|
Name |
Accession |
Description |
Interval |
E-value |
| ECH_1 |
pfam00378 |
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ... |
35-280 |
6.50e-43 |
|
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.
Pssm-ID: 395302 [Multi-domain] Cd Length: 251 Bit Score: 147.12 E-value: 6.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSaSSNVFSAGLDIFEMYNTDVERLRTVWTELQNVWIA 112
Cdd:pfam00378 5 GVAVITLNRPeAVNALSAELITELIQALEKLRTDPSvRAVVLTG-GDKAFCAGADLKEMYGEGPAHQALYRENVLDLWTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 113 LYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQGRMFTTQE 192
Cdd:pfam00378 84 LYTCPKPVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 193 AFEVGLIDEIAsSKEEALEKCAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMIREKDIADFVALASSPGVQKVMGAYLE 272
Cdd:pfam00378 164 ALKWGLVDKVV-PEDQLLDEARELAEKLAEKSPAALAQLKKALNAKLEDALPTQLEAEARLFYSTFSKDDIIEGLQAFLE 242
|
....*...
gi 19921018 273 NLKNKVKK 280
Cdd:pfam00378 243 KRKPPWED 250
|
|
| PLN03214 |
PLN03214 |
probable enoyl-CoA hydratase/isomerase; Provisional |
20-280 |
4.96e-42 |
|
probable enoyl-CoA hydratase/isomerase; Provisional
Pssm-ID: 215635 Cd Length: 278 Bit Score: 145.41 E-value: 4.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 20 STATKLTTVEINDKtGIATLTMNRPPVNSQNVQLLLDLQTSISEIENNKS-RGLILTSA-SSNVFSAGLDIFEMY--NTD 95
Cdd:PLN03214 7 PGATPGVRVDRRPG-GIAVVWLAKEPVNSMTLAMWRSLDDALTALENDPTvRGVVFASGlRRDVFTAGNDIAELYapKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 96 VERLRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPK-WLMSGFASILP 174
Cdd:PLN03214 86 AARYAEFWLTQTTFLVRLLRSRLATVCAIRGACPAGGCAVSLCCDYRLQTTEGTMGLNEVALGIPVPKfWARLFMGRVID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 175 KRVAERALTQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMIREKDIADF 254
Cdd:PLN03214 166 RKVAESLLLRGRLVRPAEAKQLGLIDEVVPA-AALMEAAASAMERALKLPSAARAATKALLREEFSAAWEAYYEEEAKGG 244
|
250 260
....*....|....*....|....*.
gi 19921018 255 VALASSPGVQKVMGAYLENLKNKVKK 280
Cdd:PLN03214 245 WKMLSEPSIIKALGGVMERLSSGKEK 270
|
|
| crotonase-like |
cd06558 |
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ... |
27-217 |
7.03e-42 |
|
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.
Pssm-ID: 119339 [Multi-domain] Cd Length: 195 Bit Score: 142.31 E-value: 7.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDktGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILTSASsNVFSAGLDIFEMYN--TDVERLRTV 102
Cdd:cd06558 2 LVERDG--GVATITLNRPEkRNALSLEMLDELAAALDEAEADPDvRVVVLTGAG-KAFCAGADLKELAAlsDAGEEARAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 103 WTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERAL 182
Cdd:cd06558 79 IRELQELLRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARARELL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 19921018 183 TQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFI 217
Cdd:cd06558 159 LTGRRISAEEALELGLVDEVVPD-EELLAAALELA 192
|
|
| CaiD |
COG1024 |
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ... |
27-272 |
2.00e-40 |
|
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440647 [Multi-domain] Cd Length: 249 Bit Score: 140.30 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDktGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSnVFSAGLDIFEMY-NTDVERLRTVW 103
Cdd:COG1024 2 LVEREG--GVATITLNRPeKLNALSLEMLAELAAALDEAEADPDvRVVVLTGAGK-AFCAGADLKELAaAADPEEARAFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 104 TELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPkwlmSGFASILPKRVAER--- 180
Cdd:COG1024 79 RGLQRLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPG----GGGTQRLPRLVGLArak 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 181 --ALTqGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMIREKDIADFVALA 258
Cdd:COG1024 155 elLLT-GRRIDAEEALELGLVNRVVPD-DELLAAALALAARLAAGPPLALAATKRALNAALEAPLDEALELEAEAFAELF 232
|
250
....*....|....
gi 19921018 259 SSPGVQKVMGAYLE 272
Cdd:COG1024 233 ASEDAREGIAAFLE 246
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
35-214 |
2.75e-23 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 99.17 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSnVFSAGLDIFE---MYNTDVERLRTVWTELQNV 109
Cdd:PRK11730 16 GIAELVFDAPgSVNKLDRATLASLGEALDALEAQSDlKGLLLTSAKD-AFIVGADITEflsLFAAPEEELSQWLHFANSI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 110 WIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIiapkwlMSGFASI--LPkRV--AERAL--- 182
Cdd:PRK11730 95 FNRLEDLPVPTVAAINGYALGGGCECVLATDYRVASPDARIGLPETKLGI------MPGFGGTvrLP-RLigADNALewi 167
|
170 180 190
....*....|....*....|....*....|..
gi 19921018 183 TQGRMFTTQEAFEVGLIDEIASSkeEALEKCA 214
Cdd:PRK11730 168 AAGKDVRAEDALKVGAVDAVVAP--EKLQEAA 197
|
|
| PRK07658 |
PRK07658 |
enoyl-CoA hydratase; Provisional |
24-227 |
3.92e-23 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181070 [Multi-domain] Cd Length: 257 Bit Score: 95.09 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 24 KLTTVEINDktGIATLTMNRPPVNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMynTDVERLRTvW 103
Cdd:PRK07658 2 KFLSVRVED--HVAVITLNHPPANALSSQVLHELSELLDQVEKDDNVRVVVIHGEGRFFSAGADIKEF--TSVTEAEQ-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 104 TEL----QNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIapkwlmSGFASI--LPKRV 177
Cdd:PRK07658 77 TELaqlgQVTFERVEKFSKPVIAAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLI------PGFAGTqrLPRYV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19921018 178 -----AERALTqGRMFTTQEAFEVGLIDEiASSKEEALEKCAAFIGTFAKVNPLA 227
Cdd:PRK07658 151 gkakaLEMMLT-SEPITGAEALKWGLVNG-VFPEETLLDDAKKLAKKIAGKSPAT 203
|
|
| PRK05809 |
PRK05809 |
short-chain-enoyl-CoA hydratase; |
25-232 |
5.21e-22 |
|
short-chain-enoyl-CoA hydratase;
Pssm-ID: 180270 [Multi-domain] Cd Length: 260 Bit Score: 92.12 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 25 LTTVEINDKTGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIFEMYNTDVERLRTV 102
Cdd:PRK05809 3 LKNVILEKEGHIAVVTINRPkALNALNSETLKELDTVLDDIENDDNvYAVILTGAGEKAFVAGADISEMKDLNEEEGRKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 103 WTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIapkwlmSGFASI--LPKRV--- 177
Cdd:PRK05809 83 GLLGNKVFRKLENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGIT------PGFGGTqrLARIVgpg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19921018 178 -AERALTQGRMFTTQEAFEVGLIDEIAsSKEEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PRK05809 157 kAKELIYTGDMINAEEALRIGLVNKVV-EPEKLMEEAKALANKIAANAPIAVKLCK 211
|
|
| PRK07657 |
PRK07657 |
enoyl-CoA hydratase; Provisional |
19-232 |
5.47e-22 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181069 [Multi-domain] Cd Length: 260 Bit Score: 92.10 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEindkTGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIFEMYNTDV 96
Cdd:PRK07657 1 MLQNISVDYVT----PHVVKITLNRPrAANALSLALLEELQNILTQINEEANvRVVILTGAGEKAFCAGADLKERAGMNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 97 ERLRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPkwlmSGFASILPKR 176
Cdd:PRK07657 77 EQVRHAVSLIRTTMEMVEQLPQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPG----AGGTQRLPRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 177 V----AERALTQGRMFTTQEAFEVGLIdEIASSKEEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PRK07657 153 IgvgrAKELIYTGRRISAQEAKEIGLV-EFVVPAHLLEEKAIEIAEKIASNGPIAVRQAK 211
|
|
| PRK06213 |
PRK06213 |
crotonase/enoyl-CoA hydratase family protein; |
23-254 |
5.25e-18 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 235744 Cd Length: 229 Bit Score: 80.40 E-value: 5.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 23 TKLTTVEINDktGIATLTMNRPPVNSQNVQLLLDLQTSISEIENNksRGLILTSASSNVFSAGLDIFEMYNTDVERLRTV 102
Cdd:PRK06213 2 SELVSYTLED--GVATITLDDGKVNALSPAMIDALNAALDQAEDD--RAVVVITGQPGIFSGGFDLKVMTSGAQAAIALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 103 wTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRV-MRPNFLIGLNEAQLGIIAPkwlmsgFASI------LPK 175
Cdd:PRK06213 78 -TAGSTLARRLLSHPKPVIVACTGHAIAKGAFLLLSADYRIgVHGPFKIGLNEVAIGMTMP------HAAIelardrLTP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921018 176 RVAERALTQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMIREKDIADF 254
Cdd:PRK06213 151 SAFQRAVINAEMFDPEEAVAAGFLDEVVPP-EQLLARAQAAARELAGLNMGAHAATKLKVRAAALEAIRAAIEGDAAEF 228
|
|
| PRK06688 |
PRK06688 |
enoyl-CoA hydratase; Provisional |
20-272 |
1.60e-17 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235852 [Multi-domain] Cd Length: 259 Bit Score: 79.91 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 20 STATKLTTVEINDktGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDIFEMYN---T 94
Cdd:PRK06688 1 MTMVTDLLVELED--GVLTITINRPdKKNALTAAMYQALADALEAAATDPAvRVVVLTGAGRA-FSAGGDIKDFPKappK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 95 DVERLRTVWTELQnvwiALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiiapkwLMSGFAS--- 171
Cdd:PRK06688 78 PPDELAPVNRFLR----AIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLG------LCPDAGGsal 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 172 ----ILPKRVAERALTqGRMFTTQEAFEVGLIDEIAsSKEEALEKCAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMIR 247
Cdd:PRK06688 148 lprlIGRARAAEMLLL-GEPLSAEEALRIGLVNRVV-PAAELDAEADAQAAKLAAGPASALRYTKRAINAATLTELEEAL 225
|
250 260
....*....|....*....|....*
gi 19921018 248 EKDIADFVALASSPGVQKVMGAYLE 272
Cdd:PRK06688 226 AREAAGFGRLLRTPDFREGATAFIE 250
|
|
| PRK05995 |
PRK05995 |
enoyl-CoA hydratase; Provisional |
26-227 |
2.02e-17 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235664 [Multi-domain] Cd Length: 262 Bit Score: 79.58 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 26 TTVEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTsASSNVFSAGLDIFEM---YNTDVERLR 100
Cdd:PRK05995 4 ETLEIEQRGQVATVTLNRPDVrNAFNETVIAELTAAFRALDADDSvRAVVLA-GAGKAFCAGADLNWMkkmAGYSDDENR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 101 TVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKWLMSGFASILPKRVAER 180
Cdd:PRK05995 83 ADARRLADMLRAIYRCPKPVIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLI-PATISPYVIRAMGERAARR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19921018 181 ALTQGRMFTTQEAFEVGLIDEIASskEEAL-EKCAAFIGTFAKVNPLA 227
Cdd:PRK05995 162 YFLTAERFDAAEALRLGLVHEVVP--AEALdAKVDELLAALVANSPQA 207
|
|
| PLN02600 |
PLN02600 |
enoyl-CoA hydratase |
32-232 |
3.48e-17 |
|
enoyl-CoA hydratase
Pssm-ID: 178210 [Multi-domain] Cd Length: 251 Bit Score: 78.69 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 32 DKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIFEMYNTDVERLRTVWTELQNV 109
Cdd:PLN02600 1 PDSGIVELRLDRPEAkNAIGKEMLRGLRSAFEKIQADASaRVVMLRSSVPGVFCAGADLKERRKMSPSEVQKFVNSLRST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 110 WIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQGRMFT 189
Cdd:PLN02600 81 FSSLEALSIPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19921018 190 TQEAFEVGLIdEIASSKEEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PLN02600 161 AREAASMGLV-NYCVPAGEAYEKALELAQEINQKGPLAIKMAK 202
|
|
| PRK07659 |
PRK07659 |
enoyl-CoA hydratase; Provisional |
23-205 |
1.83e-15 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236073 [Multi-domain] Cd Length: 260 Bit Score: 74.30 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 23 TKLTTVEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILtSASSNVFSAGLDIFEMYN-TDVERLR 100
Cdd:PRK07659 3 SKMESVVVKYEGRVATIMLNRPEAlNALDEPMLKELLQALKEVAESSAHIVVL-RGNGRGFSAGGDIKMMLSsNDESKFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 101 TVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKwlmSGFASILPKRVAER 180
Cdd:PRK07659 82 GVMNTISEIVVTLYTMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLI-PD---GGGHFFLQKRVGEN 157
|
170 180
....*....|....*....|....*....
gi 19921018 181 ALTQ----GRMFTTQEAFEVGLIDEIASS 205
Cdd:PRK07659 158 KAKQiiweGKKLSATEALDLGLIDEVIGG 186
|
|
| PRK07509 |
PRK07509 |
crotonase/enoyl-CoA hydratase family protein; |
27-217 |
6.26e-15 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181008 [Multi-domain] Cd Length: 262 Bit Score: 72.61 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDktGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDIFEMYNTDVERLRTVWT 104
Cdd:PRK07509 6 SVTIED--GIADVRLNRPdKMNALDFAMFEELIATIKRLKKDRGiRAVILSGEGGA-FCAGLDVKSVASSPGNAVKLLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 105 EL---QN-------VWIALygtTLPTAAAINGHAPAGGCLLATACEYRVMRPnfliglnEAQLGIIAPKW-------LMS 167
Cdd:PRK07509 83 RLpgnANlaqrvslGWRRL---PVPVIAALEGVCFGGGLQIALGADIRIAAP-------DTKLSIMEAKWglvpdmaGTV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19921018 168 GFASILPKRVA-ERALTqGRMFTTQEAFEVGLIDEIASSKEEALEKCAAFI 217
Cdd:PRK07509 153 SLRGLVRKDVArELTYT-ARVFSAEEALELGLVTHVSDDPLAAALALAREI 202
|
|
| PRK09674 |
PRK09674 |
enoyl-CoA hydratase-isomerase; Provisional |
35-232 |
1.07e-14 |
|
enoyl-CoA hydratase-isomerase; Provisional
Pssm-ID: 182026 [Multi-domain] Cd Length: 255 Bit Score: 72.11 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYNTDVerLRTVWTELQNVWIAL 113
Cdd:PRK09674 11 RVLLLTLNRPEArNALNNALLTQLVNELEAAATDTSIGVCVITGNARFFAAGADLNEMAEKDL--AATLNDPRPQLWQRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 114 YGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQGRMFTTQEA 193
Cdd:PRK09674 89 QAFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASQMVLTGESITAQQA 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 19921018 194 FEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PRK09674 169 QQAGLVSEVFPP-ELTLERALQLASKIARHSPLALRAAK 206
|
|
| PRK05980 |
PRK05980 |
crotonase/enoyl-CoA hydratase family protein; |
27-272 |
1.17e-14 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180335 [Multi-domain] Cd Length: 260 Bit Score: 71.71 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDKTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIFEmYNTDVER-----L 99
Cdd:PRK05980 4 TVLIEIRDGIALLTLNRPEkLNALNYALIDRLLARLDAIEVDESvRAVILTGAGDRAFSAGADIHE-FSASVAAgadvaL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 100 RTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPkwlmSGFASILP----- 174
Cdd:PRK05980 83 RDFVRRGQAMTARLEAFPKPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPT----FGGTQRLPrlagr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 175 KRVAERALTqGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLA-RGLTKLQFRGDNIKEFEMIrEKDIAD 253
Cdd:PRK05980 159 KRALELLLT-GDAFSAERALEIGLVNAVVPH-EELLPAARALARRIIRHSPVAvAAILTAVTRGLNLSIAEGL-LIESEQ 235
|
250
....*....|....*....
gi 19921018 254 FVALASSPGVQKVMGAYLE 272
Cdd:PRK05980 236 FARMAGSADLREGLAAWIE 254
|
|
| PRK08138 |
PRK08138 |
enoyl-CoA hydratase; Provisional |
35-227 |
1.84e-14 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236162 [Multi-domain] Cd Length: 261 Bit Score: 71.24 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDI--------FEMYNTDVERLrtvwte 105
Cdd:PRK08138 17 GVALLRLNRPEArNALNMEVRQQLAEHFTELSEDPDIRAIVLTGGEKVFAAGADIkefatagaIEMYLRHTERY------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 lqnvWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIiapkwlMSG------FASILPKRVAE 179
Cdd:PRK08138 91 ----WEAIAQCPKPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGL------MPGaggtqrLVRAVGKFKAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19921018 180 RALTQGRMFTTQEAFEVGLIDEIaSSKEEALEKCAAFIGTFAKVNPLA 227
Cdd:PRK08138 161 RMALTGCMVPAPEALAIGLVSEV-VEDEQTLPRALELAREIARMPPLA 207
|
|
| PRK05869 |
PRK05869 |
enoyl-CoA hydratase; Validated |
19-237 |
2.55e-14 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 235632 [Multi-domain] Cd Length: 222 Bit Score: 70.25 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEINDKTGIATLTMNRPPVNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYNTDVER 98
Cdd:PRK05869 1 MNEFVNVVVSDGSQDAGLATLLLSRPPTNALTRQVYREIVAAANELGRRDDVAAVILYGGHEIFSAGDDMPELRTLSAQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 99 LRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVA 178
Cdd:PRK05869 81 ADTAARVRQQAVDAVAAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19921018 179 ERALTQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTKLQFRG 237
Cdd:PRK05869 161 KELVFSGRFFDAEEALALGLIDEMVAP-DDVYDAAAAWARRFLDGPPHALAAAKAGISD 218
|
|
| PLN02267 |
PLN02267 |
enoyl-CoA hydratase/isomerase family protein |
50-211 |
4.76e-14 |
|
enoyl-CoA hydratase/isomerase family protein
Pssm-ID: 215151 Cd Length: 239 Bit Score: 69.74 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 50 NVQLLLDLQTSISEIENNKSRGLIL-TSASSNVFSAGLDI--FEMYNTDVERLRTVWTELQNVWIALYGTTLPTAAAING 126
Cdd:PLN02267 24 NPTLIDSIRSALRQVKSQATPGSVLiTTAEGKFFSNGFDLawAQAAGSAPSRLHLMVAKLRPLVADLISLPMPTIAAVTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 127 HAPAGGCLLATACEYRVMRPN--FLIgLNEAQLGIIAPKWLMSGF-ASILPKRVAERALTQGRMFTTQEAFEVGLIDEIA 203
Cdd:PLN02267 104 HASAAGFILALSHDYVLMRKDrgVLY-MSEVDIGLPLPDYFMALLrAKIGSPAARRDVLLRAAKLTAEEAVEMGIVDSAH 182
|
....*...
gi 19921018 204 SSKEEALE 211
Cdd:PLN02267 183 DSAEETVE 190
|
|
| PLN02664 |
PLN02664 |
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase |
19-232 |
1.43e-13 |
|
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
Pssm-ID: 178269 [Multi-domain] Cd Length: 275 Bit Score: 69.16 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEINDKTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDI--FEMYNTD 95
Cdd:PLN02664 1 MESYKTLEIIQKSPNSSVFHLNLNRPSqRNALSLDFFTEFPKALSSLDQNPNVSVIILSGAGDHFCSGIDLktLNSISEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 96 V---------ERLRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLM 166
Cdd:PLN02664 81 SssgdrgrsgERLRRKIKFLQDAITAIEQCRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921018 167 SGFASILPKRVA-ERALTqGRMFTTQEAFEVGLIDEIASSKEEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PLN02664 161 QRLPSIVGYGNAmELALT-GRRFSGSEAKELGLVSRVFGSKEDLDEGVRLIAEGIAAKSPLAVTGTK 226
|
|
| PRK06494 |
PRK06494 |
enoyl-CoA hydratase; Provisional |
33-227 |
2.60e-13 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180591 [Multi-domain] Cd Length: 259 Bit Score: 68.14 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 33 KTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENN-KSRGLILTSASSNVFSAGLDIFEMyntdVERLRTVWTE----- 105
Cdd:PRK06494 11 KGHVTIVTLNRPEVmNALHLDAHFELEEVFDDFAADpEQWVAIVTGAGDKAFSAGNDLKEQ----AAGGKRGWPEsgfgg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQnvwiALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQG 185
Cdd:PRK06494 87 LT----SRFDLDKPIIAAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19921018 186 RMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLA 227
Cdd:PRK06494 163 RRVTAREGLELGFVNEVVPA-GELLAAAERWADDILACSPLS 203
|
|
| PRK07827 |
PRK07827 |
enoyl-CoA hydratase family protein; |
19-272 |
4.36e-13 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 236109 [Multi-domain] Cd Length: 260 Bit Score: 67.40 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEINDktGIATLTMNRPP-VNSQNVQLLLDLQTSISEI-ENNKSRGLILTSaSSNVFSAGLDIFE------ 90
Cdd:PRK07827 1 DTPVDTLVRYAVDG--GVATLTLDSPHnRNALSARLVAQLHDGLRAAaADPAVRAVVLTH-TGGTFCAGADLSEaggggg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 91 -MYNTDVERLRTVWTELQnvwiALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiIAPKwLMSgf 169
Cdd:PRK07827 78 dPYDAAVARAREMTALLR----AIVELPKPVIAAIDGHVRAGGFGLVGACDIVVAGPESTFALTEARIG-VAPA-IIS-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 170 ASILPK---RVAERALTQGRMFTTQEAFEVGLIDEIASSKEEALekcAAFIGTFAKVNPLARGLTKLQFRGDNIKEFEMI 246
Cdd:PRK07827 150 LTLLPRlspRAAARYYLTGEKFGAAEAARIGLVTAAADDVDAAV---AALLADLRRGSPQGLAESKALTTAAVLAGFDRD 226
|
250 260
....*....|....*....|....*.
gi 19921018 247 REKDIADFVALASSPGVQKVMGAYLE 272
Cdd:PRK07827 227 AEELTEESARLFVSDEAREGMTAFLQ 252
|
|
| PRK07854 |
PRK07854 |
enoyl-CoA hydratase; Provisional |
28-227 |
5.48e-13 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236115 [Multi-domain] Cd Length: 243 Bit Score: 66.97 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 28 VEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSnVFSAGLDI-FEMYNTDVerlrtvWTE 105
Cdd:PRK07854 2 IGVTRDGQVLTIELQRPERrNALNAELCEELREAVRKAVDESARAIVLTGQGT-VFCAGADLsGDVYADDF------PDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQG 185
Cdd:PRK07854 75 LIEMLHAIDAAPVPVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19921018 186 RMFTTQEAFEVGLIDEIASSKEEalEKCAAFIGTFAkvnPLA 227
Cdd:PRK07854 155 EKLTAEQALATGMANRIGTLADA--QAWAAEIAGLA---PLA 191
|
|
| PRK06144 |
PRK06144 |
enoyl-CoA hydratase; Provisional |
19-236 |
1.30e-12 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180424 [Multi-domain] Cd Length: 262 Bit Score: 66.17 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEINDktGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDI--FEMYNT 94
Cdd:PRK06144 3 MTTSTDELLLEVRG--GIARITFNRPAArNAMTWAMYEGLAEICEAIAADPSiRAVVLRGAGDKAFVAGTDIaqFRAFST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 95 -----DVERlrtvwtELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRvmrpnflIGLNEAQLGIIAPKWL---- 165
Cdd:PRK06144 81 aedavAYER------RIDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLR-------IATPSARFGFPIARTLgncl 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921018 166 -MSGFASIL----PKRVAERALTqGRMFTTQEAFEVGLIDEI--ASSKEEALEKCAAFIGTFAkvnPLARGLTKLQFR 236
Cdd:PRK06144 148 sMSNLARLVallgAARVKDMLFT-ARLLEAEEALAAGLVNEVveDAALDARADALAELLAAHA---PLTLRATKEALR 221
|
|
| PRK06495 |
PRK06495 |
enoyl-CoA hydratase/isomerase family protein; |
27-272 |
1.56e-11 |
|
enoyl-CoA hydratase/isomerase family protein;
Pssm-ID: 168580 [Multi-domain] Cd Length: 257 Bit Score: 62.79 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDktGIATLTMNRPPVNSQNVQLLLDLQTSISEI-ENNKSRGLILTSAsSNVFSAGLDIFEMYNTDVE----RLRT 101
Cdd:PRK06495 7 KLEVSD--HVAVVTLDNPPVNALSRELRDELIAVFDEIsERPDVRVVVLTGA-GKVFCAGADLKGRPDVIKGpgdlRAHN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 102 VWTelQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiiapkwLMSG--FAS-ILPKRVA 178
Cdd:PRK06495 84 RRT--RECFHAIRECAKPVIAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVG------LAGGgkHAMrLFGHSLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 179 ERALTQGRMFTTQEAFEVGLIdEIASSKEEALEKCAAFIGTFAKVNPLARGLTKlqfRGDNIKEFEMIR-----EKDIAd 253
Cdd:PRK06495 156 RRMMLTGYRVPAAELYRRGVI-EACLPPEELMPEAMEIAREIASKSPLATRLAK---DALNTIENMSLRdgyryEQDIT- 230
|
250
....*....|....*....
gi 19921018 254 fVALASSPGVQKVMGAYLE 272
Cdd:PRK06495 231 -AKLAKTEDAKEAQRAFLE 248
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
35-202 |
1.59e-11 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 64.15 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRP--PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIfEMYN--TDVERLRTVWTELQNV 109
Cdd:PRK11154 15 NIAVITIDVPgeKMNTLKAEFAEQVRAILKQLREDKElKGVVFISGKPDNFIAGADI-NMLAacKTAQEAEALARQGQQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 110 WIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMR--PNFLIGLNEAQLGIIaPKwlmSGFASILPKRVA-ERALT--- 183
Cdd:PRK11154 94 FAEIEALPIPVVAAIHGACLGGGLELALACHYRVCTddPKTVLGLPEVQLGLL-PG---SGGTQRLPRLIGvSTALDmil 169
|
170
....*....|....*....
gi 19921018 184 QGRMFTTQEAFEVGLIDEI 202
Cdd:PRK11154 170 TGKQLRAKQALKLGLVDDV 188
|
|
| PRK09076 |
PRK09076 |
enoyl-CoA hydratase; Provisional |
27-227 |
2.88e-11 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236373 [Multi-domain] Cd Length: 258 Bit Score: 62.24 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDKTgiATLTMNRPPVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDIFEMYNTDVERLRTVWTE 105
Cdd:PRK09076 6 DLEIDGHV--AILTLNNPPANTWTADSLQALKQLVLELNADKDvYALVITGDGEKFFSAGADLNLFADGDKAVAREMARR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIApkwlMSGFASILPKRV----AERA 181
Cdd:PRK09076 84 FGEAFEALSAFRGVSIAAINGYAMGGGLECALACDIRIAEEQAQMALPEASVGLLP----CAGGTQNLPWLVgegwAKRM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19921018 182 LTQGRMFTTQEAFEVGLIDEIAsSKEEALEKCAAFIGTFAKVNPLA 227
Cdd:PRK09076 160 ILCGERVDAATALRIGLVEEVV-EKGEAREAALALAQKVANQSPSA 204
|
|
| PRK09245 |
PRK09245 |
crotonase/enoyl-CoA hydratase family protein; |
35-202 |
3.39e-11 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181723 Cd Length: 266 Bit Score: 61.91 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRP----PVnSQN--VQLLLDLqtsISEIENNKS-RGLILTSASSnVFSAGLDIFEMYNT------DVERLRT 101
Cdd:PRK09245 12 HIVTLTMNRPetrnAL-SDNdaVDALVAA---CAAINADRSvRAVILTGAGT-AFSSGGNVKDMRARvgafggSPADIRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 102 VWTE-LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKwlmSGFASILPK----- 175
Cdd:PRK09245 87 GYRHgIQRIPLALYNLEVPVIAAVNGPAIGAGCDLACMCDIRIASETARFAESFVKLGLI-PG---DGGAWLLPRiigma 162
|
170 180
....*....|....*....|....*..
gi 19921018 176 RVAERALTqGRMFTTQEAFEVGLIDEI 202
Cdd:PRK09245 163 RAAEMAFT-GDAIDAATALEWGLVSRV 188
|
|
| PRK11423 |
PRK11423 |
methylmalonyl-CoA decarboxylase; Provisional |
21-248 |
3.43e-11 |
|
methylmalonyl-CoA decarboxylase; Provisional
Pssm-ID: 236908 [Multi-domain] Cd Length: 261 Bit Score: 61.97 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 21 TATKLTTVEINDKtgIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKSRGLILTS-ASSNVFSAGLDIFEM------- 91
Cdd:PRK11423 1 MSMQYVNVVTINK--IATITFNNPAkRNALSKVLIDDLMQALSDLNRPEIRVVILRApSGSKVWSAGHDIHELpsggrdp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 92 --YNTDVER-LRTVWTelqnvwialygTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIiaPkWLMSG 168
Cdd:PRK11423 79 lsYDDPLRQiLRMIQK-----------FPKPVIAMVEGSVWGGAFELIMSCDLIIAASTSTFAMTPANLGV--P-YNLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 169 ---FASILPKRVAERALTQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLARGLTKLQFR--GD----N 239
Cdd:PRK11423 145 ilnFTNDAGFHIVKEMFFTASPITAQRALAVGILNHVVEV-EELEDFTLQMAHHISEKAPLAIAVIKEQLRvlGEahpmN 223
|
....*....
gi 19921018 240 IKEFEMIRE 248
Cdd:PRK11423 224 PDEFERIQG 232
|
|
| PRK05674 |
PRK05674 |
gamma-carboxygeranoyl-CoA hydratase; Validated |
23-211 |
4.69e-11 |
|
gamma-carboxygeranoyl-CoA hydratase; Validated
Pssm-ID: 168168 Cd Length: 265 Bit Score: 61.75 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 23 TKLTTVE-INDKTGIATLTMNRPPVNSQ-NVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEM-------YN 93
Cdd:PRK05674 2 SDFQTIElIRDPRGFATLWLSRADKNNAfNAQMIRELILALDQVQSDASLRFLLLRGRGRHFSAGADLAWMqqsadldYN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 94 TDVERLRtvwtELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiIAPKWLMSGFASIL 173
Cdd:PRK05674 82 TNLDDAR----ELAELMYNLYRLKIPTLAVVQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIG-LAPAVISPFVVKAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19921018 174 PKRVAER-ALTQGRmFTTQEAFEVGLIDEI--ASSKEEALE 211
Cdd:PRK05674 157 GERAARRyALTAER-FDGRRARELGLLAESypAAELEAQVE 196
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
17-202 |
5.43e-11 |
|
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).
Pssm-ID: 131494 [Multi-domain] Cd Length: 737 Bit Score: 62.93 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 17 RLMSTATKL---TTVEINDKTGIATLTMNRP--PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNVFSAGLDI-- 88
Cdd:TIGR02441 1 RLFSTSAALmarTHRHYEVKGDVAVVKIDSPnsKVNTLSKELFAEFKEVMNELWTNEAiKSAVLISGKPGSFVAGADIqm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 89 FEMYNTdVERLRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPN--FLIGLNEAQLGIIAPkwlm 166
Cdd:TIGR02441 81 IAACKT-AQEVTQLSQEGQEMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIATKDrkTLLGLPEVMLGLLPG---- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19921018 167 SGFASILPKRVAERA-----LTqGRMFTTQEAFEVGLIDEI 202
Cdd:TIGR02441 156 AGGTQRLPKLTGVPAaldmmLT-GKKIRADRAKKMGIVDQL 195
|
|
| PRK08150 |
PRK08150 |
crotonase/enoyl-CoA hydratase family protein; |
23-211 |
5.73e-11 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181254 Cd Length: 255 Bit Score: 61.19 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 23 TKLTTVEINDktGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNkSRGLILTSASSNvFSAGLDIFE---MYNTDVER 98
Cdd:PRK08150 1 PSLVSYELDG--GVATIGLNRPAKrNALNDGLIAALRAAFARLPEG-VRAVVLHGEGDH-FCAGLDLSElreRDAGEGMH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 99 LRTVWTELQNVwIAlYGTtLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIiapkwLMSGFASI-LPK-- 175
Cdd:PRK08150 77 HSRRWHRVFDK-IQ-YGR-VPVIAALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGI-----FVGGGGSVrVPRli 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19921018 176 ---RVAERALTqGRMFTTQEAFEVGL---IDEIASSKEEALE 211
Cdd:PRK08150 149 gvaRMTDMMLT-GRVYDAQEGERLGLaqyLVPAGEALDKAME 189
|
|
| PRK06142 |
PRK06142 |
crotonase/enoyl-CoA hydratase family protein; |
27-256 |
7.08e-11 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 235714 Cd Length: 272 Bit Score: 61.14 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDktGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDIF-------EMYNTDVE 97
Cdd:PRK06142 9 TVELAD--HVAQVTLNRPgKGNAMNPAFWSELPEIFRWLDADPEvRAVVLSGSGKH-FSYGIDLPamagvfgQLGKDGLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 98 R----LRTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASIL 173
Cdd:PRK06142 86 RprtdLRREILRLQAAINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRLPRII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 174 PKRVA-ERALTqGRMFTTQEAFEVGLIDEIASSKEEALEKCAAFIGTFAKVNPLA-RGlTKlqfrgdnikefEMI---RE 248
Cdd:PRK06142 166 GDGHLrELALT-GRDIDAAEAEKIGLVNRVYDDADALLAAAHATAREIAAKSPLAvRG-TK-----------EVLdymRD 232
|
250
....*....|.
gi 19921018 249 KDIAD---FVA 256
Cdd:PRK06142 233 HRVADglrYVA 243
|
|
| PRK08252 |
PRK08252 |
crotonase/enoyl-CoA hydratase family protein; |
28-232 |
1.37e-10 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181325 [Multi-domain] Cd Length: 254 Bit Score: 60.00 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 28 VEINDktGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASsNVFSAGLDIfemyntdverlrTVWTE 105
Cdd:PRK08252 7 VERRG--RVLIITINRPEArNAVNAAVAQGLAAALDELDADPDlSVGILTGAG-GTFCAGMDL------------KAFAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQNVWIALYG--------TTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPkwlmSGFASILPKRV 177
Cdd:PRK08252 72 GERPSIPGRGfgglterpPRKPLIAAVEGYALAGGFELALACDLIVAARDAKFGLPEVKRGLVAA----GGGLLRLPRRI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 178 -----AERALTqGRMFTTQEAFEVGLIDEIASSKeEALEKCAAFIGTFAKVNPLARGLTK 232
Cdd:PRK08252 148 pyhiaMELALT-GDMLTAERAHELGLVNRLTEPG-QALDAALELAERIAANGPLAVAASK 205
|
|
| PRK06072 |
PRK06072 |
enoyl-CoA hydratase; Provisional |
28-211 |
6.70e-10 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168377 [Multi-domain] Cd Length: 248 Bit Score: 58.25 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 28 VEINDKTGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENN-KSRGLILTsASSNVFSAGLDIFEMYNTDVERLRT---- 101
Cdd:PRK06072 2 IKVESREGYAIVTMSRPdKLNALNLEMRNEFISKLKQINADpKIRVVIVT-GEGRAFCVGADLSEFAPDFAIDLREtfyp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 102 VWTELQN---VWIalygttlptaAAINGHApAGGCL-LATACEYRVMRPNFLIGLNEAQLGiIAPKwlmSGFASILPK-- 175
Cdd:PRK06072 81 IIREIRFsdkIYI----------SAINGVT-AGACIgIALSTDFKFASRDVKFVTAFQRLG-LASD---TGVAYFLLKlt 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 19921018 176 --RVAERALTQGRmFTTQEAFEVGLIDEIASSKEEALE 211
Cdd:PRK06072 146 gqRFYEILVLGGE-FTAEEAERWGLLKISEDPLSDAEE 182
|
|
| PRK07468 |
PRK07468 |
crotonase/enoyl-CoA hydratase family protein; |
26-212 |
1.29e-09 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180987 [Multi-domain] Cd Length: 262 Bit Score: 57.38 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 26 TTVEIN-DKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDIFEM---YNTDVERL 99
Cdd:PRK07468 4 ETIRIAvDARGVATLTLNRPEKhNALSARMIAELTTAARRLAADAAvRVVVLTGAGKS-FCAGGDLGWMraqMTADRATR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 100 RTVWTELQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIApkwlmsgfASILPKRVAE 179
Cdd:PRK07468 83 IEEARRLAMMLKALNDLPKPLIGRIQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIP--------ATISPYVVAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19921018 180 -------RALTQGRMFTTQEAFEVGLIDEI--ASSKEEALEK 212
Cdd:PRK07468 155 mgeanarRVFMSARLFDAEEAVRLGLLSRVvpAERLDAAVEA 196
|
|
| PRK03580 |
PRK03580 |
crotonobetainyl-CoA hydratase; |
35-207 |
2.19e-09 |
|
crotonobetainyl-CoA hydratase;
Pssm-ID: 179599 [Multi-domain] Cd Length: 261 Bit Score: 56.63 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRPPVNSqnvqllLDLQTS--ISEI-----ENNKSRGLILTSASSNVFSAGLDI---FEMYNTDVERLRTVWT 104
Cdd:PRK03580 12 SILEITLDRPKANA------IDAKTSfaMGEVflnfrDDPELRVAIITGAGEKFFSAGWDLkaaAEGEAPDADFGPGGFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 105 ELQNVWialyGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIAPKWLMSGFASILPKRVAERALTQ 184
Cdd:PRK03580 86 GLTEIF----DLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMT 161
|
170 180
....*....|....*....|...
gi 19921018 185 GRMFTTQEAFEVGLIDEIASSKE 207
Cdd:PRK03580 162 GRRMDAEEALRWGIVNRVVPQAE 184
|
|
| PRK09120 |
PRK09120 |
p-hydroxycinnamoyl CoA hydratase/lyase; Validated |
19-237 |
2.33e-09 |
|
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
Pssm-ID: 236383 Cd Length: 275 Bit Score: 56.94 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEINDKTGIATLTMNRP-PVNSQNVQLLLDLQTSISEIE-NNKSRGLILTSASSNvFSAGLDIFEMY-NTD 95
Cdd:PRK09120 1 MSYENRWDTVKVEVEDGIAWVTLNRPeKRNAMSPTLNREMIDVLDALEfDDDAGVLVLTGAGDA-WSAGMDLKEYFrETD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 96 ------VERLRTV---WtelqnvWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKWLM 166
Cdd:PRK09120 80 aqpeilQERIRREaygW------WRRLRWYQKPTIAMVNGWCFGGGFSPLVACDLAIAADEAQFGLSEINWGIP-PGGGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921018 167 S-GFASILPKRVAERALTQGRMFTTQEAFEVGLIDEiASSKEEALEKCAAFIGTFAKVNPLARGLTKLQFRG 237
Cdd:PRK09120 153 SkAMADTVGHRDALYYIMTGETFTGRKAAEMGLVNE-SVPLAQLRARTRELAAKLLEKNPVVLRAAKDGFKR 223
|
|
| PRK05864 |
PRK05864 |
enoyl-CoA hydratase; Provisional |
33-222 |
2.98e-09 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168278 [Multi-domain] Cd Length: 276 Bit Score: 56.38 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 33 KTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDI--------FEMYNTDVERLRTV 102
Cdd:PRK05864 17 RPEIALITLNRPErMNSMAFDVMVPLKEALAEVSYDNSvRVVVLTGAGRG-FSSGADHksagvvphVEGLTRPTYALRSM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 103 WTeLQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLI---GLNEaqlGIIAPKWlmsGFASILPK---- 175
Cdd:PRK05864 96 EL-LDDVILALRRLHQPVIAAVNGPAIGGGLCLALAADIRVASSSAYFraaGINN---GLTASEL---GLSYLLPRaigs 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19921018 176 -RVAERALTqGRMFTTQEAFEVGLIDEIASSkEEALEKC---AAFIGTFAK 222
Cdd:PRK05864 169 sRAFEIMLT-GRDVDAEEAERIGLVSRQVPD-EQLLDTCyaiAARMAGFSR 217
|
|
| PRK06190 |
PRK06190 |
enoyl-CoA hydratase; Provisional |
28-239 |
3.72e-09 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235733 Cd Length: 258 Bit Score: 56.14 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 28 VEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASSnVFSAGLDIFEMyNTDVERLRtVWTE 105
Cdd:PRK06190 6 LLVETHDRVRTLTLNRPEArNALSAALRRALFAALAEADADDDvDVVVLTGADP-AFCAGLDLKEL-GGDGSAYG-AQDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKWLMSgfaSILPKRVAER----- 180
Cdd:PRK06190 83 LPNPSPAWPAMRKPVIGAINGAAVTGGLELALACDILIASERARFADTHARVGIL-PGWGLS---VRLPQKVGIGrarrm 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 181 ALTqGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAKVNPLA-RGLTKLQFRGDN 239
Cdd:PRK06190 159 SLT-GDFLDAADALRAGLVTEVVPH-DELLPRARRLAASIAGNNPAAvRALKASYDDGAA 216
|
|
| PRK07799 |
PRK07799 |
crotonase/enoyl-CoA hydratase family protein; |
27-227 |
1.44e-08 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181122 [Multi-domain] Cd Length: 263 Bit Score: 54.34 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDKTGIatLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS-RGLILTSASSnVFSAGLDIFEMY-NTDVERLRTVW 103
Cdd:PRK07799 8 LVEQRGHTLI--VTMNRPEArNALSTEMLRIMVDAWDRVDNDPDiRSCILTGAGG-AFCAGMDLKAATkKPPGDSFKDGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 104 TELQNVWIALYGTTL--PTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIApkwlMSGFASILPKR----V 177
Cdd:PRK07799 85 YDPSRIDALLKGRRLtkPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFP----MGGSAVRLVRQipytV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19921018 178 AERALTQGRMFTTQEAFEVGLIDEIASSKeEALEKCAAFIGTFAKVNPLA 227
Cdd:PRK07799 161 ACDLLLTGRHITAAEAKEIGLIGHVVPDG-QALDKALELAELINANGPLA 209
|
|
| PRK08260 |
PRK08260 |
enoyl-CoA hydratase; Provisional |
29-202 |
1.80e-08 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236206 [Multi-domain] Cd Length: 296 Bit Score: 54.24 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 29 EINDktGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILT------------SASSNVFsaGLDIFEMYNT 94
Cdd:PRK08260 9 DVAD--GIATITLNRPDkLNAFTVTMARELIEAFDAADADDAvRAVIVTgagrafcagadlSAGGNTF--DLDAPRTPVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 95 DVERLRTVWTELQ------NVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKWLMSG 168
Cdd:PRK08260 85 ADEEDRADPSDDGvrdgggRVTLRIFDSLKPVIAAVNGPAVGVGATMTLAMDIRLASTAARFGFVFGRRGIV-PEAASSW 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 19921018 169 FasiLPKRVA-ERALT---QGRMFTTQEAFEVGLIDEI 202
Cdd:PRK08260 164 F---LPRLVGlQTALEwvySGRVFDAQEALDGGLVRSV 198
|
|
| PRK08139 |
PRK08139 |
enoyl-CoA hydratase; Validated |
28-217 |
2.70e-08 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 181249 Cd Length: 266 Bit Score: 53.41 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 28 VEINDKTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMY-NTDVERLRTVWTE 105
Cdd:PRK08139 13 LLREDRDGVATLTLNRPQaFNALSEAMLAALQAALDAIAADPSVRVVVLAAAGKAFCAGHDLKEMRaARGLAYFRALFAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 106 LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGII--APkwlMSGFASILPKRVAERALT 183
Cdd:PRK08139 93 CSRVMQAIVALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLFcsTP---MVALSRNVPRKQAMEMLL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 19921018 184 QGRMFTTQEAFEVGLIDEIASSKE--EALEKCAAFI 217
Cdd:PRK08139 170 TGEFIDAATAREWGLVNRVVPADAldAAVARLAAVI 205
|
|
| PLN02888 |
PLN02888 |
enoyl-CoA hydratase |
32-217 |
9.24e-08 |
|
enoyl-CoA hydratase
Pssm-ID: 215480 Cd Length: 265 Bit Score: 52.06 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 32 DKTGIATLTMNRP-PVNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIF---EMYNTDVERLRT---VWT 104
Cdd:PLN02888 16 SRNGIATITINRPkALNALTRPMMVELAAAFKRLDEDDSVKVIILTGSGRAFCSGVDLTaaeEVFKGDVKDVETdpvAQM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 105 ELQNVwialygttlPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiIAPKWLMSGFAS--ILPKRVAERAL 182
Cdd:PLN02888 96 ERCRK---------PIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFG-IFPSWGLSQKLSriIGANRAREVSL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 19921018 183 TqGRMFTTQEAFEVGLIDEIASSKE---EALEKCAAFI 217
Cdd:PLN02888 166 T-AMPLTAETAERWGLVNHVVEESEllkKAREVAEAII 202
|
|
| PRK08140 |
PRK08140 |
enoyl-CoA hydratase; Provisional |
19-139 |
1.47e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236163 Cd Length: 262 Bit Score: 51.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 19 MSTATKLTTVEindkTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNvFSAGLD---------- 87
Cdd:PRK08140 1 MMYETILLAIE----AGVATLTLNRPDkLNSFTREMHRELREALDQVEDDGARALLLTGAGRG-FCAGQDladrdvtpgg 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 88 --------IFEMYNTDVERLRtvwtelqnvwiALygtTLPTAAAINGHAPAGGCLLATAC 139
Cdd:PRK08140 76 ampdlgesIETFYNPLVRRLR-----------AL---PLPVIAAVNGVAAGAGANLALAC 121
|
|
| PRK05870 |
PRK05870 |
enoyl-CoA hydratase; Provisional |
35-215 |
1.82e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180298 Cd Length: 249 Bit Score: 50.88 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSnVFSAGLDIFEMYNTDVERLRTVWTELQNVWIA 112
Cdd:PRK05870 12 GVALITVNDPDrRNAVTAEMSAQLRAAVAAAEADPDvHALVVTGAGK-AFCAGADLTALGAAPGRPAEDGLRRIYDGFLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 113 LYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiIAP----KWLMSgfaSILPKRVAERALTQGRMF 188
Cdd:PRK05870 91 VASCPLPTIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLG-LHPgggaTWMLQ---RAVGPQVARAALLFGMRF 166
|
170 180
....*....|....*....|....*...
gi 19921018 189 TTQEAFEVGLIDEIASSK-EEALEKCAA 215
Cdd:PRK05870 167 DAEAAVRHGLALMVADDPvAAALELAAG 194
|
|
| PRK06210 |
PRK06210 |
enoyl-CoA hydratase; Provisional |
32-238 |
2.75e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180472 Cd Length: 272 Bit Score: 50.47 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 32 DKTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKS-RGLILTSASSNvFSAGLDIFEMYN---TDVER---LRTVW 103
Cdd:PRK06210 12 ADSGVAVITLNRPDrLNAWTPVMEAEVYAAMDRAEADPAvRVIVLTGAGRG-FCAGADMGELQTidpSDGRRdtdVRPFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 104 TELQNVWIALYG--TTL--PTAAAINGhAPAG-GCLLATACEYRVMRPNFLIGLNEAQLGIIAPKwlmsGFASILPKRVA 178
Cdd:PRK06210 91 GNRRPDYQTRYHflTALrkPVIAAING-ACAGiGLTHALMCDVRFAADGAKFTTAFARRGLIAEH----GISWILPRLVG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921018 179 ERA----LTQGRMFTTQEAFEVGLIDEIASSkEEALEKCAAFIGTFAK-VNPLARGLTKLQFRGD 238
Cdd:PRK06210 166 HANaldlLLSARTFYAEEALRLGLVNRVVPP-DELMERTLAYAEDLARnVSPASMAVIKRQLYED 229
|
|
| PRK08290 |
PRK08290 |
enoyl-CoA hydratase; Provisional |
35-232 |
5.71e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236220 [Multi-domain] Cd Length: 288 Bit Score: 49.57 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 35 GIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEM-----YNTDVERLRTVWTELQN 108
Cdd:PRK08290 13 RIARITLNRPEArNAQNRQMLYELDAAFRRAEADDAVRVIVLAGAGKHFSAGHDLGSGtpgrdRDPGPDQHPTLWWDGAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 109 V----------WIALYGTTL-------PTAAAINGHAPAGGCLLATACEyrvmrpnfLIGLNE--------AQLGIIAPK 163
Cdd:PRK08290 93 KpgveqryareWEVYLGMCRrwrdlpkPTIAQVQGACIAGGLMLAWVCD--------LIVASDdaffsdpvVRMGIPGVE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 164 WLmsGFASILPKRVAERALTQGRMFTTQEAFEVGLIDEIASSKEeaLE-KCAAFIGTFAKVNPLARGLTK 232
Cdd:PRK08290 165 YF--AHPWELGPRKAKELLFTGDRLTADEAHRLGMVNRVVPRDE--LEaETLELARRIAAMPPFGLRLTK 230
|
|
| PRK07260 |
PRK07260 |
enoyl-CoA hydratase; Provisional |
26-99 |
6.88e-06 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180910 [Multi-domain] Cd Length: 255 Bit Score: 46.27 E-value: 6.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921018 26 TTVEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYNT----DVERL 99
Cdd:PRK07260 2 EHIIYEVEDDLATLTLNRPEVsNGFNIPMCQEILEALRLAEEDPSVRFLLINANGKVFSVGGDLVEMKRAvdedDVQSL 80
|
|
| Clp_protease_like |
cd00394 |
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ... |
107-202 |
7.01e-06 |
|
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ClpP; endopeptidase Clp; Peptidase S14; ATP-dependent protease, ClpAP)-like enzymes are highly conserved serine proteases and belong to the ClpP/Crotonase superfamily. Included in this family are Clp proteases that are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. The functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP. Active site consists of the triad Ser, His and Asp, preferring hydrophobic or non-polar residues at P1 or P1' positions. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function. Another family included in this class of enzymes is the signal peptide peptidase A (SppA; S49) which is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Mutagenesis studies suggest that the catalytic center of SppA comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain. Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain. The third family included in this hierarchy is nodulation formation efficiency D (NfeD) which is a membrane-bound Clp-class protease and only found in bacteria and archaea. Majority of the NfeD genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named stomatin operon partner protein (STOPP). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 from Pyrococcus horikoshii has been shown to possess serine protease activity having a Ser-Lys catalytic dyad.
Pssm-ID: 132923 [Multi-domain] Cd Length: 161 Bit Score: 45.08 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 107 QNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGL---------NEAQLGI-IAPKWLMSGFASIL--- 173
Cdd:cd00394 47 MNIVDALQASRKPVIAYVGGQAASAGYYIATAANKIVMAPGTRVGShgpiggyggNGNPTAQeADQRIILYFIARFIslv 126
|
90 100 110
....*....|....*....|....*....|....*
gi 19921018 174 ------PKRVAERALTQGRMFTTQEAFEVGLIDEI 202
Cdd:cd00394 127 aenrgqTTEKLEEDIEKDLVLTAQEALEYGLVDAL 161
|
|
| PRK07938 |
PRK07938 |
enoyl-CoA hydratase family protein; |
34-211 |
9.86e-06 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 181174 Cd Length: 249 Bit Score: 45.73 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 34 TGIATLTMNRPPVNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYNTD-VERLRTVWTELQNVWIA 112
Cdd:PRK07938 10 PGIAEVTVDYPPVNALPSAGWFALADAITAAGADPDTRVVVLRAEGRGFNAGVDIKELQATPgFTALIDANRGCFAAFRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 113 LYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIapkwlmsGFASILPKRVAE---RALT-QGRMF 188
Cdd:PRK07938 90 VYECAVPVIAAVHGFCLGGGIGLVGNADVIVASDDATFGLPEVDRGAL-------GAATHLQRLVPQhlmRALFfTAATI 162
|
170 180
....*....|....*....|....*.
gi 19921018 189 TTQEAFEVGLIDEI---ASSKEEALE 211
Cdd:PRK07938 163 TAAELHHFGSVEEVvprDQLDEAALE 188
|
|
| PRK07112 |
PRK07112 |
enoyl-CoA hydratase/isomerase; |
27-212 |
5.26e-05 |
|
enoyl-CoA hydratase/isomerase;
Pssm-ID: 235938 Cd Length: 255 Bit Score: 43.52 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 27 TVEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKS----RGLiltsasSNVFSAGLDIFEMYN-TDVERLR 100
Cdd:PRK07112 5 TIRVRQQGDVCFLQLHRPEAqNTINDRLIAECMDVLDRCEHAATivvlEGL------PEVFCFGADFSAIAEkPDAGRAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 101 TVWTE-LQNVWIALYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIApkwlmsgfASILP---KR 176
Cdd:PRK07112 79 LIDAEpLYDLWHRLATGPYVTIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIP--------ACVLPfliRR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19921018 177 V----AERALTQGRMFTTQEAFEVGLIDEIASSKEEALEK 212
Cdd:PRK07112 151 IgtqkAHYMTLMTQPVTAQQAFSWGLVDAYGANSDTLLRK 190
|
|
| PLN02874 |
PLN02874 |
3-hydroxyisobutyryl-CoA hydrolase-like protein |
26-213 |
1.99e-04 |
|
3-hydroxyisobutyryl-CoA hydrolase-like protein
Pssm-ID: 178462 [Multi-domain] Cd Length: 379 Bit Score: 42.48 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 26 TTVEINDKTGIATLTMNRPPV-NSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYntDVERLRTVWT 104
Cdd:PLN02874 11 EVVLGEEKGRVRVITLNRPRQlNVISLSVVSLLAEFLEQWEKDDSVELIIIKGAGRAFSAGGDLKMFY--DGRESDDSCL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 105 EL--QNVWIA--LYGTTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGiIAPKWLMSGFASILPKRVAER 180
Cdd:PLN02874 89 EVvyRMYWLCyhIHTYKKTQVALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVG-FHTDCGFSYILSRLPGHLGEY 167
|
170 180 190
....*....|....*....|....*....|....*
gi 19921018 181 -ALTQGRMfTTQEAFEVGLIDEIASSKE-EALEKC 213
Cdd:PLN02874 168 lALTGARL-NGKEMVACGLATHFVPSEKlPELEKR 201
|
|
| PRK08259 |
PRK08259 |
crotonase/enoyl-CoA hydratase family protein; |
119-220 |
2.26e-04 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 236205 Cd Length: 254 Bit Score: 41.81 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 119 PTAAAINGHAPAGGCLLATACEYRVMRPnfliglnEAQLGIIAPKW---LMSGFASILPKRVAE-RA----LTqGRMFTT 190
Cdd:PRK08259 95 PVIAAVSGYAVAGGLELALWCDLRVAEE-------DAVFGVFCRRWgvpLIDGGTVRLPRLIGHsRAmdliLT-GRPVDA 166
|
90 100 110
....*....|....*....|....*....|..
gi 19921018 191 QEAFEVGLIDEIASSKE--EALEKCAAFIGTF 220
Cdd:PRK08259 167 DEALAIGLANRVVPKGQarAAAEELAAELAAF 198
|
|
| Clp_protease_NfeD_like |
cd07021 |
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ... |
116-212 |
2.79e-04 |
|
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.
Pssm-ID: 132932 [Multi-domain] Cd Length: 178 Bit Score: 40.65 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 116 TTLPTAAAINGHAPAGGCLLATACEYRVMRPNFLIG----LNEAQLGIIAPK---WLMSGFASILPKR-----VAERALT 183
Cdd:cd07021 57 SPIPTIAYVNDRAASAGALIALAADEIYMAPGATIGaaepIPGDGNGAADEKvqsYWRAKMRAAAEKKgrdpdIAEAMVD 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19921018 184 QGRM-------------FTTQEAFEVGLIDEIASSKEEALEK 212
Cdd:cd07021 137 KDIEvpgvgikggelltLTADEALKVGYAEGIAGSLDELLVK 178
|
|
| PLN02988 |
PLN02988 |
3-hydroxyisobutyryl-CoA hydrolase |
26-219 |
5.82e-04 |
|
3-hydroxyisobutyryl-CoA hydrolase
Pssm-ID: 178568 [Multi-domain] Cd Length: 381 Bit Score: 40.86 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 26 TTVEINDKTGIATLTMNRPP-VNSQNVQLLLDLQTSISEIENNKSRGLILTSASSNVFSAGLDIFEMYNtDVE----RLR 100
Cdd:PLN02988 9 SQVLVEEKSSVRILTLNRPKqLNALSFHMISRLLQLFLAFEEDPSVKLVILKGHGRAFCAGGDVAAVVR-DIEqgnwRLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 101 TVWTE---LQNVWIALYGTTlpTAAAINGHAPAGGCLLATACEYRVMRPNFLIGLNEAQLGIIaPKWLMSGFASILPKRV 177
Cdd:PLN02988 88 ANFFSdeyMLNYVMATYSKA--QVSILNGIVMGGGAGVSVHGRFRIATENTVFAMPETALGLF-PDVGASYFLSRLPGFF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19921018 178 AERALTQGRMFTTQEAFEVGLIDE-IASSKEEALEKCAAFIGT 219
Cdd:PLN02988 165 GEYVGLTGARLDGAEMLACGLATHfVPSTRLTALEADLCRIGS 207
|
|
| NfeD |
COG1030 |
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ... |
112-212 |
1.01e-03 |
|
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440653 [Multi-domain] Cd Length: 413 Bit Score: 40.23 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 112 ALYGTTLPTAA--AINGHAPAGGCLLATACEYRVMRPNFLIG------LNEAQLGIIAPK---WLMSGFASILPKR---- 176
Cdd:COG1030 80 AILASPVPVIVyvASGARAASAGAYILLASHIAAMAPGTNIGaatpvqIGGGIDEAMEEKvinDAVAYIRSLAELRgrna 159
|
90 100 110
....*....|....*....|....*....|....*..
gi 19921018 177 -VAERALTQGRMFTTQEAFEVGLIDEIASSKEEALEK 212
Cdd:COG1030 160 dWAEAMVRESVSLTAEEALELGVIDLIAEDLDELLAT 196
|
|
| S49_SppA |
cd07014 |
Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): ... |
119-215 |
2.43e-03 |
|
Signal peptide peptidase A; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is an intramembrane enzyme found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Unlike the eukaryotic functional homologs that are proposed to be aspartic proteases, site-directed mutagenesis and sequence analysis have shown these bacterial, archaeal and thylakoid SppAs to be ClpP-like serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain, cleaving peptide bonds in the plane of the lipid bilayer. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad (both residues absolutely conserved within bacteria, chloroplast and mitochondrial signal peptidase family members) and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain (sometimes referred to as 67K type). Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain (sometimes referred to as 36K type). Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain. This family also contains homologs that either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases.
Pssm-ID: 132925 [Multi-domain] Cd Length: 177 Bit Score: 37.98 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 119 PTAAAINGHAPAGGCLLATACEYRVMRPNFLIGL---------NEAQLGIIAPKWLMSGFAS--ILPKRVAERaLTQGRM 187
Cdd:cd07014 73 PVVASGGGNAASGGYWISTPANYIVANPSTLVGSigifgvqlaDQLSIENGYKRFITLVADNrhSTPEQQIDK-IAQGGV 151
|
90 100
....*....|....*....|....*...
gi 19921018 188 FTTQEAFEVGLIDEIASSkeEALEKCAA 215
Cdd:cd07014 152 WTGQDAKANGLVDSLGSF--DDAVAKLA 177
|
|
| SppA |
COG0616 |
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ... |
137-205 |
2.60e-03 |
|
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440381 [Multi-domain] Cd Length: 215 Bit Score: 38.24 E-value: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921018 137 TACEYRVMrPNFLIGLNEAQLGIIApKWLMSGFASILpKRVAE---------RALTQGRMFTTQEAFEVGLIDEIASS 205
Cdd:COG0616 141 TAGEYKDA-LSPFRPLSEEEREQLQ-ALLDDIYDQFV-EDVAEgrglsleevREIADGRVWTGEQALELGLVDELGTL 215
|
|
| Clp_protease_NfeD_1 |
cd07020 |
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ... |
126-212 |
8.72e-03 |
|
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.
Pssm-ID: 132931 [Multi-domain] Cd Length: 187 Bit Score: 36.38 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921018 126 GHAPAGGCLLATACEYRVMRPNFLIG------LNEAQLG--IIAPKWL--MSGFA-SILPKR-----VAERALTQGRMFT 189
Cdd:cd07020 70 ARAASAGTYILLAAHIAAMAPGTNIGaahpvaIGGGGGSdpVMEKKILndAVAYIrSLAELRgrnaeWAEKAVRESLSLT 149
|
90 100
....*....|....*....|...
gi 19921018 190 TQEAFEVGLIDEIASSKEEALEK 212
Cdd:cd07020 150 AEEALKLGVIDLIAADLNELLKK 172
|
|
| |
