|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
1-413 |
0e+00 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 841.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 1 MNTESVVEFLGNVPLLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEFLLKQYD 80
Cdd:PLN02868 1 MNTESVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFLLKRYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 81 YFGVGLSGNVHSADIVAMSQLTCLVLPRDHCHLLETNSIWQSDTSLDKCSLVERILQLDPLELNIFRGITLPDAPIFGKV 160
Cdd:PLN02868 81 YFGYGLSGSVHSADVVAVSELTCLVLPHEHCHLLSPKSIWDSDKTPKDCSLVERILHLEPLEVDIFRGITLPDAPTFGKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 161 FGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKEQQG 240
Cdd:PLN02868 161 FGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 241 FEHQESTMPSVPDPDTLLSLEELRESRITDPHLPRSYRNKVATRNFVPWPIEIRFCEPSNSTNQTKSPPRLNYWFRAKGR 320
Cdd:PLN02868 241 FEHQESTMPHVPPPETLLSREELRERRLTDPRLPRSYRNKVAAKPFVPWPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 321 LSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQMFNRK 400
Cdd:PLN02868 321 LSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRK 400
|
410
....*....|...
gi 30678177 401 GELVVSLTQEALL 413
Cdd:PLN02868 401 GELVVSLTQEALL 413
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
139-414 |
2.33e-113 |
|
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: 333.17 E-value: 2.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 139 DPLELNIFRGITLPDAPIFGK-VFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRR 217
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNrTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 218 VDAVQKGNIIFILLASFQKEQQGFEHQeSTMPSVPDPD-TLLSLEELRESritDPHLPRSYRNKVatrNFVPWPIEIRFC 296
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQ-STMPKVPPPEsELPRENQLATK---YPATLPRFLKHV---VPFERPFEIRPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 297 EPSNSTNqTKSPPRLNYWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVK-SAALSLDHAMWFHRPLRADEW 375
Cdd:TIGR00189 154 NLLNYLG-GKEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFChSMAASLDHSIWFHRPFRADDW 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 30678177 376 LLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLR 414
Cdd:TIGR00189 233 LLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
134-415 |
5.78e-106 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 314.51 E-value: 5.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 134 RILQLDPLELNIFRGiTLPDAPIFGKVFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNF 213
Cdd:COG1946 7 DLLDLERLEDGLFRG-EISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 214 ATRRVDAVQKGNIIFILLASFQKEQQGFEHQEsTMPSVPDPDTLLSLEELResriTDPHLPRSYRNkvATRnfvpwPIEI 293
Cdd:COG1946 86 STRRVTAIQGGRVIFTATASFGVPEEGLEHQA-PMPDVPPPEDLPSLPELL----IAGVLPLRFFA--FLR-----PFDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 294 RFCEPSNSTNQTKSPPRLNYWFRAKGRLSDDQaLHRCVVAFASDLIFCGVGLNPHRRKGVKSAalSLDHAMWFHRPLRAD 373
Cdd:COG1946 154 RPVEGPLPFAPPSGEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLGPPLPAA--SLDHAMWFHRPFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30678177 374 EWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLRE 415
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRG 272
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
158-413 |
1.75e-49 |
|
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: 168.28 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 158 GKVFGGQFVGQALAAASKTVDfLKVVHSLHSYFLLVGDIDiPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKE 237
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVP-PDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 238 QQG-FEHQESTMPSVPDPDtllslEELRESRITDPHLPRSYRNKVAtrnfvpwPIEIRFCEPSNSTNQTkSPPRLNYWFR 316
Cdd:pfam13622 87 RSSeWELTPAAPPPLPPPE-----DCPLAADEAPFPLFRRVPGFLD-------PFEPRFARGGGPFSPG-GPGRVRLWVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 317 AKgrlSDDQALHRCVVAFASDlIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQM 396
Cdd:pfam13622 154 LR---DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229
|
250
....*....|....*..
gi 30678177 397 FNRKGELVVSLTQEALL 413
Cdd:pfam13622 230 WDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
313-413 |
1.43e-41 |
|
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: 142.39 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 313 YWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKG-VKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGF 391
Cdd:cd03444 3 VWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLfDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGRGL 82
|
90 100
....*....|....*....|..
gi 30678177 392 VTGQMFNRKGELVVSLTQEALL 413
Cdd:cd03444 83 VEGRIFTRDGELVASVAQEGLL 104
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
15-115 |
1.36e-10 |
|
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.
Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 58.57 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 15 LLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEF-LLKQYDYFGV-GLSGNVHS 92
Cdd:smart00100 1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVgTLGPGDFFGElALLTNSRR 80
|
90 100
....*....|....*....|....
gi 30678177 93 ADIVAMSQLTCLVLPR-DHCHLLE 115
Cdd:smart00100 81 AASAAAVALELATLLRiDFRDFLQ 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02868 |
PLN02868 |
acyl-CoA thioesterase family protein |
1-413 |
0e+00 |
|
acyl-CoA thioesterase family protein
Pssm-ID: 178459 [Multi-domain] Cd Length: 413 Bit Score: 841.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 1 MNTESVVEFLGNVPLLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEFLLKQYD 80
Cdd:PLN02868 1 MNTESVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFLLKRYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 81 YFGVGLSGNVHSADIVAMSQLTCLVLPRDHCHLLETNSIWQSDTSLDKCSLVERILQLDPLELNIFRGITLPDAPIFGKV 160
Cdd:PLN02868 81 YFGYGLSGSVHSADVVAVSELTCLVLPHEHCHLLSPKSIWDSDKTPKDCSLVERILHLEPLEVDIFRGITLPDAPTFGKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 161 FGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKEQQG 240
Cdd:PLN02868 161 FGGQLVGQALAAASKTVDPLKLVHSLHAYFLLVGDINLPIIYQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 241 FEHQESTMPSVPDPDTLLSLEELRESRITDPHLPRSYRNKVATRNFVPWPIEIRFCEPSNSTNQTKSPPRLNYWFRAKGR 320
Cdd:PLN02868 241 FEHQESTMPHVPPPETLLSREELRERRLTDPRLPRSYRNKVAAKPFVPWPIEIRFCEPNNSTNQTKSPPRLRYWFRAKGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 321 LSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQMFNRK 400
Cdd:PLN02868 321 LSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLKFAALSLDHSMWFHRPFRADDWLLFVIVSPAAHNGRGFATGHMFNRK 400
|
410
....*....|...
gi 30678177 401 GELVVSLTQEALL 413
Cdd:PLN02868 401 GELVVSLTQEALL 413
|
|
| tesB |
TIGR00189 |
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ... |
139-414 |
2.33e-113 |
|
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: 333.17 E-value: 2.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 139 DPLELNIFRGITLPDAPIFGK-VFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRR 217
Cdd:TIGR00189 1 EKIDENLFRGSHLSKGRQFLNrTFGGQVVGQALAAASKTVPEEFIPHSLHSYFVRAGDPKKPIIYDVERLRDGRSFITRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 218 VDAVQKGNIIFILLASFQKEQQGFEHQeSTMPSVPDPD-TLLSLEELRESritDPHLPRSYRNKVatrNFVPWPIEIRFC 296
Cdd:TIGR00189 81 VKAVQHGKTIFTLQASFQAEKSGIEHQ-STMPKVPPPEsELPRENQLATK---YPATLPRFLKHV---VPFERPFEIRPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 297 EPSNSTNqTKSPPRLNYWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVK-SAALSLDHAMWFHRPLRADEW 375
Cdd:TIGR00189 154 NLLNYLG-GKEDPPQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFChSMAASLDHSIWFHRPFRADDW 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 30678177 376 LLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLR 414
Cdd:TIGR00189 233 LLYKCSSPSAGGSRGLVEGKIFTRDGVLIASVVQEGLVR 271
|
|
| TesB |
COG1946 |
Acyl-CoA thioesterase [Lipid transport and metabolism]; |
134-415 |
5.78e-106 |
|
Acyl-CoA thioesterase [Lipid transport and metabolism];
Pssm-ID: 441549 [Multi-domain] Cd Length: 273 Bit Score: 314.51 E-value: 5.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 134 RILQLDPLELNIFRGiTLPDAPIFGKVFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNF 213
Cdd:COG1946 7 DLLDLERLEDGLFRG-EISPDQGLRRVFGGQVAAQALRAARRTVPEDRPPHSLHAYFLRPGDPDGPIEYEVERLRDGRSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 214 ATRRVDAVQKGNIIFILLASFQKEQQGFEHQEsTMPSVPDPDTLLSLEELResriTDPHLPRSYRNkvATRnfvpwPIEI 293
Cdd:COG1946 86 STRRVTAIQGGRVIFTATASFGVPEEGLEHQA-PMPDVPPPEDLPSLPELL----IAGVLPLRFFA--FLR-----PFDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 294 RFCEPSNSTNQTKSPPRLNYWFRAKGRLSDDQaLHRCVVAFASDLIFCGVGLNPHRRKGVKSAalSLDHAMWFHRPLRAD 373
Cdd:COG1946 154 RPVEGPLPFAPPSGEPRQRVWMRARDPLPDDP-LHAALLAYASDATPPATALLSWLGPPLPAA--SLDHAMWFHRPFRAD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30678177 374 EWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLRE 415
Cdd:COG1946 231 DWLLYDADSPSASGGRGLERGRIWDRDGRLVASSRQEGLVRG 272
|
|
| PRK10526 |
PRK10526 |
acyl-CoA thioesterase II; Provisional |
135-414 |
8.01e-81 |
|
acyl-CoA thioesterase II; Provisional
Pssm-ID: 182519 [Multi-domain] Cd Length: 286 Bit Score: 250.82 E-value: 8.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 135 ILQLDPLELNIFRGitlpDAPIFG--KVFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNN 212
Cdd:PRK10526 11 LLNLEKIEEGLFRG----QSEDLGlrQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSQKPIIYDVETLRDGNS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 213 FATRRVDAVQKGNIIFILLASFQKEQQGFEHQeSTMPSVPDPDTLLSLEELreSRITDPHLPRSYRNKVATRNfvpwPIE 292
Cdd:PRK10526 87 FSARRVAAIQNGKPIFYMTASFQAPEAGFEHQ-KTMPSAPAPDGLPSETDI--AQSLAHLLPPVLKDKFICDR----PLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 293 IRFCEPSNSTNQTKSPPRLNYWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPH----RRKGVKSAalSLDHAMWFHR 368
Cdd:PRK10526 160 IRPVEFHNPLKGHVAEPVRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHgigfLEPGMQIA--TIDHSMWFHR 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 30678177 369 PLRADEWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLR 414
Cdd:PRK10526 238 PFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMR 283
|
|
| 4HBT_3 |
pfam13622 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
158-413 |
1.75e-49 |
|
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: 168.28 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 158 GKVFGGQFVGQALAAASKTVDfLKVVHSLHSYFLLVGDIDiPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKE 237
Cdd:pfam13622 9 RAPHGGYVAALLLRAAERTVP-PDPLHSLHVDFLRPVPPG-PVTIRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 238 QQG-FEHQESTMPSVPDPDtllslEELRESRITDPHLPRSYRNKVAtrnfvpwPIEIRFCEPSNSTNQTkSPPRLNYWFR 316
Cdd:pfam13622 87 RSSeWELTPAAPPPLPPPE-----DCPLAADEAPFPLFRRVPGFLD-------PFEPRFARGGGPFSPG-GPGRVRLWVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 317 AKgrlSDDQALHRCVVAFASDlIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQM 396
Cdd:pfam13622 154 LR---DGGEPDPLAALAYLAD-AFPPRVLSLRLDPPASGWFPTLDLTVYFHRRPPPGEWLLLRAETPVAGDGRGDVEARL 229
|
250
....*....|....*..
gi 30678177 397 FNRKGELVVSLTQEALL 413
Cdd:pfam13622 230 WDEDGRLVATSRQEVLV 246
|
|
| Thioesterase_II_repeat1 |
cd03444 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
313-413 |
1.43e-41 |
|
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: 142.39 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 313 YWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKG-VKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGF 391
Cdd:cd03444 3 VWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPLfDASASASLDHAIWFHRPFRADDWLLYEQRSPRAGNGRGL 82
|
90 100
....*....|....*....|..
gi 30678177 392 VTGQMFNRKGELVVSLTQEALL 413
Cdd:cd03444 83 VEGRIFTRDGELVASVAQEGLL 104
|
|
| Thioesterase_II_repeat2 |
cd03445 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
144-236 |
2.27e-41 |
|
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: 141.60 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 144 NIFRGITLPDAPIFGK-VFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRVDAVQ 222
Cdd:cd03445 1 DRFRGVSPPVPPGQGRgVFGGQVLAQALVAAARTVPDDRVPHSLHSYFLRPGDPDQPIEYEVERLRDGRSFATRRVRAVQ 80
|
90
....*....|....
gi 30678177 223 KGNIIFILLASFQK 236
Cdd:cd03445 81 NGKVIFTATASFQR 94
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
313-413 |
1.88e-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: 238311 [Multi-domain] Cd Length: 99 Bit Score: 110.13 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 313 YWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRkgvkSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFV 392
Cdd:cd00556 3 FWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGA----SGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALR 78
|
90 100
....*....|....*....|.
gi 30678177 393 TGQMFNRKGELVVSLTQEALL 413
Cdd:cd00556 79 RGRAYQRDGKLVASATQSFLV 99
|
|
| Thioesterase_II |
cd00556 |
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ... |
144-236 |
3.47e-23 |
|
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: 93.18 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 144 NIFRGITLPDAPIFGKVFGGQFVGQALAAASKTVD-----FLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRV 218
Cdd:cd00556 1 DRFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPrphgaSGFASLDHHIYFHRPGDADEWLLYEVESLRDGRSRALRRG 80
|
90
....*....|....*....
gi 30678177 219 DAVQK-GNIIFILLASFQK 236
Cdd:cd00556 81 RAYQRdGKLVASATQSFLV 99
|
|
| Acyl_CoA_thio |
pfam02551 |
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ... |
290-412 |
2.16e-22 |
|
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: 92.31 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 290 PIEIRFCEPSNSTNQTKSPPRLNY---WFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRrKGVKSAALSLDHAMWF 366
Cdd:pfam02551 7 RGEYPVAVRPGELRRTFGGQVVAHqqsWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHG-FLCDGIQVSLDHSIYF 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 30678177 367 HRPLRADEWLLYVIVSPTAHETRGFVTGQMFN-RKGELVVSLTQEAL 412
Cdd:pfam02551 86 HRPGDLNKWILYDVESPSASGGRGLRQGRNFStQSGKLIASVQQEGL 132
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
15-117 |
2.09e-15 |
|
effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels
Pssm-ID: 237999 [Multi-domain] Cd Length: 115 Bit Score: 71.97 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 15 LLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSE-FLLKQYDYFGVG--LSGNVH 91
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvGFLGPGDLFGELalLGNGPR 80
|
90 100
....*....|....*....|....*..
gi 30678177 92 SADIVAMSQLTCLVLPRDH-CHLLETN 117
Cdd:cd00038 81 SATVRALTDSELLVLPRSDfRRLLQEY 107
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
33-110 |
3.66e-12 |
|
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 61.86 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 33 PKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEF-LLKQYDYFGVG--LSGNVHSADIVAMSQLTCLVLPRD 109
Cdd:pfam00027 1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILaVLGPGDFFGELalLGGEPRSATVVALTDSELLVIPRE 80
|
.
gi 30678177 110 H 110
Cdd:pfam00027 81 D 81
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
16-121 |
1.98e-11 |
|
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];
Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 63.08 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 16 LQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEF-LLKQYDYFGVG--LSGNVHS 92
Cdd:COG0664 1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILgFLGPGDFFGELslLGGEPSP 80
|
90 100 110
....*....|....*....|....*....|
gi 30678177 93 ADIVAMSQLTCLVLPRDHCH-LLETNSIWQ 121
Cdd:COG0664 81 ATAEALEDSELLRIPREDLEeLLERNPELA 110
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
15-115 |
1.36e-10 |
|
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.
Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 58.57 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678177 15 LLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEF-LLKQYDYFGV-GLSGNVHS 92
Cdd:smart00100 1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVgTLGPGDFFGElALLTNSRR 80
|
90 100
....*....|....*....|....
gi 30678177 93 ADIVAMSQLTCLVLPR-DHCHLLE 115
Cdd:smart00100 81 AASAAAVALELATLLRiDFRDFLQ 104
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
354-412 |
4.08e-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: 42.46 E-value: 4.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 30678177 354 KSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEAL 412
Cdd:cd03440 42 GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATFV 100
|
|
| |
