|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-460 |
0e+00 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 535.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFtKDAKAFGIS-GEVTFDY 79
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEA-RHAAEFGISaGAPSVDW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 80 GIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDlndgGTESVTFDNAIIATGSSTRLVPGTSL-SANV 158
Cdd:COG1249 80 AALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPGLdEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 159 VTYEEQILSRELPKSiiiagagaigM----------EFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVT 228
Cdd:COG1249 156 LTSDEALELEELPKS----------LvvigggyiglEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 229 ILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIG 308
Cdd:COG1249 226 ILTGAKVTSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 309 DVNGLLQLAHVAEAQGVVAAETIAGAETLTLgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGV 388
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENILGKKPRPV-DYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALAL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814539035 389 GDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGH 460
Cdd:COG1249 385 GETEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
3-463 |
0e+00 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 529.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 3 HYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFtKDAKAFGI-SGEVTFDYGI 81
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEI-KHAKDLGIeVENVSVDWEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 82 AYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDlNDGGTESVTFDNAIIATGSSTRLVPGTSL--SANVV 159
Cdd:TIGR01350 80 MQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVT-GENGEETLEAKNIIIATGSRPRSLPGPFDfdGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 160 TYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIA 239
Cdd:TIGR01350 159 TSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 240 DGGSQVTVTVtKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHV 319
Cdd:TIGR01350 239 KNDDQVTYEN-KGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 320 AEAQGVVAAETIAGAETlTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVA 399
Cdd:TIGR01350 318 ASHEGIVAAENIAGKEP-AHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814539035 400 DAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMIN 463
Cdd:TIGR01350 397 DKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
2-464 |
9.67e-180 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 510.84 E-value: 9.67e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 2 THYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHiFTKDAKAFGIS-GEVTFDYG 80
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERAD-EARHSEDFGIKaENVGIDFK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 81 IAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDlNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVT 160
Cdd:PRK06416 82 KVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVM-TEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 161 YEEQILS-RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIA 239
Cdd:PRK06416 161 TSDEALNlDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 240 DGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVAlTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHV 319
Cdd:PRK06416 241 QTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVK-TDRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 320 AEAQGVVAAETIAGAETLTlgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVA 399
Cdd:PRK06416 320 ASAEGIIAAEAIAGNPHPI--DYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814539035 400 DAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF 464
Cdd:PRK06416 398 DKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-464 |
6.91e-142 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 414.71 E-value: 6.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE----PKYW---GGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGIS- 72
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknPKGKpalGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 73 GEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTF--ADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVP 150
Cdd:PRK06327 82 DGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFvgKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 151 GTSLSANVVTYEEQILS-RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTI 229
Cdd:PRK06327 162 GVPFDNKIILDNTGALNfTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 230 LTATKVESIADGGSQVTVTVT-KDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIG 308
Cdd:PRK06327 242 HLGVKIGEIKTGGKGVSVAYTdADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 309 DVNGLLQLAHVAEAQGVVAAETIAGAETLTlgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGV 388
Cdd:PRK06327 322 DVVRGPMLAHKAEEEGVAVAERIAGQKGHI--DYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814539035 389 GDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF 464
Cdd:PRK06327 400 GEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLHF 475
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1-457 |
1.84e-140 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 410.72 E-value: 1.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIfTKDAKAFGISGE-VTFDY 79
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHE-AKHAEEFGIHADgPKIDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 80 GIAYDRSRKVAEGRVAGV-HFLMKKNKITEIHGYGTFADANTLLVdlndgGTESVTFDNAIIATGSSTRLVPG--TSLSA 156
Cdd:PRK06292 80 KKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRVPPIPGvwLILGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 157 NVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKlGVTILTATKVE 236
Cdd:PRK06292 155 RLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 237 SIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQL 316
Cdd:PRK06292 234 SVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 317 AHVAEAQGVVAAETIAGAETLTLgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVK 396
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDVAGGV-RYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVK 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814539035 397 LVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGL 457
Cdd:PRK06292 393 VYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDL 453
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-450 |
4.22e-106 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 322.92 E-value: 4.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIfTKDAKAFGIS--GEVTFD 78
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHL-ARRAAEYGVSvgGPVSVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 79 YGIAYDRSRKVAEGRVAGV-HFLMKKNKITEIHGYGTFADANTLLVdlndgGTESVTFDNAIIATGSSTRL--VPGTsls 155
Cdd:PRK06370 82 FKAVMARKRRIRARSRHGSeQWLRGLEGVDVFRGHARFESPNTVRV-----GGETLRAKRIFINTGARAAIppIPGL--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 156 aNVVTY--EEQILS-RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTA 232
Cdd:PRK06370 154 -DEVGYltNETIFSlDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 233 TKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNG 312
Cdd:PRK06370 233 AECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 313 LLQLAHVAEAQGVVAAETIAGAETLTLGDhRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPS 392
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLDGGRRKVSD-RIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQ 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 814539035 393 GFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEAL 450
Cdd:PRK06370 392 GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELI 449
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
4-451 |
1.86e-99 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 305.89 E-value: 1.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHiFTKDAKAFGISGEVTFDYGIAY 83
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAH-YARKPPFGGLAATVAVDFGELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 84 DRSRK-VAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLndgGTESVTFDNAIIATGSSTRL--VPGTSlSANVVT 160
Cdd:TIGR02053 80 EGKREvVEELRHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDL---GREVRGAKRFLIATGARPAIppIPGLK-EAGYLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 161 YEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIAD 240
Cdd:TIGR02053 156 SEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 241 GGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVA 320
Cdd:TIGR02053 236 RGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 321 EAQGVVAAETIAGAETLTLgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVAD 400
Cdd:TIGR02053 316 AKEGVVAAENALGGANAKL-DLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 814539035 401 AKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQ 451
Cdd:TIGR02053 395 PGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLK 445
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-419 |
1.16e-74 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 241.60 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEpKYW--GGVCLNVGCIPSKALlRNAELvHI--FTKDA--KAFGISGE 74
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE-RYRnvGGGCTHTGTIPSKAL-REAVL-RLigFNQNPlySSYRVKLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 75 VTFDYGIAydRSRKVAEGRVAGV-HFLMKkNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTS 153
Cdd:PRK05249 80 ITFADLLA--RADHVINKQVEVRrGQYER-NRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 154 LSANVVTYEEQILS-RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTA 232
Cdd:PRK05249 157 FDHPRIYDSDSILSlDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 233 TKVESIADGGSQVtVTVTKDGvaQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNG 312
Cdd:PRK05249 237 EEVEKVEGGDDGV-IVHLKSG--KKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 313 LLQLAHVAEAQGVVAAETIAGAETLTLgdHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPS 392
Cdd:PRK05249 314 FPSLASASMDQGRIAAQHAVGEATAHL--IEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQIAGDNV 391
|
410 420
....*....|....*....|....*..
gi 814539035 393 GFVKLVADAKHGELLGGHLVGHDVAEL 419
Cdd:PRK05249 392 GMLKILFHRETLEILGVHCFGERATEI 418
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-448 |
1.02e-72 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 236.21 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGIS-GEVTFDY 79
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDvTENKFDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 80 giAYDRSRKVAE-GRVAGVHF-LMKKNKITEIHGYGTFADANTLLVDlndggTESVTFDNAIIATGSSTRL--VPGTSLs 155
Cdd:PRK06116 82 --AKLIANRDAYiDRLHGSYRnGLENNGVDLIEGFARFVDAHTVEVN-----GERYTADHILIATGGRPSIpdIPGAEY- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 156 anVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKV 235
Cdd:PRK06116 154 --GITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 236 ESI---ADGGSQVTvtvTKDGvaQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNG 312
Cdd:PRK06116 232 KAVeknADGSLTLT---LEDG--ETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 313 LLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYD--VVVAKFPFTANAKAHGVGD 390
Cdd:PRK06116 307 RVELTPVAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEdnVKVYRSSFTPMYTALTGHR 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 814539035 391 PSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSE 448
Cdd:PRK06116 387 QPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
3-448 |
3.26e-72 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 234.85 E-value: 3.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 3 HYDVVVLGAGPGGYVAAIRAAqlGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKaFGISGEVTfdyGIA 82
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAAR-LGVDAELD---GVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 83 YDRSRKVAEGRV-----AGVHFLMKKN-KITEIHGYGTFADANTLLVDlnDGGTesVTFDNAIIATGSSTRlVPGTSLSA 156
Cdd:PRK07846 75 WPDIVSRVFGRIdpiaaGGEEYRGRDTpNIDVYRGHARFIGPKTLRTG--DGEE--ITADQVVIAAGSRPV-IPPVIADS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 157 NVVTYEEQILSR--ELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKlGVTILTATK 234
Cdd:PRK07846 150 GVRYHTSDTIMRlpELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASK-RWDVRLGRN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 235 VESIADGGSQVTVTVTkDGvaQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLL 314
Cdd:PRK07846 229 VVGVSQDGSGVTLRLD-DG--STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 315 QLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGF 394
Cdd:PRK07846 306 QLKHVANHEARVVQHNLLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGF 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 814539035 395 VKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVH-THPTMSE 448
Cdd:PRK07846 386 VKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPE 440
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
6-453 |
3.61e-72 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 238.13 E-value: 3.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 6 VVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIftkdakafgiSGEVTFDYGI---- 81
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHL----------RRESPFDGGIaatv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 82 -AYDRSR-------KVAEGRVAGVHFLMKKN-KITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGT 152
Cdd:PRK13748 171 pTIDRSRllaqqqaRVDELRHAKYEGILDGNpAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 153 SLSANVV-TYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIvefLPRA--LPNEDADVSKEIEKQFKKLGVTI 229
Cdd:PRK13748 251 GLKETPYwTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTI---LARStlFFREDPAIGEAVTAAFRAEGIEV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 230 LTATKVESIADGGSQVTVTvTKDGvaqELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGD 309
Cdd:PRK13748 328 LEHTQASQVAHVDGEFVLT-TGHG---ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 310 VNGLLQLAHVAEAQGVVAAETIAGAETlTLgDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVG 389
Cdd:PRK13748 404 CTDQPQFVYVAAAAGTRAAINMTGGDA-AL-DLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANF 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814539035 390 DPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQEC 453
Cdd:PRK13748 482 DTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLA 545
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
4-324 |
1.05e-65 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 213.33 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPkywGGVCLNVGCIPSKALLRNAELVHIFTKDAKAfgisgevtfdygiaY 83
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED---EGTCPYGGCVLSKALLGAAEAPEIASLWADL--------------Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 84 DRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTllvdlNDGGTESVTFDNAIIATGSSTRL--VPGTSLSA--NVV 159
Cdd:pfam07992 64 KRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLppIPGVELNVgfLVR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 160 TYE--EQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVES 237
Cdd:pfam07992 139 TLDsaEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 238 IADGGSQVTVtVTKDGvaQELKAEKVLQAIGFAPNVEgyGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVN-GLLQL 316
Cdd:pfam07992 219 IIGDGDGVEV-ILKDG--TEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPEL 293
|
....*...
gi 814539035 317 AHVAEAQG 324
Cdd:pfam07992 294 AQNAVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
1-454 |
1.10e-63 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 212.30 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE--PKYWGGVCLNVGCIPSKALLRNAElvhiftKDAkafgisgevTFD 78
Cdd:PRK07251 1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEesKAMYGGTCINIGCIPTKTLLVAAE------KNL---------SFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 79 YGIAydrSRKVAEGRVAGVHFLMKKNK-ITEIHGYGTFADANTLLVDLNDGGTEsVTFDNAIIATGS-STRL-VPGTSLS 155
Cdd:PRK07251 66 QVMA---TKNTVTSRLRGKNYAMLAGSgVDLYDAEAHFVSNKVIEVQAGDEKIE-LTAETIVINTGAvSNVLpIPGLADS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 156 ANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKV 235
Cdd:PRK07251 142 KHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 236 ESIADGGSQVTVTVTKdgvaQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQ 315
Cdd:PRK07251 222 TEVKNDGDQVLVVTED----ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 316 LAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFV 395
Cdd:PRK07251 298 FTYISLDDFRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAF 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 814539035 396 KLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECF 454
Cdd:PRK07251 378 KVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLF 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
6-461 |
5.42e-60 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 203.17 E-value: 5.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 6 VVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFtKDAKAFGIS----GEVTFDYGI 81
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTEL-RRAAELGIRfiddGEARVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 82 AYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADA----NTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTslsan 157
Cdd:PRK07845 83 VNARVKALAAAQSADIRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRILPTA----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 158 vVTYEEQILS-------RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTIL 230
Cdd:PRK07845 158 -EPDGERILTwrqlydlDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 231 TATKVESIADGGSQVTVTVTkDGvaQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDV 310
Cdd:PRK07845 237 KRSRAESVERTGDGVVVTLT-DG--RTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 311 NGLLQLAHVAEAQGVVAAETIAGaETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGD 390
Cdd:PRK07845 314 TGVLPLASVAAMQGRIAMYHALG-EAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGL 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814539035 391 PSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHM 461
Cdd:PRK07845 393 RDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAARRLMAHD 463
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
1-454 |
1.30e-56 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 193.69 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPK--YWGGVCLNVGCIPSKALlrnaelVHiftkDAKAFGisgevtfD 78
Cdd:PRK08010 1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSnaMYGGTCINIGCIPTKTL------VH----DAQQHT-------D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 79 YGIAYDRSRKVAEG-RVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTEsVTFDNAIIATGSSTRL--VPGTSLS 155
Cdd:PRK08010 64 FVRAIQRKNEVVNFlRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLE-IHGEKIFINTGAQTVVppIPGITTT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 156 ANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKV 235
Cdd:PRK08010 143 PGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 236 ESIADGGSQVTVTvTKDGvaqELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQ 315
Cdd:PRK08010 223 ERISHHENQVQVH-SEHA---QLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 316 LAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFV 395
Cdd:PRK08010 299 FTYISLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 814539035 396 KLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECF 454
Cdd:PRK08010 379 KAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLF 437
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
4-459 |
4.74e-54 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 191.67 E-value: 4.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIV--EPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAK--AFGI-------- 71
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAKlyTYGIytnafkng 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 72 -----------SGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESV--TF--D 136
Cdd:PTZ00153 197 kndpvernqlvADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERGHIVDKNTIKSEKSgkEFkvK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 137 NAIIATGSSTRLVPGTSLSANVVTYEEQILSRE-LPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVS 215
Cdd:PTZ00153 277 NIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEgLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDADVA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 216 KEIEKQF-KKLGVTILTATKVESIADGGSQVTVTV--------TKDGVAQ------ELKAEKVLQAIGFAPNVEGYGLDK 280
Cdd:PTZ00153 357 KYFERVFlKSKPVRVHLNTLIEYVRAGKGNQPVIIghserqtgESDGPKKnmndikETYVDSCLVATGRKPNTNNLGLDK 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 281 AGVALtDRKAIGVDDYMRTN------VGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGD-----------HR 343
Cdd:PTZ00153 437 LKIQM-KRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVNInvenwaskpiiYK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 344 MLPRATFCQPNVASFGLTEQQARNEGY--DVVVAKFPFTANAKA----------------------HGVGDPSGFVKLVA 399
Cdd:PTZ00153 516 NIPSVCYTTPELAFIGLTEKEAKELYPpdNVGVEISFYKANSKVlcennisfpnnsknnsynkgkyNTVDNTEGMVKIVY 595
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 400 DAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVG 459
Cdd:PTZ00153 596 LKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAG 655
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
4-448 |
5.31e-50 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 177.70 E-value: 5.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYW----------GGVCLNVGCIPSKALLRNAELVHIFtKDAKAFG--I 71
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICELPFHpissesiggvGGTCVIRGCVPKKILVYGATFGGEF-EDAKNYGweI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 72 SGEVTFDYG-IAYDRSRKVAegRVAGVH-FLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGS-STRL 148
Cdd:PLN02507 105 NEKVDFNWKkLLQKKTDEIL--RLNGIYkRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSrAQRP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 149 -VPGTSLSanvVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIveFLPRALPNE--DADVSKEIEKQFKKL 225
Cdd:PLN02507 183 nIPGKELA---ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDL--FFRKELPLRgfDDEMRAVVARNLEGR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 226 GVTILTATKVESIADGGSQVTVTVTKdgvAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIY 305
Cdd:PLN02507 258 GINLHPRTNLTQLTKTEGGIKVITDH---GEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 306 AIGDVNGLLQLAHVAEAQGVVAAETIAGAETlTLGDHRMLPRATFCQPNVASFGLTEQQARNEGY-DVVVAKFPFTANAK 384
Cdd:PLN02507 335 AIGDVTNRINLTPVALMEGTCFAKTVFGGQP-TKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKgDILVFTSSFNPMKN 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814539035 385 AHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSE 448
Cdd:PLN02507 414 TISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
4-450 |
8.12e-45 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 163.22 E-value: 8.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQL-GLSTAIVE------PKYW---GGVCLNVGCIPSKALLRNAELV-HIftKDAKAFGIS 72
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLyKKRVAVVDvqthhgPPFYaalGGTCVNVGCVPKKLMVTGAQYMdTL--RESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 73 gevtFDYGIAYDRSRKVAEGRVAGVHFLMKKNK--------ITEIHGYGTFADANTLLV----DLNDGGTESVTFDNAII 140
Cdd:TIGR01423 82 ----FDRSSVKANWKALIAAKNKAVLDINKSYEgmfadtegLTFFLGWGALEDKNVVLVresaDPKSAVKERLQAEHILL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 141 ATGSSTRL--VPGTSLsanVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNY---GVDVTIVEFLPRALPNEDADVS 215
Cdd:TIGR01423 158 ATGSWPQMlgIPGIEH---CISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDSTLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 216 KEIEKQFKKLGVTILT---ATKVESIADGGSQVTVTVTKdgvaqELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIG 292
Cdd:TIGR01423 235 KELTKQLRANGINIMTnenPAKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 293 VDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLgDHRMLPRATFCQPNVASFGLTEQQARNEGYDV 372
Cdd:TIGR01423 310 VDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKT-DHTRVASAVFSIPPIGTCGLVEEDAAKKFEKV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 373 VVAKFPFTanAKAHGVgdpSG------FVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTM 446
Cdd:TIGR01423 389 AVYESSFT--PLMHNI---SGskykkfVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTS 463
|
....
gi 814539035 447 SEAL 450
Cdd:TIGR01423 464 AEEL 467
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
4-448 |
1.74e-44 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 163.63 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKaLLRNAELVHIFTKDAKAFGISGEVTFDYGIAY 83
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKK-IMFNAASIHDILENSRHYGFDTQFSFNLPLLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 84 DRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLL---VDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSA---- 156
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikkVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGknil 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 157 ----------NVVTYEEQILSR-----ELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQ 221
Cdd:PTZ00058 208 iavgnkpifpDVKGKEFTISSDdffkiKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEND 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 222 FKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQElKAEKVLQAIGFAPNVEGYGLdKAGVALTDRKAIGVDDYMRTNV 301
Cdd:PTZ00058 288 MKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYE-HFDYVIYCVGRSPNTEDLNL-KALNIKTPKGYIKVDDNQRTSV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 302 GHIYAIGDVNGL----------------------------------LQLAHVAEAQGVVAAETIAGAETLTlGDHRMLPR 347
Cdd:PTZ00058 366 KHIYAVGDCCMVkknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRT-TNYKLIPS 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 348 ATFCQPNVASFGLTEQQARN----EGYDVVVAKFP--FTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLP 421
Cdd:PTZ00058 445 VIFSHPPIGTIGLSEQEAIDiygkENVKIYESRFTnlFFSVYDMDPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEILQ 524
|
490 500
....*....|....*....|....*..
gi 814539035 422 ELTLAQRWDLTASELARNVHTHPTMSE 448
Cdd:PTZ00058 525 GFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
4-448 |
2.54e-42 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 156.55 E-value: 2.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAI---VEPK----YW--GGVCLNVGCIPSKaLLRNAELVHIFTKDAKAFGISGE 74
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLldfVTPTplgtRWgiGGTCVNVGCIPKK-LMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 75 VTFDYGiaYDRSRKVAEGRVAGVHFL----MKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRL-- 148
Cdd:TIGR01438 82 ETVKHD--WKRLVEAVQNHIGSLNWGyrvaLREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYpg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 149 VPGTSlsanvvtyEEQILSREL------PKSIIIAGAGAIGMEFGYVLKNYGVDVTIvefLPRALPNE--DADVSKEIEK 220
Cdd:TIGR01438 160 IPGAK--------ELCITSDDLfslpycPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRSILLRgfDQDCANKVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 221 QFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKA-IGVDDYMRT 299
Cdd:TIGR01438 229 HMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGkIPADEEEQT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 300 NVGHIYAIGDV-NGLLQLAHVAEAQGVVAAETIAGAETLTLgDHRMLPRATFCQPNVASFGLTEQQA----RNEGYDVVV 374
Cdd:TIGR01438 309 NVPYIYAVGDIlEDKPELTPVAIQAGRLLAQRLFKGSTVIC-DYENVPTTVFTPLEYGACGLSEEKAvekfGEENVEVFH 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814539035 375 AKF-PFTANAKAHgvgDPSGF--VKLVADAKHGE-LLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSE 448
Cdd:TIGR01438 388 SYFwPLEWTIPSR---DNHNKcyAKLVCNKKENErVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAE 462
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
4-448 |
1.44e-41 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 155.42 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYW----------GGVCLNVGCIPSKALLRNAELVHIFtKDAKAFGIsg 73
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCELPFAtissdtlggvGGTCVLRGCVPKKLLVYASKYSHEF-EESRGFGW-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 74 evTFDYGIAYDRSRKVAEG-----RVAGVH-FLMKKNKITEIHGYGTFADANTLLVDlndggTESVTFDNAIIATGSSTR 147
Cdd:PLN02546 157 --KYETEPKHDWNTLIANKnaelqRLTGIYkNILKNAGVTLIEGRGKIVDPHTVDVD-----GKLYTARNILIAVGGRPF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 148 L--VPGtslSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKL 225
Cdd:PLN02546 230 IpdIPG---IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 226 GVTILTATKVESI---ADGG-SQVTVTVTKDGVAQelkaekVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNV 301
Cdd:PLN02546 307 GIEFHTEESPQAIiksADGSlSLKTNKGTVEGFSH------VMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSV 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 302 GHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETlTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVakfpFTA 381
Cdd:PLN02546 381 PSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEP-TKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDV----FTA 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814539035 382 N---AKAHGVGDPSG-FVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSE 448
Cdd:PLN02546 456 NfrpLKATLSGLPDRvFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
346-452 |
2.39e-41 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 143.08 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 346 PRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTL 425
Cdd:pfam02852 2 PSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAAL 81
|
90 100
....*....|....*....|....*..
gi 814539035 426 AQRWDLTASELARNVHTHPTMSEALQE 452
Cdd:pfam02852 82 AIKMGATVEDLANTIHIHPTLSEALVE 108
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
95-340 |
1.63e-29 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 117.60 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 95 AGVHFLMKkNKITEIHgygtfADANTllVDLNDGgtESVTFDNAIIATGSSTRL--VPGTSLsANVVT---YEE-----Q 164
Cdd:COG0446 49 KGIDVRTG-TEVTAID-----PEAKT--VTLRDG--ETLSYDKLVLATGARPRPppIPGLDL-PGVFTlrtLDDadalrE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 165 ILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIaDGGSQ 244
Cdd:COG0446 118 ALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAI-DGDDK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 245 VTVTVTkDGvaQELKAEKVLQAIGFAPNVEgygL-DKAGVALTDRKAIGVDDYMRTNVGHIYAIGDV----------NGL 313
Cdd:COG0446 197 VAVTLT-DG--EEIPADLVVVAPGVRPNTE---LaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCaevphpvtgkTVY 270
|
250 260
....*....|....*....|....*..
gi 814539035 314 LQLAHVAEAQGVVAAETIAGAETLTLG 340
Cdd:COG0446 271 IPLASAANKQGRVAAENILGGPAPFPG 297
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
3-437 |
3.26e-27 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 112.54 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 3 HYDVVVLGAGPGGYVAAIRAAQLGLSTAIV----EPkywggvclnvgCIP------SKALLRNAELVHIFTKDAKAFGis 72
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITvigaEP-----------HPPynrpplSKVLAGETDEEDLLLRPADFYE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 73 gevtfDYGIAYDRSRKVaegrvagvhflmkknkiTEIHgygtfADANTllVDLNDGgtESVTFDNAIIATGSSTRL--VP 150
Cdd:COG1251 68 -----ENGIDLRLGTRV-----------------TAID-----RAART--VTLADG--ETLPYDKLVLATGSRPRVppIP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 151 GTSLsANVVTYeeqilsRELPKSIIIAGAGAIG------------MEFGYVLKNYGVDVTIVEFLPRALPNE-DADVSKE 217
Cdd:COG1251 117 GADL-PGVFTL------RTLDDADALRAALAPGkrvvvigggligLEAAAALRKRGLEVTVVERAPRLLPRQlDEEAGAL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 218 IEKQFKKLGVTILTATKVESIaDGGSQVTVTVTKDGvaQELKAEKVLQAIGFAPNVEgyGLDKAGVAlTDRkAIGVDDYM 297
Cdd:COG1251 190 LQRLLEALGVEVRLGTGVTEI-EGDDRVTGVRLADG--EELPADLVVVAIGVRPNTE--LARAAGLA-VDR-GIVVDDYL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 298 RTNVGHIYAIGDV-------NGLLQLAHV--AEAQGVVAAETIAGAETlTLGDHRMLPRATFCQPNVASFGLTEqqarnE 368
Cdd:COG1251 263 RTSDPDIYAAGDCaehpgpvYGRRVLELVapAYEQARVAAANLAGGPA-AYEGSVPSTKLKVFGVDVASAGDAE-----G 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814539035 369 GYDVVVakfpftanakahgVGDPSG--FVKLVadAKHGELLGGHLVGH--DVAELLPelTLAQRWDLTASELA 437
Cdd:COG1251 337 DEEVVV-------------RGDPARgvYKKLV--LRDGRLVGAVLVGDtsDAGALRQ--LIKNGRPLPPRALL 392
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
4-449 |
2.10e-25 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 108.76 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAI---VEPKY----WG--GVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGE 74
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALfdyVKPSTqgtkWGlgGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 75 VTFDYGiaydRSRKVAEGRVAGVHFL----MKKNKITEIHGYGTFADANTLLVDLNdGGTESVTFDNAIIATGSSTRL-- 148
Cdd:PTZ00052 86 SSFNWG----KLVTTVQNHIRSLNFSyrtgLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIpe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 149 -VPGTSLSAnvVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTI-VEFLPraLPNEDADVSKEIEKQFKKLG 226
Cdd:PTZ00052 161 dVPGAKEYS--ITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVaVRSIP--LRGFDRQCSEKVVEYMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 227 VTILTATKVESIADGGSQVTVTVTkDGVAQELkaEKVLQAIGFAPNVEGYGLDKAGVALTDR-KAIGVDDYmrTNVGHIY 305
Cdd:PTZ00052 237 TLFLEGVVPINIEKMDDKIKVLFS-DGTTELF--DTVLYATGRKPDIKGLNLNAIGVHVNKSnKIIAPNDC--TNIPNIF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 306 AIGDV-NGLLQLAHVAEAQGVVAAETIAGaETLTLGDHRMLPRATFCQPNVASFGLTEQQARNE----GYDVVVAKFPFT 380
Cdd:PTZ00052 312 AVGDVvEGRPELTPVAIKAGILLARRLFK-QSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKygedDIEEYLQEFNTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 381 ANAKAH---------GVGD----PSGFVKLVADAKHGE-LLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTM 446
Cdd:PTZ00052 391 EIAAVHrekherarkDEYDfdvsSNCLAKLVCVKSEDNkVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTD 470
|
...
gi 814539035 447 SEA 449
Cdd:PTZ00052 471 AEV 473
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-332 |
5.79e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 95.96 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCI------PSKalLRNAELVHIFTKDAKAFGIsgevtf 77
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIenypgfPEG--ISGPELAERLREQAERFGA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 78 dygiaydrsrKVAEGRVAGVHFlmkknkiteihgygtfaDANTLLVDLNDGGTesVTFDNAIIATGSSTRLVP------- 150
Cdd:COG0492 73 ----------EILLEEVTSVDK-----------------DDGPFRVTTDDGTE--YEAKAVIIATGAGPRKLGlpgeeef 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 151 -GTSLSANVVT----YEEQ---ILSrelpksiiiagAGAIGMEFGYVLKNYGVDVTIV----EFlpRALPNEdadvskeI 218
Cdd:COG0492 124 eGRGVSYCATCdgffFRGKdvvVVG-----------GGDSALEEALYLTKFASKVTLIhrrdEL--RASKIL-------V 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 219 EKQFKKLGVTILTATKVESIA--DGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGygLDKAGVALTDRKAIGVDDY 296
Cdd:COG0492 184 ERLRANPKIEVLWNTEVTEIEgdGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTEL--LKGLGLELDEDGYIVVDED 261
|
330 340 350
....*....|....*....|....*....|....*..
gi 814539035 297 MRTNVGHIYAIGDVN-GLLQLAHVAEAQGVVAAETIA 332
Cdd:COG0492 262 METSVPGVFAAGDVRdYKYRQAATAAGEGAIAALSAA 298
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
116-413 |
1.88e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 84.32 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 116 ADANTLLV-DLNDGGTESVTFDNAIIATGSSTRLVPGTSLSA-NVVTYEE--------QILSRELPKSIIIAGAGAIGME 185
Cdd:PRK09564 84 AKNKTITVkNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLeNVYTLKSmedglalkELLKDEEIKNIVIIGAGFIGLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 186 FGYVLKNYGVDVTIVEFLPRALPNE-DADVSKEIEKQFKKLGVTILTATKVESIaDGGSQVTVTVTKDGvaqELKAEKVL 264
Cdd:PRK09564 164 AVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSL-IGEDKVEGVVTDKG---EYEADVVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 265 QAIGFAPNVEgyGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDV----NGLLQ------LAHVAEAQGVVAAETIAGA 334
Cdd:PRK09564 240 VATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCatiyNIVSNknvyvpLATTANKLGRMVGENLAGR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 335 ETLTLGdhrMLPRATF--CQPNVASFGLTEQQA--RNEGYDVVVAKfpfTANAKAHGVGDPSGFVKLVADAKHGELLGGH 410
Cdd:PRK09564 318 HVSFKG---TLGSACIkvLDLEAARTGLTEEEAkkLGIDYKTVFIK---DKNHTNYYPGQEDLYVKLIYEADTKVILGGQ 391
|
...
gi 814539035 411 LVG 413
Cdd:PRK09564 392 IIG 394
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-332 |
5.42e-15 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 76.32 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 5 DVVVLGAGPGGYVAAIRAAqlglstaivepkywggvclnvgcipsKALLRNAELV-------HIFtkdaK------AFGI 71
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLR--------------------------KKLGGDAEVTlidpnpyHLF----QpllpevAAGT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 72 --SGEVTFDYgiaydrsRKVAEGrvAGVHFLMkkNKITEIHgygtfADANTllVDLNDGgtESVTFDNAIIATGSSTRL- 148
Cdd:COG1252 53 lsPDDIAIPL-------RELLRR--AGVRFIQ--GEVTGID-----PEART--VTLADG--RTLSYDYLVIATGSVTNFf 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 149 -VPGtsLSANVV---TYEEQILSRELPKSIIIAGAGAIGMEF--------------------GYVLKNYGVD-----VTI 199
Cdd:COG1252 113 gIPG--LAEHALplkTLEDALALRERLLAAFERAERRRLLTIvvvgggptgvelagelaellRKLLRYPGIDpdkvrITL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 200 VEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGsqVTvtvTKDGvaQELKAEKVLQAIGFAPNVEgygLD 279
Cdd:COG1252 191 VEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG--VT---LEDG--EEIPADTVIWAAGVKAPPL---LA 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814539035 280 KAGVALTDRKAIGVDDYMRTnVGH--IYAIGDV--------NGLLQLAHVAEAQGVVAAETIA 332
Cdd:COG1252 261 DLGLPTDRRGRVLVDPTLQV-PGHpnVFAIGDCaavpdpdgKPVPKTAQAAVQQAKVLAKNIA 322
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
182-252 |
1.99e-14 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 68.38 E-value: 1.99e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814539035 182 IGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKD 252
Cdd:pfam00070 10 IGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
133-336 |
3.11e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 65.62 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 133 VTFDNAIIATGSSTRL--VPGTSLSANVV--TYEE--QILS-RELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPR 205
Cdd:TIGR02374 95 LSYDKLILATGSYPFIlpIPGADKKGVYVfrTIEDldAIMAmAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 206 ALPNE-DADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVtKDGvaQELKAEKVLQAIGFAPNVE---GYGLDKA 281
Cdd:TIGR02374 175 LMAKQlDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRF-KDG--SSLEADLIVMAAGIRPNDElavSAGIKVN 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814539035 282 GvaltdrkAIGVDDYMRTNVGHIYAIGDV---NGLLQ-LAHVAEAQGVVAAETIAGAET 336
Cdd:TIGR02374 252 R-------GIIVNDSMQTSDPDIYAVGECaehNGRVYgLVAPLYEQAKVLADHICGVEC 303
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
194-339 |
1.09e-10 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 63.01 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 194 GVDVTIVE----FLPRALPNEdadVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDgvaQELKAEKVLQAIGF 269
Cdd:PRK04965 164 GKAVTLVDnaasLLASLMPPE---VSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSG---RSIEVDAVIAAAGL 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814539035 270 APNVegyGLDK-AGVALtdRKAIGVDDYMRTNVGHIYAIGD---VNGLLqLAHVAEAQ--GVVAAETIAGAET-LTL 339
Cdd:PRK04965 238 RPNT---ALARrAGLAV--NRGIVVDSYLQTSAPDIYALGDcaeINGQV-LPFLQPIQlsAMALAKNLLGQNTpLKL 308
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
5-60 |
2.72e-07 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 52.55 E-value: 2.72e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 814539035 5 DVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKywGGVCLNVGCIPSKALLRNAELVH 60
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHN--TDTIAELSCNPSIGGIAKGHLVR 54
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
190-373 |
4.34e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 52.09 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 190 LKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIadGGSQVTVtvtKDGVAQELkaEKVLQAIGF 269
Cdd:PRK13512 167 LYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI--NGNEVTF---KSGKVEHY--DMIIEGVGT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 270 APNVEGygLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDV-----NGLLQLAHVAEAQGV-----VAAETIAGAETLT- 338
Cdd:PRK13512 240 HPNSKF--IESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIitshyRHVDLPASVPLAWGAhraasIVAEQIAGNDTIEf 317
|
170 180 190
....*....|....*....|....*....|....*...
gi 814539035 339 ---LGDHRMlpraTFCQPNVASFGLTEQQARNEGYDVV 373
Cdd:PRK13512 318 kgfLGNNIV----KFFDYTFASVGVKPNELKQFDYKMV 351
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
5-34 |
1.06e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 50.69 E-value: 1.06e-06
10 20 30
....*....|....*....|....*....|
gi 814539035 5 DVVVLGAGPGGYVAAIRAAQLGLSTAIVEP 34
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVER 30
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
4-39 |
3.49e-06 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 49.26 E-value: 3.49e-06
10 20 30
....*....|....*....|....*....|....*..
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVE-PKYWGG 39
Cdd:PRK07843 8 YDVVVVGSGAAGMVAALTAAHRGLSTVVVEkAPHYGG 44
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-33 |
3.62e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 3.62e-06
10 20 30
....*....|....*....|....*....|...
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLE 33
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
1-33 |
1.48e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 47.14 E-value: 1.48e-05
10 20 30
....*....|....*....|....*....|...
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLE 33
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
227-310 |
1.84e-05 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 47.05 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 227 VTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYgLDKAGVALTDRKAIGVD-DYMRTNVGHIY 305
Cdd:COG0493 327 VTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDeETYQTSLPGVF 405
|
....*
gi 814539035 306 AIGDV 310
Cdd:COG0493 406 AGGDA 410
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
4-90 |
1.88e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 47.06 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVE--PKYWGGVCLNVGC--IPSKALLRNAELVHIFTKDAKAFgisGEVTFDY 79
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEkqDKVGGSTAMSGGVlwLPNNPLMKAAGVPDSHEDALAYL---DAVVGDQ 83
|
90
....*....|.
gi 814539035 80 GIAYDRSRKVA 90
Cdd:PRK12844 84 GPASSPERREA 94
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
197-310 |
2.53e-05 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 46.69 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 197 VTIVEFLP------------RALPNedadvskeiekqfkklgVTILTATKVESIADGGSQVTVTVTKD---GVAQELKAE 261
Cdd:PRK15317 377 VTVLEFAPelkadqvlqdklRSLPN-----------------VTIITNAQTTEVTGDGDKVTGLTYKDrttGEEHHLELE 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 814539035 262 KVLQAIGFAPNVEgygLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDV 310
Cdd:PRK15317 440 GVFVQIGLVPNTE---WLKGTVELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
195-333 |
2.91e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 46.30 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 195 VDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSqvtvtVTKDGvaQELKAEKVLQAIGFAPNVE 274
Cdd:PTZ00318 211 CKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEV-----VLKDG--EVIPTGLVVWSTGVGPGPL 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814539035 275 GYGLDkagVALTDRKAIGVDDYMRT-NVGHIYAIGDV-----NGLLQLAHVAEAQGVVAAETIAG 333
Cdd:PTZ00318 284 TKQLK---VDKTSRGRISVDDHLRVkPIPNVFALGDCaaneeRPLPTLAQVASQQGVYLAKEFNN 345
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
5-33 |
4.09e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 45.74 E-value: 4.09e-05
10 20
....*....|....*....|....*....
gi 814539035 5 DVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVE 29
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
190-309 |
6.76e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 45.49 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 190 LKNYGVDVTIVEFLPRALPNE-DADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVT-KDGvaQELKAEKVLQAI 267
Cdd:PRK14989 164 LKNLGVETHVIEFAPMLMAEQlDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRfADG--SELEVDFIVFST 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 814539035 268 GFAPNvegyglDK----AGVALTDRKAIGVDDYMRTNVGHIYAIGD 309
Cdd:PRK14989 242 GIRPQ------DKlatqCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
256-309 |
8.29e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 44.77 E-value: 8.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 814539035 256 QELKAEKVLQAIGFAPNVEGYgLDKAGVALTDRKAIGVDDY-MRTNVGHIYAIGD 309
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNaYQTSNPKVFAAGD 438
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
3-32 |
1.52e-04 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 44.26 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|
gi 814539035 3 HYDVVVLGAGPGGYVAAIRAAQLGLSTAIV 32
Cdd:PRK07803 8 SYDVVVIGAGGAGLRAAIEARERGLRVAVV 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
4-33 |
1.72e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 1.72e-04
10 20 30
....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIE 30
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-34 |
1.96e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.39 E-value: 1.96e-04
10 20 30
....*....|....*....|....*....|....
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEP 34
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
4-148 |
1.97e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 43.08 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNA-ELVHIFTKDAKA-----FGISGEVTF 77
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGALSPRALEELDlPGELIVNLVRGArffspNGDSVEIPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814539035 78 DYGIAYDRSRK------VAEGRVAGVHFLMKK-NKITEIHGygtfaDANTLLVdlnDGGTESVTFDNAIIATGSSTRL 148
Cdd:TIGR02032 81 ETELAYVIDRDafdeqlAERAQEAGAELRLGTrVLDVEIHD-----DRVVVIV---RGSEGTVTAKIVIGADGSRSIV 150
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-35 |
2.22e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 43.35 E-value: 2.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPK 35
Cdd:PRK07494 5 KEHTDIAVIGGGPAGLAAAIALARAGASVALVAPE 39
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
3-32 |
3.70e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.53 E-value: 3.70e-04
10 20 30
....*....|....*....|....*....|
gi 814539035 3 HYDVVVLGAGPGGYVAAIRAAQLGLSTAIV 32
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
2-47 |
6.32e-04 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 42.10 E-value: 6.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 814539035 2 THYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE--PKYWGGVCLNVGCI 47
Cdd:PRK12835 10 REVDVLVVGSGGGGMTAALTAAARGLDTLVVEksAHFGGSTALSGGGI 57
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
4-39 |
8.00e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 42.03 E-value: 8.00e-04
10 20 30
....*....|....*....|....*....|....*..
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVE-PKYWGG 39
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVErTEYVGG 53
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-33 |
1.16e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 41.00 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|...
gi 814539035 1 MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLE 36
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
4-33 |
3.78e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.81 E-value: 3.78e-03
10 20 30
....*....|....*....|....*....|
gi 814539035 4 YDVVVLGAGPGGYVAAIRAAQLGLSTAIVE 33
Cdd:PRK12839 9 YDVVVVGSGAGGLSAAVAAAYGGAKVLVVE 38
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
223-331 |
6.80e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 38.62 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814539035 223 KKLGVTILTATK-VESIADGGSQVTVTVTK----------------DGVAQELKAEKVLQAIGFAPNVEGYGLDKaGVAL 285
Cdd:PRK11749 322 KEEGVEFEWLAApVEILGDEGRVTGVEFVRmelgepdasgrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTP-GLEL 400
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 814539035 286 TDRKAIGVDD-YMRTNVGHIYAIGD-VNGllqLAHVAEA--QGVVAAETI 331
Cdd:PRK11749 401 NRWGTIIADDeTGRTSLPGVFAGGDiVTG---AATVVWAvgDGKDAAEAI 447
|
|
| |
