|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-306 |
5.05e-47 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 161.93 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSRGglPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGV--FLVPGPADparGIRVVENWNH 115
Cdd:COG1960 126 EPGAGSDAAA--LRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGHRGIslFLVPKDTP---GVTVGRIEDK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 116 LGLRASGSHETVLDDVWIPPEYavdlRLPEQwtPAGASQAdidanadqQAWMV---VLLGSLYDAVARAGFDWIRDFVQT 192
Cdd:COG1960 201 MGLRGSDTGELFFDDVRVPAEN----LLGEE--GKGFKIA--------MSTLNagrLGLAAQALGIAEAALELAVAYARE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 193 RAPAslGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPgDSGLLKFTVTGNAIRAVELALQLAGNHGLS 272
Cdd:COG1960 267 REQF--GRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
250 260 270
....*....|....*....|....*....|....
gi 759727903 273 RNNPLERHYRDVLCGRVHTPQDDAILIAAGRHAL 306
Cdd:COG1960 344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
12-288 |
2.81e-43 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 150.90 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 12 HWPPAATQRVFDSAVSEGALINALRVEPelGSPSRGGLPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQP- 90
Cdd:cd00567 51 YGTEEQKERYLPPLASGEAIAAFALTEP--GAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 91 --RVGVFLVPgpADpARGIRVVENWNHLGLRASGSHETVLDDVWIPPEYavdlRLPEQwtPAGASQAdidanadQQAWMV 168
Cdd:cd00567 129 hrGISAFLVP--AD-TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDN----LLGEE--GGGFELA-------MKGLNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 169 --VLLGSLYDAVARAGFDWIRDFVQTRAPasLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSGL 246
Cdd:cd00567 193 grLLLAAVALGAARAALDEAVEYAKQRKQ--FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAM 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 759727903 247 LKFTVTGNAIRAVELALQLAGNHGLSRNNPLERHYRDVLCGR 288
Cdd:cd00567 271 AKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAAR 312
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
177-289 |
6.21e-15 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 70.75 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 177 AVARAGFDWIRDFVQTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSgLLKFTVTGNAI 256
Cdd:pfam00441 24 GLARRALDEALAYARRRK--AFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEAS-MAKLYASEAAV 100
|
90 100 110
....*....|....*....|....*....|...
gi 759727903 257 RAVELALQLAGNHGLSRNNPLERHYRDVLCGRV 289
Cdd:pfam00441 101 EVADLAMQLHGGYGYLREYPVERLYRDARVLRI 133
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
33-306 |
2.72e-07 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 51.37 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 33 NALRVEPELGSpSRGGLPgTVATRTADGWRLHGRKLYCTGIPALRWLAVWARtDEPQPRVGVF--LVPGPADParGIRVv 110
Cdd:PRK03354 121 NSAITEPGAGS-DVGSLK-TTYTRRNGKVYLNGSKCFITSSAYTPYIVVMAR-DGASPDKPVYteWFVDMSKP--GIKV- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 111 ENWNHLGLRASGSHETVLDDVwippeyavDLRLPEQWTPAGASQADIDANADQQAWMVVLLGslYDAvARAGFDWIRDFV 190
Cdd:PRK03354 195 TKLEKLGLRMDSCCEITFDDV--------ELDEKDMFGREGNGFNRVKEEFDHERFLVALTN--YGT-AMCAFEDAARYA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 191 QTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPpTPGDSGLLKFTVTGNAIRAVELALQLAGNHG 270
Cdd:PRK03354 264 NQRV--QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTI-TSGDAAMCKYFCANAAFEVVDSAMQVLGGVG 340
|
250 260 270
....*....|....*....|....*....|....*.
gi 759727903 271 LSRNNPLERHYRDVLCGRVHTPQDDAILIAAGRHAL 306
Cdd:PRK03354 341 IAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVL 376
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-306 |
5.05e-47 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 161.93 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSRGglPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGV--FLVPGPADparGIRVVENWNH 115
Cdd:COG1960 126 EPGAGSDAAA--LRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGHRGIslFLVPKDTP---GVTVGRIEDK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 116 LGLRASGSHETVLDDVWIPPEYavdlRLPEQwtPAGASQAdidanadqQAWMV---VLLGSLYDAVARAGFDWIRDFVQT 192
Cdd:COG1960 201 MGLRGSDTGELFFDDVRVPAEN----LLGEE--GKGFKIA--------MSTLNagrLGLAAQALGIAEAALELAVAYARE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 193 RAPAslGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPgDSGLLKFTVTGNAIRAVELALQLAGNHGLS 272
Cdd:COG1960 267 REQF--GRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
250 260 270
....*....|....*....|....*....|....
gi 759727903 273 RNNPLERHYRDVLCGRVHTPQDDAILIAAGRHAL 306
Cdd:COG1960 344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
12-288 |
2.81e-43 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 150.90 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 12 HWPPAATQRVFDSAVSEGALINALRVEPelGSPSRGGLPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQP- 90
Cdd:cd00567 51 YGTEEQKERYLPPLASGEAIAAFALTEP--GAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 91 --RVGVFLVPgpADpARGIRVVENWNHLGLRASGSHETVLDDVWIPPEYavdlRLPEQwtPAGASQAdidanadQQAWMV 168
Cdd:cd00567 129 hrGISAFLVP--AD-TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDN----LLGEE--GGGFELA-------MKGLNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 169 --VLLGSLYDAVARAGFDWIRDFVQTRAPasLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSGL 246
Cdd:cd00567 193 grLLLAAVALGAARAALDEAVEYAKQRKQ--FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAM 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 759727903 247 LKFTVTGNAIRAVELALQLAGNHGLSRNNPLERHYRDVLCGR 288
Cdd:cd00567 271 AKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAAR 312
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
13-306 |
3.44e-21 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 92.39 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 13 WPPAATQRVFDSAVSEGALI-NAlrvepelGSPSRGGLPGTVATRTA---DGWRLHGRKLYCTGIPALRWLAVWArTDEP 88
Cdd:cd01163 86 AGPEQFRKRWFGRVLNGWIFgNA-------VSERGSVRPGTFLTATVrdgGGYVLNGKKFYSTGALFSDWVTVSA-LDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 89 QPRVGVFLvpgPADpARGIRVVENWNHLGLRASGSHETVLDDVWIPPEYAVDlrlpeqwTPAGASQADIDANADQQAWMV 168
Cdd:cd01163 158 GKLVFAAV---PTD-RPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLP-------RPNAPDRGTLLTAIYQLVLAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 169 VLLGslydaVARAGFDWIRDFVQTRA-PAS-LGAPLATL-PRVQQTIGEIAALLQANRALLDDATSRID----AGHPPTP 241
Cdd:cd01163 227 VLAG-----IARAALDDAVAYVRSRTrPWIhSGAESARDdPYVQQVVGDLAARLHAAEALVLQAARALDaaaaAGTALTA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759727903 242 GDSGLL-------KFTVTGNAIRAVELALQLAGNHGLSRNNPLERHYRDVlcgRVHTPQDDAILIAA--GRHAL 306
Cdd:cd01163 302 EARGEAalavaaaKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNA---RTHTLHNPVIYKERavGDYAL 372
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
50-307 |
2.05e-18 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 84.32 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 50 PGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQ--PRVGVFLVPgpadpARGIRVVENWNHLGLRASGSHETV 127
Cdd:cd01159 109 PGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDggPLPRAFVVP-----RAEYEIVDTWHVVGLRGTGSNTVV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 128 LDDVWIPPEYAVDLRLPEQWTPAGASQADIDANADQ---QAWMVVLLGSLYDAVAragfDWIRDFVQTRAPASLGAPLAT 204
Cdd:cd01159 184 VDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLRQvfpLSFAAVSLGAAEGALA----EFLELAGKRVRQYGAAVKMAE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 205 LPRVQQTIGEIAALLQANRALLDDATSRIDA----GHPPTPGDSGLLKFT---VTGNAIRAVELALQLAGNHGLSRNNPL 277
Cdd:cd01159 260 APITQLRLAEAAAELDAARAFLERATRDLWAhalaGGPIDVEERARIRRDaayAAKLSAEAVDRLFHAAGGSALYTASPL 339
|
250 260 270
....*....|....*....|....*....|.
gi 759727903 278 ERHYRDVLCGRVHTP-QDDAILIAAGRHALA 307
Cdd:cd01159 340 QRIWRDIHAAAQHAAlNPETAAEAYGRALLG 370
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-284 |
6.79e-18 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 83.09 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSrGGLpGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGV--FLVPgpaDPARGIRVVENWNH 115
Cdd:cd01158 121 EPGAGSDA-AAL-KTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSKGYRGItaFIVE---RDTPGLSVGKKEDK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 116 LGLRASGSHETVLDDVWIPPE---------YAVDLRLPEQWTPAGASQAdidanadqqawmvvlLGslydaVARAGFDWI 186
Cdd:cd01158 196 LGIRGSSTTELIFEDVRVPKEnilgeegegFKIAMQTLDGGRIGIAAQA---------------LG-----IAQAALDAA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 187 RDFVQTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPgDSGLLKFTVTGNAIRAVELALQLA 266
Cdd:cd01158 256 VDYAKERK--QFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIK-EAAMAKLFASEVAMRVTTDAVQIF 332
|
250
....*....|....*...
gi 759727903 267 GNHGLSRNNPLERHYRDV 284
Cdd:cd01158 333 GGYGYTKDYPVERYYRDA 350
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
40-290 |
3.26e-15 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 75.17 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 40 ELGSPSRGGLPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPR-VGVFLVPgpaDPARGIRVVENWNHLGL 118
Cdd:cd01162 122 EPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKgISCFVVE---KGTPGLSFGANEKKMGW 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 119 RASGSHETVLDDVWIPpeyaVDLRLPEQwtPAGASQADIDANADQQAWMVVLLGSlydavARAGFDWIRDFVQTRApaSL 198
Cdd:cd01162 199 NAQPTRAVIFEDCRVP----VENRLGGE--GQGFGIAMAGLNGGRLNIASCSLGA-----AQAALDLARAYLEERK--QF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 199 GAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSGLLKFTVTGNAIRAVELALQLAGNHGLSRNNPLE 278
Cdd:cd01162 266 GKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVE 345
|
250
....*....|..
gi 759727903 279 RHYRDVlcgRVH 290
Cdd:cd01162 346 QYVRDL---RVH 354
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
177-289 |
6.21e-15 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 70.75 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 177 AVARAGFDWIRDFVQTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSgLLKFTVTGNAI 256
Cdd:pfam00441 24 GLARRALDEALAYARRRK--AFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEAS-MAKLYASEAAV 100
|
90 100 110
....*....|....*....|....*....|...
gi 759727903 257 RAVELALQLAGNHGLSRNNPLERHYRDVLCGRV 289
Cdd:pfam00441 101 EVADLAMQLHGGYGYLREYPVERLYRDARVLRI 133
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
38-283 |
4.12e-14 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 72.01 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSrGGLpGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGVFLVPGpadpARGIRVVENWNHLG 117
Cdd:cd01151 134 EPNHGSDP-GGM-ETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETGKIRGFILERG----MKGLSAPKIQGKFS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 118 LRASGSHETVLDDVWIPPEYavdlRLPEqwtpagasqadIDANAD-----QQAWMVVLLGSLydAVARAGFDWIRDFVQT 192
Cdd:cd01151 208 LRASITGEIVMDNVFVPEEN----LLPG-----------AEGLRGpfkclNNARYGIAWGAL--GAAEDCYHTARQYVLD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 193 RapASLGAPLATLPRVQQ----TIGEIAALLQANRALlddatSRI-DAGHpPTPGDSGLLKFTVTGNAIRAVELALQLAG 267
Cdd:cd01151 271 R--KQFGRPLAAFQLVQKkladMLTEIALGLLACLRV-----GRLkDQGK-ATPEQISLLKRNNCGKALEIARTAREMLG 342
|
250
....*....|....*.
gi 759727903 268 NHGLSRNNPLERHYRD 283
Cdd:cd01151 343 GNGISDEYHIIRHMVN 358
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
15-291 |
1.04e-12 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 67.91 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 15 PAATQRVFDSAVSeGALINALRV-EPELGSPSRGglPGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTD-EPQPRV 92
Cdd:cd01160 97 PEQKERVLPQMVA-GKKIGAIAMtEPGAGSDLQG--IRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGgEARGAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 93 GV--FLVPGPADparGIRVVENWNHLGLRASGSHETVLDDVWIPPEYAvdlrLPEQwtpaGASQADIDANADQQAwmvVL 170
Cdd:cd01160 174 GIslFLVERGTP---GFSRGRKLKKMGWKAQDTAELFFDDCRVPAENL----LGEE----NKGFYYLMQNLPQER---LL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 171 LGSLYDAVARAGFDWIRDFVQTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPtPGDSGLLKFT 250
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRK--AFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYW 316
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 759727903 251 VTGNAIRAVELALQLAGNHGLSRNNPLERHYRDvlcGRVHT 291
Cdd:cd01160 317 ATELQNRVAYECVQLHGGWGYMREYPIARAYRD---ARVQP 354
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
178-291 |
1.86e-12 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 63.52 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 178 VARAGFDWIRDFVQTRAPASLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRI----DAGHPPTPGDSGLL---KFT 250
Cdd:pfam08028 9 AARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaAAGKPVTPALRAEArraAAF 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 759727903 251 VTGNAIRAVELALQLAGNHGLSRNNPLERHYRDVLCGRVHT 291
Cdd:pfam08028 89 ATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHA 129
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
38-129 |
4.34e-09 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 53.05 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPsrgglPGTVATRTADG----WRLHGRKLYCTGIPALRWLAVWARTDEPQPRVG--VFLVPgPADParGIRVVE 111
Cdd:pfam02770 6 EPGAGSD-----VASLKTTAADGdgggWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGisLFLVP-KDAP--GVSVRR 77
|
90
....*....|....*...
gi 759727903 112 NWNHLGLRASGSHETVLD 129
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
33-306 |
2.72e-07 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 51.37 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 33 NALRVEPELGSpSRGGLPgTVATRTADGWRLHGRKLYCTGIPALRWLAVWARtDEPQPRVGVF--LVPGPADParGIRVv 110
Cdd:PRK03354 121 NSAITEPGAGS-DVGSLK-TTYTRRNGKVYLNGSKCFITSSAYTPYIVVMAR-DGASPDKPVYteWFVDMSKP--GIKV- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 111 ENWNHLGLRASGSHETVLDDVwippeyavDLRLPEQWTPAGASQADIDANADQQAWMVVLLGslYDAvARAGFDWIRDFV 190
Cdd:PRK03354 195 TKLEKLGLRMDSCCEITFDDV--------ELDEKDMFGREGNGFNRVKEEFDHERFLVALTN--YGT-AMCAFEDAARYA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 191 QTRApaSLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPpTPGDSGLLKFTVTGNAIRAVELALQLAGNHG 270
Cdd:PRK03354 264 NQRV--QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTI-TSGDAAMCKYFCANAAFEVVDSAMQVLGGVG 340
|
250 260 270
....*....|....*....|....*....|....*.
gi 759727903 271 LSRNNPLERHYRDVLCGRVHTPQDDAILIAAGRHAL 306
Cdd:PRK03354 341 IAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
54-283 |
3.50e-07 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 50.87 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 54 ATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGV--FLVPgPADParGIRVVENWNHLGLRASGSHETVLDDV 131
Cdd:cd01156 138 AEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDPSAGAHGItaFIVE-KGMP--GFSRAQKLDKLGMRGSNTCELVFEDC 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 132 WIPPEYAVDlrlpeqwtPAGASQADIDANADQQAwMVVLLGSLydAVARAGFDWIRDFVQTRapASLGAPLATLPRVQQT 211
Cdd:cd01156 215 EVPEENILG--------GENKGVYVLMSGLDYER-LVLAGGPI--GIMQAALDVAIPYAHQR--KQFGQPIGEFQLVQGK 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759727903 212 IGEIAALLQANRALLDDATSRIDAGHpPTPGDSGLLKFTVTGNAIRAVELALQLAGNHGLSRNNPLERHYRD 283
Cdd:cd01156 282 LADMYTRLNASRSYLYTVAKACDRGN-MDPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRD 352
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
42-283 |
4.28e-07 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 50.83 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 42 GSPSRGGlpGTVATRTADG-WRLHGRKLYCTGIPALRWLaVWARTDEPQPR---VGVFLVPG--PADPARGIRVVENWNH 115
Cdd:cd01154 159 GSDLGAN--ETTAERSGGGvYRLNGHKWFASAPLADAAL-VLARPEGAPAGargLSLFLVPRllEDGTRNGYRIRRLKDK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 116 LGLRASGSHETVLDDvwippeyAVDLRLPEQwtPAGASQADIDANADQQAWMVVLLGslydaVARAGFDWIRDFVQTRAp 195
Cdd:cd01154 236 LGTRSVATGEVEFDD-------AEAYLIGDE--GKGIYYILEMLNISRLDNAVAALG-----IMRRALSEAYHYARHRR- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 196 aSLGAPLATLPRVQQTIGEIAALLQANRALLDDAtsrIDAGHPPTPGDSG----------LLKFTVTGNAIRAVELALQL 265
Cdd:cd01154 301 -AFGKPLIDHPLMRRDLAEMEVDVEAATALTFRA---ARAFDRAAADKPVeahmarlatpVAKLIACKRAAPVTSEAMEV 376
|
250
....*....|....*...
gi 759727903 266 AGNHGLSRNNPLERHYRD 283
Cdd:cd01154 377 FGGNGYLEEWPVARLHRE 394
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
54-283 |
1.34e-06 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 49.49 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 54 ATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPRVGV--FLVpgpADPARGIRVVENWNHLGLRASGSHETVLDDV 131
Cdd:PLN02519 164 AERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGItaFII---EKGMPGFSTAQKLDKLGMRGSDTCELVFENC 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 132 WIPPEYAVDlrlpeqwtPAGASQADIDANADQQAwMVVLLGSLydAVARAGFDWIRDFVQTRapASLGAPLATLPRVQQT 211
Cdd:PLN02519 241 FVPEENVLG--------QEGKGVYVMMSGLDLER-LVLAAGPL--GLMQACLDVVLPYVRQR--EQFGRPIGEFQFIQGK 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759727903 212 IGEIAALLQANRALLDDATSRIDAGHPPTPGDSGLLKFTvtgnAIRAVELALQ----LAGNhGLSRNNPLERHYRD 283
Cdd:PLN02519 308 LADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCA----AERATQVALQaiqcLGGN-GYINEYPTGRLLRD 378
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
38-271 |
7.14e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 47.15 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSRGglPGTVATRTADGWRLHGRKlyctgipalRW---------LAVWARTDEPQpRVGVFLVPGPADparGIR 108
Cdd:PLN02526 150 EPDYGSDASS--LNTTATKVEGGWILNGQK---------RWignstfadvLVIFARNTTTN-QINGFIVKKGAP---GLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 109 VVENWNHLGLRASGSHETVLDDVWIPPEyavDlRLPeqwtpaGA-SQADIDanaDQQAWMVVLLGSLYDAVARAGFDWIR 187
Cdd:PLN02526 215 ATKIENKIGLRMVQNGDIVLKDVFVPDE---D-RLP------GVnSFQDTN---KVLAVSRVMVAWQPIGISMGVYDMCH 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 188 DFVQTRapASLGAPLATLPRVQQTIGEIAALLQAnRALLDDATSRIDAGHPPTPGDSGLLKFTVTGNAIRAVELALQLAG 267
Cdd:PLN02526 282 RYLKER--KQFGAPLAAFQINQEKLVRMLGNIQA-MFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLG 358
|
....
gi 759727903 268 NHGL 271
Cdd:PLN02526 359 GNGI 362
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
38-276 |
3.57e-05 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 45.03 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSpSRGGLpGTVATRTADGWRLHGRKLYCTGIPALRWLAVWARTDEPQPR---VGVFLVPGPADparGIRVVENWN 114
Cdd:cd01152 125 EPGAGS-DLAGL-RTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrgISILLVDMDSP---GVTVRPIRS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 115 HLGlrASGSHETVLDDVWIPpeyaVDLRLPEQwtpagasqadidaNADQQAWMVVLL---GSLYDAVARAGFDWIRDFVQ 191
Cdd:cd01152 200 ING--GEFFNEVFLDDVRVP----DANRVGEV-------------NDGWKVAMTTLNferVSIGGSAATFFELLLARLLL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 192 TRAPaslGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGDSgLLKFTVTGNAIRAVELALQLAGNHGL 271
Cdd:cd01152 261 LTRD---GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEAS-IAKLFGSELAQELAELALELLGTAAL 336
|
....*
gi 759727903 272 SRNNP 276
Cdd:cd01152 337 LRDPA 341
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
38-283 |
2.75e-03 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 39.15 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 38 EPELGSPSRGGLpgTVATRTADG-WRLHGRKLYCTGIPALRWLAVWARTDEpqpRVGVFLVpgpADPARGIRVVENWNHL 116
Cdd:PTZ00461 159 EPGAGTDVLGMR--TTAKKDSNGnYVLNGSKIWITNGTVADVFLIYAKVDG---KITAFVV---ERGTKGFTQGPKIDKC 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 117 GLRASGSHETVLDDVWIPPEYAvdlrLPEQwtpaGASQADIDANADQQAwmvVLLGSLYDAVARAGFDWIRDFVQTRApa 196
Cdd:PTZ00461 231 GMRASHMCQLFFEDVVVPAENL----LGEE----GKGMVGMMRNLELER---VTLAAMAVGIAERSVELMTSYASERK-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759727903 197 SLGAPLATLPRVQQTIGEIAALLQANRALLDDATSRIDAGHPPTPGdSGLLKFTVTGNAIRAVELALQLAGNHGLSRNNP 276
Cdd:PTZ00461 298 AFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAKLFATPIAKKVADSAIQVMGGMGYSRDMP 376
|
....*..
gi 759727903 277 LERHYRD 283
Cdd:PTZ00461 377 VERLWRD 383
|
|
| |
