEVVRVGRSS 77
|
90 100
....*....|....*....|...
gi 7496167 432 ATIEGRIWRRDGVLIASCQQEAL 454
Cdd:cd03440 78 VTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
185-263 |
6.25e-05 |
|
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: 42.08 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 185 HHGAAYGGLIFSQALAAAEKTVDEQFKP------HSMHSYFILNVDTKEPISYNVRRIRDGRSFITRTVEA-VQKDKVCF 257
Cdd:cd03440 14 GGGIVHGGLLLALADEAAGAAAARLGGRglgavtLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVrNEDGKLVA 93
|
....*.
gi 7496167 258 VLQCSF 263
Cdd:cd03440 94 TATATF 99
|
|
| SPK |
smart00583 |
domain in SET and PHD domain containing proteins and protein kinases; |
42-124 |
5.57e-03 |
|
domain in SET and PHD domain containing proteins and protein kinases;
Pssm-ID: 214732 Cd Length: 114 Bit Score: 36.77 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7496167 42 YIEQFVAFVAKRYKDTTTPV----PSKELYEGFKNKIKFKKHTdTLRKSIQPFLMGAFKDSDYDDEKKVQMLFVTSTPLK 117
Cdd:smart00583 1 ELTRFMDFLVEKTKDAIEPLvvplKVFEEFSKLEGNSLLSYET-YYKRFHNKLAPNMIKLNNYSIEERIRMMFALSGKVE 79
|
....*..
gi 7496167 118 DGmFLEK 124
Cdd:smart00583 80 DD-FLER 85
|
|
| |
