|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-472 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 683.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTDKEGKLALGGTCLNVGCIPSKALLDSSWKFHEAQDGFAIHGIN 80
Cdd:PRK06327 1 MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 HAGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLL----AGKKVEVTKPDGSVeiIEAENVILAPGSRPI 156
Cdd:PRK06327 81 VDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETV--ITAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 157 DIPPAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQG 236
Cdd:PRK06327 159 HLPGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 237 LDIKLGARVTGSKVNGDEVVVNYTDANGE-QNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVY 315
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGVSVAYTDADGEaQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 316 AIGDVVRGMMLAHKASEEGIMVVERIKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMA 395
Cdd:PRK06327 319 AIGDVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495293109 396 ANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIHI 472
Cdd:PRK06327 399 MGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLHF 475
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
2-467 |
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: 577.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 2 SQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDgFAIHGINH 81
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-------LGGTCLNVGCIPSKALLHAAEVAHEARH-AAEFGISA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 82 AGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKpdgsVEIIEAENVILAPGSRPIDIPPA 161
Cdd:COG1249 73 GAPSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 162 PVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKL 241
Cdd:COG1249 149 GLDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 242 GARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDVV 321
Cdd:COG1249 229 GAKVTSVEKTGDGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 322 RGMMLAHKASEEGIMVVERIKGHKAQ-MNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTG 400
Cdd:COG1249 309 GGPQLAHVASAEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495293109 401 GFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNG 467
Cdd:COG1249 389 GFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-472 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 553.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKytDKegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDGfAIHGIN 80
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK--EK-----LGGTCLNRGCIPSKALLHAAERADEARHS-EDFGIK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 HAGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSvEIIEAENVILAPGSRPIDIPP 160
Cdd:PRK06416 73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE-QTYTAKNIILATGSRPRELPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 161 APVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIK 240
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 241 LGARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDeRGFVHVDDHCATTVPGVYAIGDV 320
Cdd:PRK06416 232 TGAKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 321 VRGMMLAHKASEEGIMVVERIKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTG 400
Cdd:PRK06416 311 VGGPMLAHKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495293109 401 GFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIHI 472
Cdd:PRK06416 391 GFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
5-471 |
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: 538.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDgFAIHGINHAGV 84
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEY-------LGGTCLNVGCIPTKALLHSAEVYDEIKH-AKDLGIEVENV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 85 TMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSvEIIEAENVILAPGSRPIDIP-PAPV 163
Cdd:TIGR01350 74 SVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGE-ETLEAKNIIIATGSRPRSLPgPFDF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 164 DQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGA 243
Cdd:TIGR01350 153 DGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 244 RVTGSKVNGDEVVVNyTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDVVRG 323
Cdd:TIGR01350 233 KVTAVEKNDDQVTYE-NKGGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 324 MMLAHKASEEGIMVVERIKG-HKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTGGF 402
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENIAGkEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495293109 403 VKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIH 471
Cdd:TIGR01350 392 VKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
3-472 |
8.56e-178 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 506.25 E-value: 8.56e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDgFAIHGINHA 82
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGP-------LGGTCLNVGCIPSKALIAAAEAFHEAKH-AEEFGIHAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 83 GVTMDVPAMVGRKANIVKGLTSGV-ATLFKANGVTSIQGHGKLLAGKKVEVTKpdgsvEIIEAENVILAPGSRPIDIPPA 161
Cdd:PRK06292 74 GPKIDFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEVNG-----ERIEAKNIVIATGSRVPPIPGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 162 -PVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQgLDIK 240
Cdd:PRK06292 149 wLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 241 LGARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDV 320
Cdd:PRK06292 228 LGAKVTSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 321 VRGMMLAHKASEEGIMVVERIKGHKAQ-MNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDT 399
Cdd:PRK06292 308 NGKPPLLHEAADEGRIAAENAAGDVAGgVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKN 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 400 GGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIHI 472
Cdd:PRK06292 388 DGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIHG 460
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-462 |
1.74e-104 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 319.46 E-value: 1.74e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKytdkegkLALGGTCLNVGCIPSKALLDSSWKFHEAQDGfAIHGIN 80
Cdd:PRK06370 2 PAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIER-------GLLGGTCVNTGCVPTKTLIASARAAHLARRA-AEYGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 HAG-VTMDVPAMVGRKANIVKGLTSGVATLFKA-NGVTSIQGHGKLLAGKKVEVtkpDGsvEIIEAENVILAPGSRPIdI 158
Cdd:PRK06370 74 VGGpVSVDFKAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRV---GG--ETLRAKRIFINTGARAA-I 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 159 PPAP-VDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGL 237
Cdd:PRK06370 148 PPIPgLDEVGYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 238 DIKLGARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAI 317
Cdd:PRK06370 228 DVRLNAECIRVERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 318 GDVVRGMMLAHKASEEGIMVVERIKGHKAQMNYDLI-PSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAA 396
Cdd:PRK06370 308 GDCNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIvPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEK 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495293109 397 NDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAA 462
Cdd:PRK06370 388 GETQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLA 453
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-463 |
2.35e-96 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 298.22 E-value: 2.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklALGGTCLNVGCIPSKAL----LDSSWkFHeaQDGFAI 76
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYR------NVGGGCTHTGTIPSKALreavLRLIG-FN--QNPLYS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 77 HGINHAGVTMdvPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSVEIIEAENVILAPGSRPI 156
Cdd:PRK05249 73 SYRVKLRITF--ADLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 157 DIPPAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSkEALKT-LTKQ 235
Cdd:PRK05249 151 RPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEIS-DALSYhLRDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 236 GLDIKLGARVTGSKVNGDEVVVnyTDANGEQnITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVY 315
Cdd:PRK05249 230 GVTIRHNEEVEKVEGGDDGVIV--HLKSGKK-IKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 316 AIGDVVRGMMLAHKASEEGIMVVERIKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMA 395
Cdd:PRK05249 307 AVGDVIGFPSLASASMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQI 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495293109 396 ANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAAL 463
Cdd:PRK05249 387 AGDNVGMLKILFHRETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAEAYRVAAL 454
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
5-466 |
1.17e-93 |
|
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: 291.63 E-value: 1.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDGFaiHGINHAGV 84
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGP-------LGGTCVNVGCVPSKMLLRAAEVAHYARKPP--FGGLAATV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 85 TMDVPAMVGRKANIVKGL-TSGVATLFKANGVTSIQGHGKLLAGKKVEVtkpDGSVEIIEAENVILAPGSRPiDIPPAP- 162
Cdd:TIGR02053 72 AVDFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV---DLGREVRGAKRFLIATGARP-AIPPIPg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 163 VDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLG 242
Cdd:TIGR02053 148 LKEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 243 ARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDVVR 322
Cdd:TIGR02053 228 AQVKAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 323 GMMLAHKASEEGIMVVER-IKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTGG 401
Cdd:TIGR02053 308 GLQLEYVAAKEGVVAAENaLGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495293109 402 FVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVN 466
Cdd:TIGR02053 388 FIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFY 452
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
3-460 |
6.93e-81 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 257.76 E-value: 6.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEkytdkEGKLALGGTCLNVGCIPSKALL---DSSWKFHEAqdgfaihgI 79
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVE-----ESKAMYGGTCINIGCIPTKTLLvaaEKNLSFEQV--------M 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 80 NHAGVtmdvpaMVGRKANIVKGLTSGvatlfkaNGVTSIQGHGKLLAGKKVEVTKPDGSVEIiEAENVILAPGSRPIDIP 159
Cdd:PRK07251 69 ATKNT------VTSRLRGKNYAMLAG-------SGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 160 -PAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLD 238
Cdd:PRK07251 135 iPGLADSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 239 IKLGARVTGSKVNGDEVVVNytdANGEqNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIG 318
Cdd:PRK07251 215 FLLNAHTTEVKNDGDQVLVV---TEDE-TYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 319 DVVRGMMLAHKASEEGIMVVERIKGHKaqmNYDL-----IPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRA 393
Cdd:PRK07251 291 DVNGGPQFTYISLDDFRIVFGYLTGDG---SYTLedrgnVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495293109 394 MAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHE 460
Cdd:PRK07251 368 HVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLND 434
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-334 |
2.13e-77 |
|
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: 244.15 E-value: 2.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEkytdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDGfaihginhagv 84
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----------DEGTCPYGGCVLSKALLGAAEAPEIASLW----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 85 tmdvPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVevtkpDGSVEIIEAENVILAPGSRPIDiPPAP-V 163
Cdd:pfam07992 60 ----ADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELV-----DGDGETITYDRLVIATGARPRL-PPIPgV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 164 DQNVI-----VDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLD 238
Cdd:pfam07992 130 ELNVGflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 239 IKLGARVTgsKVNGDEVVVNYTDANGEQnITFDKLIVAVGRRPVTTDLLAAdcGVTLDERGFVHVDDHCATTVPGVYAIG 318
Cdd:pfam07992 210 VRLGTSVK--EIIGDGDGVEVILKDGTE-IDADLVVVAIGRRPNTELLEAA--GLELDERGGIVVDEYLRTSVPGIYAAG 284
|
330
....*....|....*..
gi 495293109 319 DV-VRGMMLAHKASEEG 334
Cdd:pfam07992 285 DCrVGGPELAQNAVAQG 301
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-456 |
4.44e-77 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 248.15 E-value: 4.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYtdkegklALGGTCLNVGCIPSKALLDSSwKFHEA-QDGFAIHGI 79
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAK-------RLGGTCVNVGCVPKKLMWYGA-QIAEAfHDYAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 80 NHAGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKpdgsvEIIEAENVILAPGSRPIdIP 159
Cdd:PRK06116 73 DVTENKFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNG-----ERYTADHILIATGGRPS-IP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 160 PAPVDQNVIvDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDI 239
Cdd:PRK06116 147 DIPGAEYGI-TSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 240 KLGARVTGSKVNGDEVVVNYTDaNGEQnITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD 319
Cdd:PRK06116 226 HTNAVPKAVEKNADGSLTLTLE-DGET-LTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 320 VVRGMMLAHKASEEGIMVVERIKGHK--AQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTfpFAASGRAMAAN 397
Cdd:PRK06116 304 VTGRVELTPVAIAAGRRLSERLFNNKpdEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKV--YRSSFTPMYTA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 398 DTGG----FVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSE 456
Cdd:PRK06116 382 LTGHrqpcLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
5-464 |
6.09e-77 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 247.56 E-value: 6.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAqlGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLdsswkfHEAQDGFAIHGINHAGV 84
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFA--DKRIAIVEKGT-------FGGTCLNVGCIPTKMFV------YAADVARTIREAARLGV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 85 TMDVPAMvgRKANIVK---GLTSGVAtlfkANG----------VTSIQGHGKLLAGKKVEVtkpdGSVEIIEAENVILAP 151
Cdd:PRK07846 67 DAELDGV--RWPDIVSrvfGRIDPIA----AGGeeyrgrdtpnIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 152 GSRPIdIPPAPVDQNVIV---DSTGALEfqSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSkEA 228
Cdd:PRK07846 137 GSRPV-IPPVIADSGVRYhtsDTIMRLP--ELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDIS-ER 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 229 LKTLTKQGLDIKLGARVTGSKVNGDEVVVNYTDAngeQNITFDKLIVAVGRRPvTTDLL-AADCGVTLDERGFVHVDDHC 307
Cdd:PRK07846 213 FTELASKRWDVRLGRNVVGVSQDGSGVTLRLDDG---STVEADVLLVATGRVP-NGDLLdAAAAGVDVDEDGRVVVDEYQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 308 ATTVPGVYAIGDVVRGMMLAHKASEEGimvveRIKGHK-------AQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEV 380
Cdd:PRK07846 289 RTSAEGVFALGDVSSPYQLKHVANHEA-----RVVQHNllhpddlIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 381 NVGTFPFA--ASGRAMaaNDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGM-MVFSHPTLSEA 457
Cdd:PRK07846 364 TVKVQNYGdvAYGWAM--EDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARgQYWIHPALPEV 441
|
....*..
gi 495293109 458 LHEAALA 464
Cdd:PRK07846 442 VENALLG 448
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
3-460 |
3.14e-68 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 224.66 E-value: 3.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEkytdkEGKLALGGTCLNVGCIPSKALLdsswkfHEAQDgfaihginha 82
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAIIE-----QSAQMYGGTCINIGCIPTKTLV------HDAEQ---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 83 gvTMDVPAMVGRKANIVKGL-TSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSVEiIEAENVILAPGSRPI--DIP 159
Cdd:NF040477 61 --HQDFSTAMQRKSSVVGFLrDKNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQE-LRGEKIFINTGAQSVlpPIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 160 PAPVDQNVIvDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDI 239
Cdd:NF040477 138 GLTTTPGVY-DSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 240 KLGARVTGSKVNGDEVVVNYtdANGEQniTFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD 319
Cdd:NF040477 217 ILNAQVQRVSSHEGEVQLET--AEGVL--TVDALLVASGRKPATAGLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 320 VVRGMMLAHKASEEGIMVVERIKGHKAQMNYDL--IPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAAN 397
Cdd:NF040477 293 VTGGLQFTYISLDDFRIVRDSLLGEGKRSTDDRqnVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMN 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 398 DTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHE 460
Cdd:NF040477 373 DTRGVLKAVVDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLND 435
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
5-458 |
4.69e-67 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 222.02 E-value: 4.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYtdkegklALGGTCLNVGCIPSKALL---DSSWKFHEAQD-GFAIHGIN 80
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVEAK-------KLGGTCVNVGCVPKKVMWyasDLAERMHDAADyGFYQNDEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 hagvTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDgsveiIEAENVILAPGSRPIdIPP 160
Cdd:TIGR01421 76 ----TFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPS-FPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 161 APVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDI- 239
Cdd:TIGR01421 146 NIPGAELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 240 KLGARVTGSKVNGDEVVVNYTDanGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD 319
Cdd:TIGR01421 226 KLSKPVKVEKTVEGKLVIHFED--GKSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 320 VVRGMMLAHKASEEGIMVVERIKGHK--AQMNYDLIPSVIYTHPEIAWVGKTE-QALKAEGVE-VNVGTFPFAASGRAMA 395
Cdd:TIGR01421 304 VVGKVELTPVAIAAGRKLSERLFNGKtdDKLDYNNVPTVVFSHPPIGTIGLTEkEAIEKYGKEnIKVYNSSFTPMYYAMT 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 396 ANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEAL 458
Cdd:TIGR01421 384 SEKQKCRMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-471 |
1.35e-65 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 223.25 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKytdkeGKLALGGTCLNVGCIPSKALLDSSWKFHEAQ--DGFAIHGIN 80
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFTG-----DDDSIGGTCVNVGCIPSKALLYATGKYRELKnlAKLYTYGIY 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 HAG------------------VTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLA--GKKVE--VTKPDGS 138
Cdd:PTZ00153 190 TNAfkngkndpvernqlvadtVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYerGHIVDknTIKSEKS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 139 VEIIEAENVILAPGSRPiDIPP-APVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFL 217
Cdd:PTZ00153 270 GKEFKVKNIIIATGSTP-NIPDnIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 218 MAADTAVSKEALKTLTK-QGLDIKLGAR---VTGSKvNGDEVVVNYTDAN-GEQN-----------ITFDKLIVAVGRRP 281
Cdd:PTZ00153 349 PLLDADVAKYFERVFLKsKPVRVHLNTLieyVRAGK-GNQPVIIGHSERQtGESDgpkknmndikeTYVDSCLVATGRKP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 282 VTTDLLAADCGVTLDeRGFVHVDDHCAT------TVPGVYAIGDVVRGMMLAHKASEEGIMVVERIKGHKAQ-------- 347
Cdd:PTZ00153 428 NTNNLGLDKLKIQMK-RGFVSVDEHLRVlredqeVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninven 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 348 -----MNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFP--FAASGRAMAAND---------------------- 398
Cdd:PTZ00153 507 waskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEIsfYKANSKVLCENNisfpnnsknnsynkgkyntvdn 586
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 399 TGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAALAVNGGAIH 471
Cdd:PTZ00153 587 TEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
4-460 |
3.34e-64 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 214.11 E-value: 3.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTACIEkytdkEGKLALGGTCLNVGCIPSKALLdsswkfHEAQDgfaiHGinhag 83
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIE-----QSNAMYGGTCINIGCIPTKTLV------HDAQQ----HT----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 84 vtmDVPAMVGRKANIVKGL-TSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSVEIiEAENVILAPGSRPIdIPPAP 162
Cdd:PRK08010 63 ---DFVRAIQRKNEVVNFLrNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEI-HGEKIFINTGAQTV-VPPIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 163 --VDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIK 240
Cdd:PRK08010 138 giTTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 241 LGARVtgSKVNGDEVVVNYTDANGEQNItfDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDV 320
Cdd:PRK08010 218 LNAHV--ERISHHENQVQVHSEHAQLAV--DALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 321 VRGMMLAHKASEEGIMVVERI--KGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAAND 398
Cdd:PRK08010 294 TGGLQFTYISLDDYRIVRDELlgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMND 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495293109 399 TGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHE 460
Cdd:PRK08010 374 TRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLND 435
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
5-465 |
1.04e-62 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 210.38 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAqlGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFHEAQDG--FAIHG-INH 81
Cdd:TIGR03452 3 YDLIIIGTGSGNSIPDPRFA--DKRIAIVEKGT-------FGGTCLNVGCIPTKMFVYAAEVAQSIGESarLGIDAeIDS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 82 agvtMDVPAMVGRK-ANIVKGLTSGVATLFKANGVTSI---QGHGKLLAGKKVEVtkpdGSVEIIEAENVILAPGSRPId 157
Cdd:TIGR03452 74 ----VRWPDIVSRVfGDRIDPIAAGGEDYRRGDETPNIdvyDGHARFVGPRTLRT----GDGEEITGDQIVIAAGSRPY- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 158 IPPAPVDQNV-IVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSkEALKTLTKQG 236
Cdd:TIGR03452 145 IPPAIADSGVrYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDIS-DRFTEIAKKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 237 LDIKLGARVTGSKVNGDEVVVNYTDANgeqNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYA 316
Cdd:TIGR03452 224 WDIRLGRNVTAVEQDGDGVTLTLDDGS---TVTADVLLVATGRVPNGDLLDAEAAGVEVDEDGRIKVDEYGRTSARGVWA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 317 IGDVVRGMMLAHKASEEGIMVVERIKGHKA--QMNYDLIPSVIYTHPEIAWVGKTEQALKAEG--VEVNVGTFPFAASGR 392
Cdd:TIGR03452 301 LGDVSSPYQLKHVANAEARVVKHNLLHPNDlrKMPHDFVPSAVFTHPQIATVGLTEQEAREAGhdITVKIQNYGDVAYGW 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495293109 393 AMaaNDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGM-MVFSHPTLSEALHEAALAV 465
Cdd:TIGR03452 381 AM--EDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPALPEVVENALLGL 452
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
2-462 |
1.62e-62 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 212.70 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 2 SQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALLDSSWKFH-EAQDGFaihgin 80
Cdd:PRK13748 96 ERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGT-------IGGTCVNVGCVPSKIMIRAAHIAHlRRESPF------ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 81 HAGVTMDVPAMVgrKANIVKGLTSGVATLFKAN---------GVTSIQGHGKLLAGKKVEVTKPDGSVEIIEAENVILAP 151
Cdd:PRK13748 163 DGGIAATVPTID--RSRLLAQQQARVDELRHAKyegildgnpAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 152 GSRPIdIPPAP-VDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLeALDTFLMAADTAVSKEALK 230
Cdd:PRK13748 241 GASPA-VPPIPgLKETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTIL-ARSTLFFREDPAIGEAVTA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 231 TLTKQGLDIKLGARVTGSKVNGDEVVVnyTDANGEqnITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATT 310
Cdd:PRK13748 319 AFRAEGIEVLEHTQASQVAHVDGEFVL--TTGHGE--LRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 311 VPGVYAIGDVVRGMMLAHKASEEGIMVVERIKGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAAS 390
Cdd:PRK13748 395 VPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNV 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495293109 391 GRAMAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAA 462
Cdd:PRK13748 475 PRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-462 |
8.67e-58 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 197.78 E-value: 8.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 7 VVVIGAGPGGYVAAIKAAQLGLSTACIEKytdkEGklaLGGTCLNVGCIPSKALLDSSW---KFHEAQD-GFAIHGINHA 82
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIER----DG---LGGAAVLTDCVPSKTLIATAEvrtELRRAAElGIRFIDDGEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 83 GVtmDVPAMVGRkaniVKGLT----SGVATLFKANGVTSIQGHGKL----LAGKKVEVTKPDGSVEIIEAENVILAPGSR 154
Cdd:PRK07845 77 RV--DLPAVNAR----VKALAaaqsADIRARLEREGVRVIAGRGRLidpgLGPHRVKVTTADGGEETLDADVVLIATGAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 155 PIDIPPAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMA--ADTAVSKEalKTL 232
Cdd:PRK07845 151 PRILPTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGedADAAEVLE--EVF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 233 TKQGLDIKLGARVTGSKVNGDEVVVNYTDAngeQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVP 312
Cdd:PRK07845 229 ARRGMTVLKRSRAESVERTGDGVVVTLTDG---RTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 313 GVYAIGDVVRGMMLAHKASEEGimvveRIKGHKA------QMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFP 386
Cdd:PRK07845 306 GIYAAGDCTGVLPLASVAAMQG-----RIAMYHAlgeavsPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLP 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495293109 387 FAASGRAMAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEALHEAA 462
Cdd:PRK07845 381 LATNPRAKMSGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLSGSITEAA 456
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
5-456 |
1.67e-56 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 195.42 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIE---KYTDKEGKLALGGTCLNVGCIPSKALLDSSWKFHEAQD----GFAIH 77
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDaknyGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 78 GinhaGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSVEIIEAENVILAPGSRPId 157
Cdd:PLN02507 106 E----KVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQ- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 158 iPPAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGL 237
Cdd:PLN02507 181 -RPNIPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 238 DIKLGARVTGSKVNGDEVVVnYTDaNGEQnITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAI 317
Cdd:PLN02507 260 NLHPRTNLTQLTKTEGGIKV-ITD-HGEE-FVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 318 GDVVRGMMLAHKASEEGIMVVERIKGHKA-QMNYDLIPSVIYTHPEIAWVGKTE-QALKAEGVEVNVGTFPFAASGRAMA 395
Cdd:PLN02507 337 GDVTNRINLTPVALMEGTCFAKTVFGGQPtKPDYENVACAVFCIPPLSVVGLSEeEAVEQAKGDILVFTSSFNPMKNTIS 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495293109 396 ANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSE 456
Cdd:PLN02507 417 GRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
4-456 |
3.33e-54 |
|
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: 188.91 E-value: 3.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTACIE--KYTDKEGKLALGGTCLNVGCIPSK-----ALLDSSWKFHEAQDGFAI 76
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvTPTPLGTRWGIGGTCVNVGCIPKKlmhqaALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 77 HGINHagvtmDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTKPDGSVEIIEAENVILAPGSRPi 156
Cdd:TIGR01438 82 ETVKH-----DWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 157 DIPPAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLeALDTFLMAADTAVSKEALKTLTKQG 236
Cdd:TIGR01438 156 RYPGIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDCANKVGEHMEEHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 237 LDIKLGARVTGSKVNGDEVVVNYTDANGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDER-GFVHVDDHCATTVPGVY 315
Cdd:TIGR01438 235 VKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 316 AIGDVVRGMM-LAHKASEEGIMVVERI-KGHKAQMNYDLIPSVIYTHPEIAWVGKTE----QALKAEGVEVNVGTF-PFA 388
Cdd:TIGR01438 315 AVGDILEDKPeLTPVAIQAGRLLAQRLfKGSTVICDYENVPTTVFTPLEYGACGLSEekavEKFGEENVEVFHSYFwPLE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495293109 389 ASgraMAANDTGGF--VKVIADAKTD-RVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSE 456
Cdd:TIGR01438 395 WT---IPSRDNHNKcyAKLVCNKKENeRVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAE 462
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-458 |
9.28e-51 |
|
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: 179.78 E-value: 9.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 2 SQKFDVVVIGAGPGGYVAAIKAAQL-GLSTACIEKYTDKEGKL--ALGGTCLNVGCIPSKALLDSSWKFHEAQD--GFAI 76
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLREsaGFGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 77 HgINHAGVTMDVPAMVGRKANIVKGLTSGVATLFK-ANGVTSIQGHGKLLAGKKV---EVTKPDGSV-EIIEAENVILAP 151
Cdd:TIGR01423 81 E-FDRSSVKANWKALIAAKNKAVLDINKSYEGMFAdTEGLTFFLGWGALEDKNVVlvrESADPKSAVkERLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 152 GSRPiDIPPAPVDQNVIvDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSR---LGAQVTVLEALDTFLMAADTAVSKEA 228
Cdd:TIGR01423 160 GSWP-QMLGIPGIEHCI-SSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 229 LKTLTKQGLDIKlgarvtgSKVNGDEVVVNytdANGEQNITF--------DKLIVAVGRRPVTTDLLAADCGVTLDERGF 300
Cdd:TIGR01423 238 TKQLRANGINIM-------TNENPAKVTLN---ADGSKHVTFesgktldvDVVMMAIGRVPRTQTLQLDKVGVELTKKGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 301 VHVDDHCATTVPGVYAIGDVVRGMMLAHKASEEGIMVVERIKGHKAQ-MNYDLIPSVIYTHPEIAWVGKTEQALKAEGVE 379
Cdd:TIGR01423 308 IQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRkTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 380 VNVGTFPFAASGRAMAANDTGGFV-KVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSEAL 458
Cdd:TIGR01423 388 VAVYESSFTPLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
5-456 |
2.71e-50 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 180.07 E-value: 2.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEK-----YTDKEGklALGGTCLNVGCIPSKALLDSSWKFHEAQDGFAIHGI 79
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCELpfatiSSDTLG--GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 80 NHAGVTMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVtkpDGsvEIIEAENVILAPGSRPIdIP 159
Cdd:PLN02546 158 YETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV---DG--KLYTARNILIAVGGRPF-IP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 160 PAPVDQNVIvDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDI 239
Cdd:PLN02546 232 DIPGIEHAI-DSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 240 KLGARVTGSKVNGDEVVVNYTdaNGEQNITFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD 319
Cdd:PLN02546 311 HTEESPQAIIKSADGSLSLKT--NKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGD 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 320 VVRGMMLAHKASEEGIMVVERIKGHK-AQMNYDLIPSVIYTHPEIAWVGKTE-QALKAEGvEVNVgtfpFAASGRAMAAN 397
Cdd:PLN02546 389 VTDRINLTPVALMEGGALAKTLFGNEpTKPDYRAVPSAVFSQPPIGQVGLTEeQAIEEYG-DVDV----FTANFRPLKAT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 398 DTG----GFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSE 456
Cdd:PLN02546 464 LSGlpdrVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-456 |
1.53e-48 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 175.19 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklaLGGTCLNVGCIPSKALldsswkFHEAQDGFAIHGINHAGV 84
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDY-------LGGTCVNVGCVPKKIM------FNAASIHDILENSRHYGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 85 ----TMDVPAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVTK-------PDGSV-------------- 139
Cdd:PTZ00058 116 dtqfSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeADESDddevtivsagvsql 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 140 ---EIIEAENVILAPGSRPIdIPPAPVDQNVIvDSTGALEFQSvPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTF 216
Cdd:PTZ00058 196 ddgQVIEGKNILIAVGNKPI-FPDVKGKEFTI-SSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 217 LMAADTAVSKEALKTLTKQGLDIKLGA---RVTGSKVNGDEVVVnytdANGEQNITFDKLIVAVGRRPVTTDLlaaDCGV 293
Cdd:PTZ00058 273 LRKFDETIINELENDMKKNNINIITHAnveEIEKVKEKNLTIYL----SDGRKYEHFDYVIYCVGRSPNTEDL---NLKA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 294 TLD--ERGFVHVDDHCATTVPGVYAIGDVV--------RGMMLAHKASEE--------------------------GIMV 337
Cdd:PTZ00058 346 LNIktPKGYIKVDDNQRTSVKHIYAVGDCCmvkknqeiEDLNLLKLYNEEpylkkkentsgesyynvqltpvainaGRLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 338 VERIKGHKAQM-NYDLIPSVIYTHPEIAWVGKTE-QALKAEGVEvNVGTFP------FAASGRAMAANDTGGFVKVIADA 409
Cdd:PTZ00058 426 ADRLFGPFSRTtNYKLIPSVIFSHPPIGTIGLSEqEAIDIYGKE-NVKIYEsrftnlFFSVYDMDPAQKEKTYLKLVCVG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 495293109 410 KTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTLSE 456
Cdd:PTZ00058 505 KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
353-461 |
3.67e-48 |
|
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: 161.18 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 353 IPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPFAASGRAMAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGA 432
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 495293109 433 IGMEFGTSAEDLGMMVFSHPTLSEALHEA 461
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-457 |
2.94e-44 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 162.30 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIE--KYTDKEGKLALGGTCLNVGCIPSK-----ALLDSSWKFHEAQDGFAIH 77
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTQGTKWGLGGTCVNVGCVPKKlmhyaANIGSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 78 GINHAGvtmdvpAMVGRKANIVKGLTSGVATLFKANGVTSIQGHGKLLAGKKVEVtKPDGSVEIIEAENVILAPGSRPiD 157
Cdd:PTZ00052 86 SSFNWG------KLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSY-GDNSQEETITAKYILIATGGRP-S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 158 IP-PAPVDQNVIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVleALDTF-LMAADTAVSKEALKTLTKQ 235
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--AVRSIpLRGFDRQCSEKVVEYMKEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 236 GLDIKLGA-RVTGSKVNgDEVVVNYTDANGEQnitFDKLIVAVGRRPVTTDLLAADCGVTLDERGFVHVDDHCaTTVPGV 314
Cdd:PTZ00052 236 GTLFLEGVvPINIEKMD-DKIKVLFSDGTTEL---FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 315 YAIGDVVRGM-MLAHKASEEGIMVVERI-KGHKAQMNYDLIPSVIYTHPEIAWVGKTEQALKAEGVEVNVGTFPF----- 387
Cdd:PTZ00052 311 FAVGDVVEGRpELTPVAIKAGILLARRLfKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQefntl 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 388 --AASGR---AMAANDTGGFVK--------VIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTL 454
Cdd:PTZ00052 391 eiAAVHRekhERARKDEYDFDVssnclaklVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTD 470
|
...
gi 495293109 455 SEA 457
Cdd:PTZ00052 471 AEV 473
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
115-346 |
4.87e-30 |
|
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: 119.15 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 115 VTSIQghgklLAGKKVEVTkpDGsvEIIEAENVILAPGSRPIdIPPAP------VDQNVIVDSTGAL-----EFQsvPKR 183
Cdd:COG0446 59 VTAID-----PEAKTVTLR--DG--ETLSYDKLVLATGARPR-PPPIPgldlpgVFTLRTLDDADALrealkEFK--GKR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 184 LGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGARVTgsKVNGDE-VVVNYTDa 262
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVV--AIDGDDkVAVTLTD- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 263 nGEQnITFDKLIVAVGRRPVTTdlLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDVVR----------GMMLAHKASE 332
Cdd:COG0446 204 -GEE-IPADLVVVAPGVRPNTE--LAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktvYIPLASAANK 279
|
250
....*....|....
gi 495293109 333 EGIMVVERIKGHKA 346
Cdd:COG0446 280 QGRVAAENILGGPA 293
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
107-322 |
1.90e-26 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 110.62 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 107 ATLFKANGVTsiqghgkLLAGKKVE--------VTKPDGsvEIIEAENVILAPGSRPIdIPPAPVD--QNVIV-----DS 171
Cdd:COG1251 63 ADFYEENGID-------LRLGTRVTaidraartVTLADG--ETLPYDKLVLATGSRPR-VPPIPGAdlPGVFTlrtldDA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 172 TGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFL-MAADTAVSKEALKTLTKQGLDIKLGARVTGskV 250
Cdd:COG1251 133 DALRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTE--I 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495293109 251 NGDEVVVNYTDANGEQnITFDKLIVAVGRRPVTTdlLAADCGVTLDeRGfVHVDDHCATTVPGVYAIGDVVR 322
Cdd:COG1251 211 EGDDRVTGVRLADGEE-LPADLVVVAIGVRPNTE--LARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAE 277
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-338 |
2.19e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 105.59 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKytdkegkLALGGTCLNVGCI---PSkalldsswkFHEAQDGFAI--HGI 79
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-------GEPGGQLATTKEIenyPG---------FPEGISGPELaeRLR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 80 NHAgvtmdvpamvgRKANIVkgltsgvatlFKANGVTSIQghgklLAGKKVEVTKPDGsvEIIEAENVILAPGS--RPID 157
Cdd:COG0492 65 EQA-----------ERFGAE----------ILLEEVTSVD-----KDDGPFRVTTDDG--TEYEAKAVIIATGAgpRKLG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 158 IP--PAPVDQNVivdSTGA----LEFQSvpKRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFlMAADtaVSKEALKT 231
Cdd:COG0492 117 LPgeEEFEGRGV---SYCAtcdgFFFRG--KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDEL-RASK--ILVERLRA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 232 LTKqgLDIKLGARVTgsKVNGDE----VVVNYTDANGEQNITFDKLIVAVGRRPVTTdlLAADCGVTLDERGFVHVDDHC 307
Cdd:COG0492 189 NPK--IEVLWNTEVT--EIEGDGrvegVTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGYIVVDEDM 262
|
330 340 350
....*....|....*....|....*....|..
gi 495293109 308 ATTVPGVYAIGDVVRG-MMLAHKASEEGIMVV 338
Cdd:COG0492 263 ETSVPGVFAAGDVRDYkYRQAATAAGEGAIAA 294
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
183-261 |
8.84e-18 |
|
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: 77.63 E-value: 8.84e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495293109 183 RLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGARVTGSKVNGDEVVVNYTD 261
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
148-327 |
1.46e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.03 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 148 ILAPGSRPIdIPPAPVDQnVIVDSTGALEFQSV------PKRLGVIGAGVIGLELGSVWSRLGAQVTVLEaLDTFLMAAD 221
Cdd:PRK04965 104 VLATGASAF-VPPIPGRE-LMLTLNSQQEYRAAetqlrdAQRVLVVGGGLIGTELAMDLCRAGKAVTLVD-NAASLLASL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 222 TA--VSKEALKTLTKQGLDIKLGARVTGSKVNGDEVVVnyTDANGEQnITFDKLIVAVGRRPVTTdlLAADCGVTLdERG 299
Cdd:PRK04965 181 MPpeVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRA--TLDSGRS-IEVDAVIAAAGLRPNTA--LARRAGLAV-NRG 254
|
170 180 190
....*....|....*....|....*....|
gi 495293109 300 FVhVDDHCATTVPGVYAIGDV--VRGMMLA 327
Cdd:PRK04965 255 IV-VDSYLQTSAPDIYALGDCaeINGQVLP 283
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
181-321 |
3.10e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 74.01 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 181 PKRLGVIGAGVIGLEL-GSVWSRLG------------AQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGARVTg 247
Cdd:COG1252 149 LLTIVVVGGGPTGVELaGELAELLRkllrypgidpdkVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVT- 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495293109 248 sKVNGDEVVVnytdANGEQnITFDKLIVAVGRRPVTtdlLAADCGVTLDERGFVHVDDHC-ATTVPGVYAIGDVV 321
Cdd:COG1252 228 -EVDADGVTL----EDGEE-IPADTVIWAAGVKAPP---LLADLGLPTDRRGRVLVDPTLqVPGHPNVFAIGDCA 293
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
182-321 |
1.39e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 69.43 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 182 KRLGVIGAGVIGLE-LGSVWSRlGAQVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGARVtgSKVNGDEVvvNYT 260
Cdd:PRK13512 149 DKALVVGAGYISLEvLENLYER-GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEI--DAINGNEV--TFK 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495293109 261 DANGEqniTFDKLIVAVGRRPVTTDLlaADCGVTLDERGFVHVDDHCATTVPGVYAIGDVV 321
Cdd:PRK13512 224 SGKVE---HYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDII 279
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
182-451 |
4.70e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 67.76 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 182 KRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFLMAA-DTAVSKEALKTLTKQGLDIKLGARVTgSKVNGDEVVVNYT 260
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVK-SLIGEDKVEGVVT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 261 DANgeqNITFDKLIVAVGRRPVTTdlLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD--VVRGMM--------LAHKA 330
Cdd:PRK09564 229 DKG---EYEADVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcaTIYNIVsnknvyvpLATTA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 331 SEEGIMVVERIKGHKAQMNYDLIPSVIYTHP-EIAWVGKTEQALKAEGVEVNVGTFpfaaSGRAMAANDTGG---FVKVI 406
Cdd:PRK09564 304 NKLGRMVGENLAGRHVSFKGTLGSACIKVLDlEAARTGLTEEEAKKLGIDYKTVFI----KDKNHTNYYPGQedlYVKLI 379
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495293109 407 ADAKTDRVLGVHVIGPSAAEL-VQQGAIGMEFGTSAEDLGMMVFSH 451
Cdd:PRK09564 380 YEADTKVILGGQIIGKKGAVLrIDALAVAIYAKLTTQELGMMDFCY 425
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
182-320 |
4.97e-12 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 67.26 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 182 KRLGVIGAGVIGLELGSVWSRLGAQVTVLEALDTFL-MAADTAVSKEALKTLTKQGLDIKLGARVTgSKVNGDEVVVnyT 260
Cdd:PRK09754 145 RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIE-HVVDGEKVEL--T 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 261 DANGEQNITfDKLIVAVGRRpvTTDLLAADCGvtLDERGFVHVDDHCATTVPGVYAIGDV 320
Cdd:PRK09754 222 LQSGETLQA-DVVIYGIGIS--ANDQLAREAN--LDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
145-320 |
1.17e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 64.08 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 145 ENVILAPGSRPIdIPPAP-VDQNVI-----VDSTGALEFQSVP-KRLGVIGAGVIGLELGSVWSRLGAQVTVLEaLDTFL 217
Cdd:TIGR02374 98 DKLILATGSYPF-ILPIPgADKKGVyvfrtIEDLDAIMAMAQRfKKAAVIGGGLLGLEAAVGLQNLGMDVSVIH-HAPGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 218 MAA--DTAVSKEALKTLTKQGLDIKLGARVTgsKVNGDEVVVNYTDANGEQnITFDKLIVAVGRRPVTTdlLAADCGVTL 295
Cdd:TIGR02374 176 MAKqlDQTAGRLLQRELEQKGLTFLLEKDTV--EIVGATKADRIRFKDGSS-LEADLIVMAAGIRPNDE--LAVSAGIKV 250
|
170 180
....*....|....*....|....*
gi 495293109 296 DeRGFVhVDDHCATTVPGVYAIGDV 320
Cdd:TIGR02374 251 N-RGII-VNDSMQTSDPDIYAVGEC 273
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
129-318 |
1.31e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 62.24 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 129 KVE-VTKPDG------SVEIIEAENVILAPG--SRP--IDIPPAPV------------DQNVIVdstgalefqsvpkrlg 185
Cdd:pfam13738 97 EVTsVKKEDDgfvvttSKGTYQARYVIIATGefDFPnkLGVPELPKhysyvkdfhpyaGQKVVV---------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 186 vIGA---GV-IGLELgsvwSRLGAQVTVLEAlDTFLMAADTAVS-------KEALKTLTKQG-LDIKLGARVTGSKVNGD 253
Cdd:pfam13738 161 -IGGynsAVdAALEL----VRKGARVTVLYR-GSEWEDRDSDPSyslspdtLNRLEELVKNGkIKAHFNAEVKEITEVDV 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495293109 254 EVVVNYtdANGEQNITFDKLIVAVGRRPvTTDLLAAdCGVTLDERGFVHVDDH-CATTVPGVYAIG 318
Cdd:pfam13738 235 SYKVHT--EDGRKVTSNDDPILATGYHP-DLSFLKK-GLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
5-320 |
4.70e-09 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 58.63 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACI-EKYtdkegklalGGTCLnvgcipskalldsswkfheaqDGFAIHgiNHAG 83
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaERF---------GGQVL---------------------DTMGIE--NFIS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 84 VtmdvPAMVGRKanivkgLTSGVATLFKANGVTSIQGHgkllagKKVEVTKPDGSVEI-------IEAENVILAPGS--R 154
Cdd:PRK15317 260 V----PETEGPK------LAAALEEHVKEYDVDIMNLQ------RASKLEPAAGLIEVelangavLKAKTVILATGArwR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 155 PIDIPpapvdqnvivdstGALEFQS-----VP---------KRLGVIGAGVIGLEL-----GSVwsrlgAQVTVLEALDT 215
Cdd:PRK15317 324 NMNVP-------------GEDEYRNkgvayCPhcdgplfkgKRVAVIGGGNSGVEAaidlaGIV-----KHVTVLEFAPE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 216 flMAADtAVSKEALKTLTKqgLDIKLGARVT-----GSKVNGdevvVNYTD-ANGE-QNITFDKLIVAVGRRPvTTDLLA 288
Cdd:PRK15317 386 --LKAD-QVLQDKLRSLPN--VTIITNAQTTevtgdGDKVTG----LTYKDrTTGEeHHLELEGVFVQIGLVP-NTEWLK 455
|
330 340 350
....*....|....*....|....*....|..
gi 495293109 289 ADcgVTLDERGFVHVDDHCATTVPGVYAIGDV 320
Cdd:PRK15317 456 GT--VELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
182-319 |
8.04e-09 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 58.21 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 182 KRLGVIGAGVIGLELGSVWSRLGAQVTVLEaLDTFLMAadtavskEALKTLTKQGLDIK---LGARVTGSKvNGDEVVVN 258
Cdd:PRK14989 146 KRGAVVGGGLLGLEAAGALKNLGVETHVIE-FAPMLMA-------EQLDQMGGEQLRRKiesMGVRVHTSK-NTLEIVQE 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495293109 259 YTDANGEQN------ITFDKLIVAVGRRPvtTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGD 319
Cdd:PRK14989 217 GVEARKTMRfadgseLEVDFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
244-323 |
1.58e-08 |
|
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: 56.68 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 244 RVTGSKVngDEVVVNYTDANG----------EQNITFDKLIVAVGRRPVTtDLLAADCGVTLDERGFVHVD-DHCATTVP 312
Cdd:COG0493 326 RVTGLEC--VRMELGEPDESGrrrpvpiegsEFTLPADLVILAIGQTPDP-SGLEEELGLELDKRGTIVVDeETYQTSLP 402
|
90
....*....|.
gi 495293109 313 GVYAIGDVVRG 323
Cdd:COG0493 403 GVFAGGDAVRG 413
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-153 |
3.95e-08 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 55.25 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTDkegklalggTCLNVGCIPSKALLDSSWKFHE--AQDGFAIHGINHAG 83
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTD---------TIAELSCNPSIGGIAKGHLVREidALGGLMGKAADKTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 84 VTMDV------PAMVGRKANIVKGLTSGVAT--LFKANGVTSIQGHGKLL---AGKKVEVTKPDGsvEIIEAENVILAPG 152
Cdd:pfam01134 72 IQFRMlntskgPAVRALRAQVDRDLYSKEMTetLENHPNLTLIQGEVTDLipeNGKVKGVVTEDG--EEYKAKAVVLATG 149
|
.
gi 495293109 153 S 153
Cdd:pfam01134 150 T 150
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
206-319 |
8.54e-07 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 51.31 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 206 QVTVLEALDTFLMAADTAVSKEALKTLTKQGLDIKLGARVTGskVNGDEVVVNytdaNGEQNITfdKLIV---AVGRRPV 282
Cdd:PTZ00318 212 KVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKE--VLDKEVVLK----DGEVIPT--GLVVwstGVGPGPL 283
|
90 100 110
....*....|....*....|....*....|....*...
gi 495293109 283 TTDLlaadcGVTLDERGFVHVDDHC-ATTVPGVYAIGD 319
Cdd:PTZ00318 284 TKQL-----KVDKTSRGRISVDDHLrVKPIPNVFALGD 316
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
4-35 |
1.10e-06 |
|
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: 50.99 E-value: 1.10e-06
10 20 30
....*....|....*....|....*....|..
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEK 34
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
244-323 |
1.87e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 50.16 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 244 RVTGSKV------NGDEVVVnytdANGEQNITFDKLIVAVGRRPVTTDLLAaDCGVTLDERGFVHVDDHC-ATTVPGVYA 316
Cdd:PRK12810 361 KVTGVKVvrtelgEGDFEPV----EGSEFVLPADLVLLAMGFTGPEAGLLA-QFGVELDERGRVAAPDNAyQTSNPKVFA 435
|
....*..
gi 495293109 317 IGDVVRG 323
Cdd:PRK12810 436 AGDMRRG 442
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-48 |
2.86e-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: 49.53 E-value: 2.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTdkegklALGGT 48
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRG------FLGGM 37
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-35 |
1.07e-05 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 47.72 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PRK07843 4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEK 38
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-35 |
1.26e-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: 47.28 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEK 30
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-62 |
3.09e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.03 E-value: 3.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKyTDKEGK---LALGGTClNV--GCIPSKALLD 62
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEK-GKKLGRkilISGGGRC-NVtnLSEEPDNFLS 61
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
271-323 |
6.67e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.17 E-value: 6.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 495293109 271 DKLIVAVGRRPVTTDLLAADcGVTLDERGFVHVDD-HCATTVPGVYAIGDVVRG 323
Cdd:PRK11749 377 DLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDeTGRTSLPGVFAGGDIVTG 429
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
182-334 |
7.25e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 45.49 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 182 KRLGVIGAGVIGLELGSVWSRLGA-QVTVLEALDTFLMAADTAVSKEALKtltkQGLDIK-LGARVTGSKVNGDEVVV-- 257
Cdd:PRK12814 324 KKVVVIGGGNTAIDAARTALRLGAeSVTILYRRTREEMPANRAEIEEALA----EGVSLReLAAPVSIERSEGGLELTai 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 258 ----NYTDANG----------EQNITFDKLIVAVGRRpVTTDLLAADcGVTLDERGFVHVDDH-CATTVPGVYAIGDVVR 322
Cdd:PRK12814 400 kmqqGEPDESGrrrpvpvegsEFTLQADTVISAIGQQ-VDPPIAEAA-GIGTSRNGTVKVDPEtLQTSVAGVFAGGDCVT 477
|
170
....*....|..
gi 495293109 323 GMMLAHKASEEG 334
Cdd:PRK12814 478 GADIAINAVEQG 489
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
268-341 |
7.45e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 44.98 E-value: 7.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495293109 268 ITFDKLIVAVGRRPvTTDLLAADCGVTLDERGFVHVDDHCATTVPGVYAIGDVVRGMMLAHKASEEGIMVVERI 341
Cdd:PRK12770 273 LEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSI 345
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-31 |
8.18e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 44.79 E-value: 8.18e-05
10 20
....*....|....*....|....*...
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTA 31
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVA 29
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
3-35 |
1.08e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.46 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|...
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEK 34
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-48 |
1.74e-04 |
|
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: 43.70 E-value: 1.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTDkegklaLGGT 48
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADD------VGGT 44
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
3-35 |
4.04e-04 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 42.72 E-value: 4.04e-04
10 20 30
....*....|....*....|....*....|...
gi 495293109 3 QKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PRK07803 7 HSYDVVVIGAGGAGLRAAIEARERGLRVAVVCK 39
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
4-52 |
4.89e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.53 E-value: 4.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKytdKEGKLALGGTCLNV 52
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAK---GQGALHFSSGSIDL 47
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
270-335 |
6.38e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 41.93 E-value: 6.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495293109 270 FDKLIVAVGRRPVTTdLLAADCGVTLDERGFVHVD-DHCATTVPGVYAIGDVVRG------MMLAHKASEEGI 335
Cdd:PRK12831 385 VDTVIMSLGTSPNPL-ISSTTKGLKINKRGCIVADeETGLTSKEGVFAGGDAVTGaatvilAMGAGKKAAKAI 456
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-33 |
1.23e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 41.04 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|...
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACI 33
Cdd:PRK07494 4 EKEHTDIAVIGGGPAGLAAAIALARAGASVALV 36
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
263-323 |
1.46e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 41.27 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495293109 263 NGEQNITFDKLIVAVGRRPvtTDLLAADC-GVTLDERGFVHVDDHCATTVPGVYAIGDVVRG 323
Cdd:PRK12778 668 GSTFTVDVDLVIVSVGVSP--NPLVPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
5-35 |
1.90e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.88 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|.
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVER 47
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
7-323 |
2.32e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 40.52 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 7 VVVIGAGPGGYVAAIKAAQLGLStacIEKYtdkEGKLALGGTcLNVGcIPSKALLDsswkfhEAQDGfAIHGINHAGVTM 86
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGYE---VTVY---ESLSKPGGV-MRYG-IPSYRLPD------EALDK-DIAFIEALGVKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 87 DVPAMVGRKANIVKgLTSGVATLFKANGVTsiqghgkllAGKKvevTKPDGSveiiEAENVILApgsrpidippAPVDQN 166
Cdd:PRK13984 351 HLNTRVGKDIPLEE-LREKHDAVFLSTGFT---------LGRS---TRIPGT----DHPDVIQA----------LPLLRE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 167 VIVDSTGALEFQSVPKRLGVIGAGVIGLELGSVWSRLGAQ------VTVLEALDTFL-MAADTAVSKEALKtltkQGLDI 239
Cdd:PRK13984 404 IRDYLRGEGPKPKIPRSLVVIGGGNVAMDIARSMARLQKMeygevnVKVTSLERTFEeMPADMEEIEEGLE----EGVVI 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495293109 240 KLGARVTGSKVNGDEV-------VVNYTDANGEQNITFDK----------LIVAVGRRPvTTDLLAADCGVTLD-ERGFV 301
Cdd:PRK13984 480 YPGWGPMEVVIENDKVkgvkfkkCVEVFDEEGRFNPKFDEsdqiiveadmVVEAIGQAP-DYSYLPEELKSKLEfVRGRI 558
|
330 340
....*....|....*....|..
gi 495293109 302 HVDDHCATTVPGVYAIGDVVRG 323
Cdd:PRK13984 559 LTNEYGQTSIPWLFAGGDIVHG 580
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-35 |
2.35e-03 |
|
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: 39.99 E-value: 2.35e-03
10 20 30
....*....|....*....|....*....|.
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
4-35 |
2.69e-03 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 40.11 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|..
gi 495293109 4 KFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PTZ00139 29 TYDAVVVGAGGAGLRAALGLVELGYKTACISK 60
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-47 |
2.73e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 40.17 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTDKEGKLALGG 47
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSG 54
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
6-59 |
3.24e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 40.22 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEK-YTDKEGKLALGGTCLNVGCIPSKA 59
Cdd:PRK13800 15 DVLVIGGGTAGTMAALTAAEHGANVLLLEKaHVRHSGALAMGMDGVNNAVIPGKA 69
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
1-35 |
4.08e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 39.81 E-value: 4.08e-03
10 20 30
....*....|....*....|....*....|....*
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PRK12839 5 MTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEK 39
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
5-47 |
4.22e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 39.74 E-value: 4.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTDKEGKLALGG 47
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSG 49
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
6-48 |
5.57e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 39.29 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 495293109 6 DVVVIGAGPGGYVAAIKAAQLGLSTACIEKytdkegKLALGGT 48
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEK------EPVFGGT 47
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
2-38 |
6.06e-03 |
|
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: 38.77 E-value: 6.06e-03
10 20 30
....*....|....*....|....*....|....*..
gi 495293109 2 SQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEKYTD 38
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPP 37
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
1-35 |
7.72e-03 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 38.66 E-value: 7.72e-03
10 20 30
....*....|....*....|....*....|....*
gi 495293109 1 MSQKFDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PRK06481 58 LKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEK 92
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
5-35 |
8.60e-03 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 38.68 E-value: 8.60e-03
10 20 30
....*....|....*....|....*....|.
gi 495293109 5 FDVVVIGAGPGGYVAAIKAAQLGLSTACIEK 35
Cdd:PLN00128 51 YDAVVVGAGGAGLRAAIGLSEHGFNTACITK 81
|
|
| |
