|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
103-553 |
0e+00 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 616.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 103 LHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQnehHMKSFGLQVSAAGYDRQGVADHANNLATKIRNN 182
Cdd:PRK06416 21 IRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEAR---HSEDFGIKAENVGIDFKKVQEWKNGVVNRLTGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 183 LTNSMKAIGVDILTGFGSVLGPQKVKYGKDN---IITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAI 259
Cdd:PRK06416 98 VEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDgeqTYTAKNIILATGSRPRELPGIEIDGRVIWTSDEALNLDEVPKSLVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 260 VGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGkpvlIELIDAK 339
Cdd:PRK06416 178 IGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKK-RGIKIKTGAKAKKVEQTDDG----VTVTLED 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 340 TKEPKdTLEVDAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGI 419
Cdd:PRK06416 253 GGKEE-TLEADYVLVAVGRRPNTENLGLEELGVKTDRGFIEVDEQLR------TNVPNIYAIGDIVGGPMLAHKASAEGI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 420 SVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEkgekEGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDN 499
Cdd:PRK06416 326 IAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKE----EGFDVKVVKFPFAGNGKALALGETDGFVKLIFDKKD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145332599 500 GEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAA 553
Cdd:PRK06416 402 GEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAA 455
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
105-553 |
4.19e-167 |
|
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: 484.59 E-value: 4.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELqneHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLT 184
Cdd:COG1249 22 AAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEA---RHAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 185 NSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGY 264
Cdd:COG1249 99 ELLKKNGVDVIRGRARFVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEELPKSLVVIGGGY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 265 IGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITpaRDGKPVLIELIDAKTKEpk 344
Cdd:COG1249 179 IGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEK-EGIDILTGAKVTSVE--KTGDGVTVTLEDGGGEE-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 345 dTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGISVVE 423
Cdd:COG1249 254 -AVEADKVLVATGRRPNTDGLGLEAAGVeLDERGGIKVDEYLR------TSVPGIYAIGDVTGGPQLAHVASAEGRVAAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 424 QVSGRD-HVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEkegfKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEI 502
Cdd:COG1249 327 NILGKKpRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGI----DVKVGKFPFAANGRALALGETEGFVKLIADAETGRI 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 145332599 503 LGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAA 553
Cdd:COG1249 403 LGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-558 |
5.13e-147 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 440.50 E-value: 5.13e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 3 SAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNR-----IQFLSRKSFQVSASASSNG 77
Cdd:PTZ00153 30 GHQLHALHEKGFPVPLGKSTSSTFIRCNFVPSPANPISLGASKQESPGILTPMPSSarlssPQPRSEKSLRANGFATSQS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 78 NGapPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGD--VVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFG 155
Cdd:PTZ00153 110 MN--FSDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDddSIGGTCVNVGCIPSKALLYATGKYRELKNLAKLYTYG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 156 LQVSAAGY------------------DRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGpQKVKYGKDNIITA 217
Cdd:PTZ00153 188 IYTNAFKNgkndpvernqlvadtvqiDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIY-ERGHIVDKNTIKS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 218 ---------KDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQ 288
Cdd:PTZ00153 267 eksgkefkvKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 289 LMPGFDPEISKLAQRVLINPRKIDYHTGVFASKITPARDGKPVLIELIDAKTKEPKDT---------LEVDAALIATGRA 359
Cdd:PTZ00153 347 LLPLLDADVAKYFERVFLKSKPVRVHLNTLIEYVRAGKGNQPVIIGHSERQTGESDGPkknmndikeTYVDSCLVATGRK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 360 PFTNGLGLENVNVVTQRGFIPVDERMRVIDGKGTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRD------HVLN 433
Cdd:PTZ00153 427 PNTNNLGLDKLKIQMKRGFVSVDEHLRVLREDQEVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGkenvniNVEN 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 434 HLS-------IPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSVvkTSFKANTKALAENE-------------------- 486
Cdd:PTZ00153 507 WASkpiiyknIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEI--SFYKANSKVLCENNisfpnnsknnsynkgkyntv 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145332599 487 --GEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKA-AKVESH 558
Cdd:PTZ00153 585 dnTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAiAGVRTH 659
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
109-553 |
3.08e-136 |
|
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: 405.87 E-value: 3.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 109 GLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQnehHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMK 188
Cdd:TIGR01350 24 GLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIK---HAKDLGIEVENVSVDWEKMQKRKNKVVKKLVGGVSGLLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 189 AIGVDILTGFGSVLGPQKVKYGKDN---IITAKDIIIATGSVPFVPKG-IEVDGKTVITSDHALKLESVPEWIAIVGSGY 264
Cdd:TIGR01350 101 KNKVTVIKGEAKFLDPGTVSVTGENgeeTLEAKNIIIATGSRPRSLPGpFDFDGKVVITSTGALNLEEVPESLVIIGGGV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 265 IGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKPVLIElidaktKEPK 344
Cdd:TIGR01350 181 IGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKK-KGVKILTNTKVTAVEKNDDQVTYENK------GGET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 345 DTLEVDAALIATGRAPFTNGLGLENVNVV-TQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGISVVE 423
Cdd:TIGR01350 254 ETLTGEKVLVAVGRKPNTEGLGLEKLGVElDERGRIVVDEYMR------TNVPGIYAIGDVIGGPMLAHVASHEGIVAAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 424 QVSGRDHV-LNHLSIPAACFTHPEISMVGLTEPQAKEKgekeGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEI 502
Cdd:TIGR01350 328 NIAGKEPAhIDYDAVPSVIYTDPEVASVGLTEEQAKEA----GYDVKIGKFPFAANGKALALGETDGFVKIIADKKTGEI 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 145332599 503 LGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAA 553
Cdd:TIGR01350 404 LGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAA 454
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
105-553 |
6.33e-127 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 381.83 E-value: 6.33e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQnehHMKSFGLQVSAAGYDRQGVADHANnlatKIRNNLT 184
Cdd:PRK06292 22 AAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAK---HAEEFGIHADGPKIDFKKVMARVR----RERDRFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 185 NSM-----KAIGVDILTGFGSVLGPQKVKYGkDNIITAKDIIIATGS-VPFVPKGIEVDGKTVITSDHALKLESVPEWIA 258
Cdd:PRK06292 95 GGVvegleKKPKIDKIKGTARFVDPNTVEVN-GERIEAKNIVIATGSrVPPIPGVWLILGDRLLTSDDAFELDKLPKSLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 259 IVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLinPRKIDYHTGVFASKITPARDGKPVLIELiDA 338
Cdd:PRK06292 174 VIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKIL--SKEFKIKLGAKVTSVEKSGDEKVEELEK-GG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 339 KTKepkdTLEVDAALIATGRAPFTNGLGLENVNVVT-QRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQ 417
Cdd:PRK06292 251 KTE----TIEADYVLVATGRRPNTDGLGLENTGIELdERGRPVVDEHTQ------TSVPGIYAAGDVNGKPPLLHEAADE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 418 GISVVEQVSG--RDHVlNHLSIPAACFTHPEISMVGLTEPQAKEkgekEGFKVSVVKTSFKANTKALAENEGEGIAKMIY 495
Cdd:PRK06292 321 GRIAAENAAGdvAGGV-RYHPIPSVVFTDPQIASVGLTEEELKA----AGIDYVVGEVPFEAQGRARVMGKNDGFVKVYA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 145332599 496 RPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAA 553
Cdd:PRK06292 396 DKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDL 453
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
105-548 |
2.04e-113 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 347.68 E-value: 2.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIE-------GDVVGGTCVNRGCVPSKALLAVSGRMRELQneHHMKSFGLQVSAAGYDRQGVADHANNLAT 177
Cdd:PRK06327 23 AAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAG--HHFADHGIHVDGVKIDVAKMIARKDKVVK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 178 KIRNNLTNSMKAIGVDILTGFGSVLGPQ------KVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLE 251
Cdd:PRK06327 101 KMTGGIEGLFKKNKITVLKGRGSFVGKTdagyeiKVTGEDETVITAKHVIIATGSEPRHLPGVPFDNKIILDNTGALNFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 252 SVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGkpV 331
Cdd:PRK06327 181 EVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTK-QGLDIHLGVKIGEIKTGGKG--V 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 332 LIELIDAKTKEpkDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLML 410
Cdd:PRK06327 258 SVAYTDADGEA--QTLEVDKLIVSIGRVPNTDGLGLEAVGLkLDERGFIPVDDHCR------TNVPNVYAIGDVVRGPML 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 411 AHAASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEkgekEGFKVSVVKTSFKANTKALAENEGEGI 490
Cdd:PRK06327 330 AHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVEYKAGKFPFMANGRALAMGEPDGF 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 145332599 491 AKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDE 548
Cdd:PRK06327 406 VKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHE 463
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
105-546 |
8.02e-87 |
|
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: 278.15 E-value: 8.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLavsgrmRELQNEHHMK--SFGLQVSAAGYDRQGVADHANNLATKIRNN 182
Cdd:TIGR02053 19 AAELGASVAMVERGPLGGTCVNVGCVPSKMLL------RAAEVAHYARkpPFGGLAATVAVDFGELLEGKREVVEELRHE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 183 -LTNSMKAIGVDILTGFGSVLGPQKVKYGKDN-IITAKDIIIATGSVPFVPkgiEVDG-KTV--ITSDHALKLESVPEWI 257
Cdd:TIGR02053 93 kYEDVLSSYGVDYLRGRARFKDPKTVKVDLGReVRGAKRFLIATGARPAIP---PIPGlKEAgyLTSEEALALDRIPESL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 258 AIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITpaRDGKPVLIELid 337
Cdd:TIGR02053 170 AVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAE-EGIEVVTSAQVKAVS--VRGGGKIITV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 338 aKTKEPKDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASA 416
Cdd:TIGR02053 245 -EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVkLDERGGILVDETLR------TSNPGIYAAGDVTGGLQLEYVAAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 417 QG-ISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGekEGFKVSVVKTSfkANTKALAENEGEGIAKMIY 495
Cdd:TIGR02053 318 EGvVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAG--IECDCRTLPLT--NVPRARINRDTRGFIKLVA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 145332599 496 RPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVL 546
Cdd:TIGR02053 394 EPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
105-552 |
8.50e-87 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 278.24 E-value: 8.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSgrmRELQNEHHMKSFGLQVSAA-GYDRQGVADHANNLATKIRNNL 183
Cdd:PRK06370 24 AAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASA---RAAHLARRAAEYGVSVGGPvSVDFKAVMARKRRIRARSRHGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 184 TNSMKAI-GVDILTGFGSVLGPQKVKYGkDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGS 262
Cdd:PRK06370 101 EQWLRGLeGVDVFRGHARFESPNTVRVG-GETLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDELPEHLVIIGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 263 GYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRkIDYHTGVFASKITPARDGKPVLIELIDAktke 342
Cdd:PRK06370 180 GYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREG-IDVRLNAECIRVERDGDGIAVGLDCNGG---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 343 pKDTLEVDAALIATGRAPFTNGLGLENVNVVT-QRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGISV 421
Cdd:PRK06370 255 -APEITGSHILVAVGRVPNTDDLGLEAAGVETdARGYIKVDDQLR------TTNPGIYAAGDCNGRGAFTHTAYNDARIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 422 VEQVSGRDHV-LNHLSIPAACFTHPEISMVGLTEPQAKEKGEkegfKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNG 500
Cdd:PRK06370 328 AANLLDGGRRkVSDRIVPYATYTDPPLARVGMTEAEARKSGR----RVLVGTRPMTRVGRAVEKGETQGFMKVVVDADTD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 145332599 501 EILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKA 552
Cdd:PRK06370 404 RILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQA 455
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
105-544 |
8.04e-75 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 246.22 E-value: 8.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSgRMRELQnEHHMKSFGLQVSAAGYD----RQGVADHANNLATKIR 180
Cdd:PRK06116 23 AAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGA-QIAEAF-HDYAPGYGFDVTENKFDwaklIANRDAYIDRLHGSYR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 181 NNLTNSmkaiGVDILTGFGSVLGPQKVKYGkDNIITAKDIIIATGSVPFVP--KGIEVdgktVITSDHALKLESVPEWIA 258
Cdd:PRK06116 101 NGLENN----GVDLIEGFARFVDAHTVEVN-GERYTADHILIATGGRPSIPdiPGAEY----GITSDGFFALEELPKRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 259 IVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKpVLIELIDA 338
Cdd:PRK06116 172 VVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEK-KGIRLHTNAVPKAVEKNADGS-LTLTLEDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 339 KtkepkdTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQ 417
Cdd:PRK06116 250 E------TLTVDCLIWAIGREPNTDGLGLENAGVkLNEKGYIIVDEYQN------TNVPGIYAVGDVTGRVELTPVAIAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 418 GISVVEQVSG--RDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEgfKVSVVKTSFKANTKALAENEGEGIAKMIY 495
Cdd:PRK06116 318 GRRLSERLFNnkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGED--NVKVYRSSFTPMYTALTGHRQPCLMKLVV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 145332599 496 RPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSE 544
Cdd:PRK06116 396 VGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAE 444
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
105-517 |
3.25e-64 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 218.49 E-value: 3.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIE-GDVVGGTCVNRGCVPSKAL----LAVSG-RMRELQNEHHMKsfgLQVSAAgyDrqgVADHANNLATK 178
Cdd:PRK05249 24 AAKLGKRVAVIErYRNVGGGCTHTGTIPSKALreavLRLIGfNQNPLYSSYRVK---LRITFA--D---LLARADHVINK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 179 IRNNLTNSMKAIGVDILTGFGSVLGPQKVKY----GKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVP 254
Cdd:PRK05249 96 QVEVRRGQYERNRVDLIQGRARFVDPHTVEVecpdGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSILSLDHLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 255 EWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGkpVLIE 334
Cdd:PRK05249 176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRD-SGVTIRHNEEVEKVEGGDDG--VIVH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 335 LIDAKtkepkdTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHA 413
Cdd:PRK05249 253 LKSGK------KIKADCLLYANGRTGNTDGLNLENAGLeADSRGQLKVNENYQ------TAVPHIYAVGDVIGFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 414 ASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEkgekEGFKVSVVKTSFKANTKALAENEGEGIAKM 493
Cdd:PRK05249 321 SMDQGRIAAQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQELTA----AKVPYEVGRARFKELARAQIAGDNVGMLKI 396
|
410 420
....*....|....*....|....
gi 145332599 494 IYRPDNGEILGVHIFGLHAADLIH 517
Cdd:PRK05249 397 LFHRETLEILGVHCFGERATEIIH 420
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
85-546 |
1.28e-60 |
|
glutathione-disulfide reductase, plant; 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 plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 208.51 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 85 FDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEhhmKSFGLQVSAAGYD 164
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDA---AGYGWTVGKARFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 165 ----RQGVADHANNLATKIRNNLTNSmkaiGVDILTGFGSVLGPQKVKYG-KDNIITAKDIIIATGSVPFVPK--GIEVd 237
Cdd:TIGR01424 78 wkklLAAKDQEIARLSGLYRKGLANA----GAELLDGRAELVGPNTVEVLaSGKTYTAEKILIAVGGRPPKPAlpGHEL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 238 gktVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGV 317
Cdd:TIGR01424 153 ---GITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEE-RGIRILPED 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 318 FASKITPARDGKPVLielidakTKEPKDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVP 396
Cdd:TIGR01424 229 SITSISKDDDGRLKA-------TLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVrLNDLGAIAVDEYSR------TSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 397 NLYCIGDANGKLMLAHAASAQGISVVE-QVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEkegfKVSVVKTSF 475
Cdd:TIGR01424 296 SIYAVGDVTDRINLTPVAIHEATCFAEtEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFG----DIEVYRAEF 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145332599 476 KANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVL 546
Cdd:TIGR01424 372 RPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEEL 442
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
12-575 |
2.82e-60 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 210.50 E-value: 2.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 12 TSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIR--SNRIQFLSRKSFQVSASASSNGnGAPPKSFDYDL 89
Cdd:PLN02546 4 TLPSTSKLTSSPSLQTLYRKLPLRLPLPSSSSSSHLPLPKTLTRlsSPRPLSHHHRRRSVSRAAAPNG-AESERHYDFDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 90 IIIGAGVGGHGAALHAVEKGLKTAIIE-------GDV---VGGTCVNRGCVPSKALLAVSGRMRELQNEHhmkSFGLQVS 159
Cdd:PLN02546 83 FTIGAGSGGVRASRFASNFGASAAVCElpfatisSDTlggVGGTCVLRGCVPKKLLVYASKYSHEFEESR---GFGWKYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 160 A-AGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKY-GKdnIITAKDIIIATGSVPFVPK--GIE 235
Cdd:PLN02546 160 TePKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVdGK--LYTARNILIAVGGRPFIPDipGIE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 236 vdgkTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEV-TFIEAlDQLMPGFDPEISK-LAQRVLInpRKIDY 313
Cdd:PLN02546 238 ----HAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVhVFIRQ-KKVLRGFDEEVRDfVAEQMSL--RGIEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 314 HTGVFASKITPARDGkpvlieLIDAKTKepKDTLE-VDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgk 391
Cdd:PLN02546 311 HTEESPQAIIKSADG------SLSLKTN--KGTVEgFSHVMFATGRKPNTKNLGLEEVGVkMDKNGAIEVDEYSR----- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 392 gTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRDHVL-NHLSIPAACFTHPEISMVGLTEPQAKEkgekEGFKVSV 470
Cdd:PLN02546 378 -TSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKpDYRAVPSAVFSQPPIGQVGLTEEQAIE----EYGDVDV 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 471 VKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLdelf 550
Cdd:PLN02546 453 FTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF---- 528
|
570 580
....*....|....*....|....*
gi 145332599 551 kaakveshATTRTGDAKIKLNTNQE 575
Cdd:PLN02546 529 --------VTMRTPTRKIRKDSPSE 545
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
109-545 |
2.95e-60 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 207.50 E-value: 2.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 109 GLKTAIIEGDVVGGTCVNRGCVPSKALLavsgrmrelqnehHMKSFGLQVSAAGydRQGVADHANNLA-TKIRNNL---T 184
Cdd:PRK07846 22 DKRIAIVEKGTFGGTCLNVGCIPTKMFV-------------YAADVARTIREAA--RLGVDAELDGVRwPDIVSRVfgrI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 185 NSMKAIG----------VDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVP 254
Cdd:PRK07846 87 DPIAAGGeeyrgrdtpnIDVYRGHARFIGPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADSGVRYHTSDTIMRLPELP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 255 EWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISK----LAQrvlinpRKIDYHTGvfaSKITPA-RDGK 329
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISErfteLAS------KRWDVRLG---RNVVGVsQDGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 330 PVLIELIDAktkepkDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKL 408
Cdd:PRK07846 238 GVTLRLDDG------STVEADVLLVATGRVPNGDLLDAAAAGVdVDEDGRVVVDEYQR------TSAEGVFALGDVSSPY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 409 MLAHAASAQGiSVVEQVSGRDHVL---NHLSIPAACFTHPEISMVGLTEPQAKEKgekeGFKVSVVKTSFKANTKALAEN 485
Cdd:PRK07846 306 QLKHVANHEA-RVVQHNLLHPDDLiasDHRFVPAAVFTHPQIASVGLTENEARAA----GLDITVKVQNYGDVAYGWAME 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145332599 486 EGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIklavhA------HPTLSEV 545
Cdd:PRK07846 381 DTTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREM-----ArgqywiHPALPEV 441
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
105-546 |
1.28e-59 |
|
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: 205.84 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 105 AVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELqneHHMKSFGLQVSAAG-YDRQGVADHANNLATKIRNNL 183
Cdd:TIGR01421 21 AAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERM---HDAADYGFYQNDENtFNWPELKEKRDAYVDRLNGIY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 184 TNSMKAIGVDILTGFGSVLGPQKVKYGKDNiITAKDIIIATGSVPFVPKGIEvDGKTVITSDHALKLESVPEWIAIVGSG 263
Cdd:TIGR01421 98 QKNLEKNKVDVIFGHARFTKDGTVEVNGRD-YTAPHILIATGGKPSFPENIP-GAELGTDSDGFFALEELPKRVVIVGAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 264 YIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKPVlIELIDAKTkep 343
Cdd:TIGR01421 176 YIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEK-EGINVHKLSKPVKVEKTVEGKLV-IHFEDGKS--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 344 kdTLEVDAALIATGRAPFTNGLGLENVNVVT-QRGFIPVDERmrvidgKGTLVPNLYCIGDANGKLMLAHAASAQGISVV 422
Cdd:TIGR01421 251 --IDDVDELIWAIGRKPNTKGLGLENVGIKLnEKGQIIVDEY------QNTNVPGIYALGDVVGKVELTPVAIAAGRKLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 423 EQVSG--RDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEgfKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNG 500
Cdd:TIGR01421 323 ERLFNgkTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKE--NIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKEE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 145332599 501 EILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVL 546
Cdd:TIGR01421 401 KVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEEL 446
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
103-418 |
3.42e-57 |
|
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: 194.84 E-value: 3.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 103 LHAVEKGLKTAIIEgdvVGGTCVNRGCVPSKALLAVSGRMRELqnehhmksfglqvsaagYDRQGVADHANNLATKIRNN 182
Cdd:pfam07992 17 LTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIA-----------------SLWADLYKRKEEVVKKLNNG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 183 LTNSMKAIGVDILTGFGSVLGPQKVKyGKDNIITAKDIIIATGSVPFVP--KGIE---VDGKTVITSDHALKLESVPEWI 257
Cdd:pfam07992 77 IEVLLGTEVVSIDPGAKKVVLEELVD-GDGETITYDRLVIATGARPRLPpiPGVElnvGFLVRTLDSAEALRLKLLPKRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 258 AIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGkpvlielID 337
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEK-NGVEVRLGTSVKEIIGDGDG-------VE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 338 AKTKEpKDTLEVDAALIATGRAPFTNGL---GLEnvnvVTQRGFIPVDERMRvidgkgTLVPNLYCIGDAN-GKLMLAHA 413
Cdd:pfam07992 228 VILKD-GTEIDADLVVVAIGRRPNTELLeaaGLE----LDERGGIVVDEYLR------TSVPGIYAAGDCRvGGPELAQN 296
|
....*
gi 145332599 414 ASAQG 418
Cdd:pfam07992 297 AVAQG 301
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
109-550 |
1.43e-53 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 189.19 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 109 GLKTAIIEGD--VVGGTCVNRGCVPSKALLavsgrmrelqnehhmksfglqVSAA-GYDRQGVADHANNLATKIRNNLTN 185
Cdd:PRK07251 26 GKKVALVEESkaMYGGTCINIGCIPTKTLL---------------------VAAEkNLSFEQVMATKNTVTSRLRGKNYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 186 SMKAIGVDILTGFGSVLGPQ--KVKYGKDNII-TAKDIIIATGSVPFVPK--GIEvDGKTVITSDHALKLESVPEWIAIV 260
Cdd:PRK07251 85 MLAGSGVDLYDAEAHFVSNKviEVQAGDEKIElTAETIVINTGAVSNVLPipGLA-DSKHVYDSTGIQSLETLPERLGII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 261 GSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLiNPRKIDYHTGVFASKItpARDGKPVLIelidakt 340
Cdd:PRK07251 164 GGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYM-EEDGITFLLNAHTTEV--KNDGDQVLV------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 341 KEPKDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGI 419
Cdd:PRK07251 234 VTEDETYRFDALLYATGRKPNTEPLGLENTDIeLTERGAIKVDDYCQ------TSVPGVFAVGDVNGGPQFTYISLDDFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 420 SVVEQVSGrDHVLNH---LSIPAACFTHPEISMVGLTEPQAKEKgekeGFKVSVVKTSFKANTKALAENEGEGIAKMIYR 496
Cdd:PRK07251 308 IVFGYLTG-DGSYTLedrGNVPTTMFITPPLSQVGLTEKEAKEA----GLPYAVKELLVAAMPRAHVNNDLRGAFKVVVN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145332599 497 PDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELF 550
Cdd:PRK07251 383 TETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLF 436
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
62-544 |
4.11e-52 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 186.95 E-value: 4.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 62 LSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIE-------GDV---VGGTCVNRGCVP 131
Cdd:PLN02507 1 MARKMLIDGEVAKVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisSESiggVGGTCVIRGCVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 132 SKALLAVSGRMRELQNEhhmKSFGLQVSAaGYDRQGVADHANNLATKIRNN------LTNSmkaiGVDILTGFGSVLGPQ 205
Cdd:PLN02507 81 KKILVYGATFGGEFEDA---KNYGWEINE-KVDFNWKKLLQKKTDEILRLNgiykrlLANA----GVKLYEGEGKIVGPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 206 KVKY----GKDNIITAKDIIIATGSVPFVPKgieVDGKTV-ITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEV 280
Cdd:PLN02507 153 EVEVtqldGTKLRYTAKHILIATGSRAQRPN---IPGKELaITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 281 TFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKPVLIelidaktkEPKDTLEVDAALIATGRAP 360
Cdd:PLN02507 230 DLFFRKELPLRGFDDEMRAVVARNLEG-RGINLHPRTNLTQLTKTEGGIKVIT--------DHGEEFVADVVLFATGRAP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 361 FTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGISVVEQV-SGRDHVLNHLSIP 438
Cdd:PLN02507 301 NTKRLNLEAVGVeLDKAGAVKVDEYSR------TNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVfGGQPTKPDYENVA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 439 AACFTHPEISMVGLTEPQAKEKGEKEgfkVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHE 518
Cdd:PLN02507 375 CAVFCIPPLSVVGLSEEEAVEQAKGD---ILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQG 451
|
490 500
....*....|....*....|....*.
gi 145332599 519 ASNAIALGTRIQDIKLAVHAHPTLSE 544
Cdd:PLN02507 452 IAVALKCGATKAQFDSTVGIHPSAAE 477
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
114-543 |
2.25e-49 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 178.52 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 114 IIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMksfGLQVS---AAGYDRQGVADHANNLATKIRNNLTNSMKAI 190
Cdd:PRK07845 29 VIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAEL---GIRFIddgEARVDLPAVNARVKALAAAQSADIRARLERE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 191 GVDILTGFGSV----LGPQKVKY----GKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGS 262
Cdd:PRK07845 106 GVRVIAGRGRLidpgLGPHRVKVttadGGEETLDADVVLIATGASPRILPTAEPDGERILTWRQLYDLDELPEHLIVVGS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 263 GYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITpaRDGKPVLIELIDAKtke 342
Cdd:PRK07845 186 GVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFAR-RGMTVLKRSRAESVE--RTGDGVVVTLTDGR--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 343 pkdTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQG-IS 420
Cdd:PRK07845 260 ---TVEGSHALMAVGSVPNTAGLGLEEAGVeLTPSGHITVDRVSR------TSVPGIYAAGDCTGVLPLASVAAMQGrIA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 421 VV----EQVSGrdhvLNHLSIPAACFTHPEISMVGLTEpQAKEKGEKEGfkvSVVKTSFKANTKALAENEGEGIAKMIYR 496
Cdd:PRK07845 331 MYhalgEAVSP----LRLKTVASNVFTRPEIATVGVSQ-AAIDSGEVPA---RTVMLPLATNPRAKMSGLRDGFVKLFCR 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 145332599 497 PDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLS 543
Cdd:PRK07845 403 PGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
120-546 |
2.62e-48 |
|
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: 175.93 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 120 VGGTCVNRGCVPSKALLAVSGRMRELQNEhhmKSFGLQvsaagYDRQGVADH------ANNLATKIRNNLTNSMKAI--G 191
Cdd:TIGR01423 47 LGGTCVNVGCVPKKLMVTGAQYMDTLRES---AGFGWE-----FDRSSVKANwkaliaAKNKAVLDINKSYEGMFADteG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 192 VDILTGFGSVlgPQK----VKYGKD------NIITAKDIIIATGSVPFVPK--GIEVdgktVITSDHALKLESVPEWIAI 259
Cdd:TIGR01423 119 LTFFLGWGAL--EDKnvvlVRESADpksavkERLQAEHILLATGSWPQMLGipGIEH----CISSNEAFYLDEPPRRVLT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 260 VGSGYIGLEFSDV---YTALGSEVTFIEALDQLMPGFDPEISK-LAQRVLINprKIDYHTGVFASKITPARDGKPVLiel 335
Cdd:TIGR01423 193 VGGGFISVEFAGIfnaYKPRGGKVTLCYRNNMILRGFDSTLRKeLTKQLRAN--GINIMTNENPAKVTLNADGSKHV--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 336 idakTKEPKDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAA 414
Cdd:TIGR01423 268 ----TFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVeLTKKGAIQVDEFSR------TNVPNIYAIGDVTDRVMLTPVA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 415 SAQGISVVEQVSG-RDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKegfkVSVVKTSFKANTKALAENEGEG-IAK 492
Cdd:TIGR01423 338 INEGAAFVDTVFGnKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK----VAVYESSFTPLMHNISGSKYKKfVAK 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145332599 493 MIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVL 546
Cdd:TIGR01423 414 IVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
103-550 |
1.41e-45 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 169.95 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 103 LHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAvSGRMRELQNEHHMKSfGLQVSAAGYDRQGVADHANNLATKIRN- 181
Cdd:PRK13748 115 LKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIR-AAHIAHLRRESPFDG-GIAATVPTIDRSRLLAQQQARVDELRHa 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 182 ---NLTNSMKAIGVdiLTGFGSVLGPQ----KVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVP 254
Cdd:PRK13748 193 kyeGILDGNPAITV--LHGEARFKDDQtlivRLNDGGERVVAFDRCLIATGASPAVPPIPGLKETPYWTSTEALVSDTIP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 255 EWIAIVGSGYIGLEFSDVYTALGSEVTfIEALDQLMPGFDPEISKlAQRVLINPRKIDYHTGVFASKITPArDGKPVLie 334
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVT-ILARSTLFFREDPAIGE-AVTAAFRAEGIEVLEHTQASQVAHV-DGEFVL-- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 335 lidaKTKEpkDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHA 413
Cdd:PRK13748 346 ----TTGH--GELRADKLLVATGRAPNTRSLALDAAGVtVNAQGAIVIDQGMR------TSVPHIYAAGDCTDQPQFVYV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 414 ASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGekegfkvsvVKTSFKANT-----KALAENEGE 488
Cdd:PRK13748 414 AAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDG---------IETDSRTLTldnvpRALANFDTR 484
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332599 489 GIAKMIYRPDNGEILGVHIfglhaadLIHEAsnaialGTRIQDIKLAVHAHPTLSEVLDELF 550
Cdd:PRK13748 485 GFIKLVIEEGSGRLIGVQA-------VAPEA------GELIQTAALAIRNRMTVQELADQLF 533
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
120-550 |
7.20e-41 |
|
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: 155.40 E-value: 7.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 120 VGGTCVNRGCVPSKaLLAVSGRM-RELQnehHMKSFGLQVSAA---GYDR--QGVADHANNLATKIRNNLtNSMKaigVD 193
Cdd:TIGR01438 45 IGGTCVNVGCIPKK-LMHQAALLgQALK---DSRNYGWKVEETvkhDWKRlvEAVQNHIGSLNWGYRVAL-REKK---VK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 194 ILTGFGSVLGPQKVKY----GKDNIITAKDIIIATGSVPFVPkGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEF 269
Cdd:TIGR01438 117 YENAYAEFVDKHRIKAtnkkGKEKIYSAERFLIATGERPRYP-GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALEC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 270 SDVYTALGSEVTfIEALDQLMPGFDPEISklaqrvlinpRKIDYH---TGV-FASKITPARdgkpvlIELIDAKT----- 340
Cdd:TIGR01438 196 AGFLAGIGLDVT-VMVRSILLRGFDQDCA----------NKVGEHmeeHGVkFKRQFVPIK------VEQIEAKVlveft 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 341 -KEPKDTLEVDAALIATGRAPFTNGLGLENVNVVTQR--GFIPVDERMRvidgkgTLVPNLYCIGD-ANGKLMLAHAASA 416
Cdd:TIGR01438 259 dSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKktGKIPADEEEQ------TNVPYIYAVGDiLEDKPELTPVAIQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 417 QGISVVEQV-SGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEgfKVSVVKTSFKANTKALAENEGEG--IAKM 493
Cdd:TIGR01438 333 AGRLLAQRLfKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEE--NVEVFHSYFWPLEWTIPSRDNHNkcYAKL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 145332599 494 I-YRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELF 550
Cdd:TIGR01438 411 VcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLS 468
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
61-544 |
1.22e-39 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 153.23 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 61 FLSRKSFQVSASASSNgngAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSG 140
Cdd:PTZ00058 26 FSFYHNLEASSAPTHL---KKKPRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAAS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 141 RMRELQNEHHmksFGLQVSAAgYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGK--------- 211
Cdd:PTZ00058 103 IHDILENSRH---YGFDTQFS-FNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgead 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 212 -------------------DNIITAKDIIIATGSVPFVP--KGIEvdgkTVITSDHALKLESvPEWIAIVGSGYIGLEFS 270
Cdd:PTZ00058 179 esdddevtivsagvsqlddGQVIEGKNILIAVGNKPIFPdvKGKE----FTISSDDFFKIKE-AKRIGIAGSGYIAVELI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 271 DVYTALGSEVTFIEALDQLMPGFDPEIS-KLAQRVLINPRKIDYHTGVfaSKITPARDgKPVLIELIDAKTKEpkdtlEV 349
Cdd:PTZ00058 254 NVVNRLGAESYIFARGNRLLRKFDETIInELENDMKKNNINIITHANV--EEIEKVKE-KNLTIYLSDGRKYE-----HF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 350 DAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRvidgkgTLVPNLYCIGDANG----------------------- 406
Cdd:PTZ00058 326 DYVIYCVGRSPNTEDLNLKALNIKTPKGYIKVDDNQR------TSVKHIYAVGDCCMvkknqeiedlnllklyneepylk 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 407 -----------KLMLAHAASAQGISVVEQVSG-RDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKV--SVVK 472
Cdd:PTZ00058 400 kkentsgesyyNVQLTPVAINAGRLLADRLFGpFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIyeSRFT 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332599 473 TSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSE 544
Cdd:PTZ00058 480 NLFFSVYDMDPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
109-554 |
4.03e-39 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 149.39 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 109 GLKTAIIE--GDVVGGTCVNRGCVPSKALLavsgrmrelqneHHMKSFGLQVSAAgydrQGVADHANNLATKirnNLTNS 186
Cdd:PRK08010 26 GWRVALIEqsNAMYGGTCINIGCIPTKTLV------------HDAQQHTDFVRAI----QRKNEVVNFLRNK---NFHNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 187 MKAIGVDILTGFGSVLGPQKVKY---GKDNIITAKDIIIATGSVPFVP--KGIEVDGKtVITSDHALKLESVPEWIAIVG 261
Cdd:PRK08010 87 ADMPNIDVIDGQAEFINNHSLRVhrpEGNLEIHGEKIFINTGAQTVVPpiPGITTTPG-VYDSTGLLNLKELPGHLGILG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 262 SGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLiNPRKIDYHTGVFASKITpARDGKpvlielidAKTK 341
Cdd:PRK08010 166 GGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATIL-RDQGVDIILNAHVERIS-HHENQ--------VQVH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 342 EPKDTLEVDAALIATGRAPFTNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDANGKLMLAHAASAQGIS 420
Cdd:PRK08010 236 SEHAQLAVDALLIASGRQPATASLHPENAGIaVNERGAIVVDKYLH------TTADNIWAMGDVTGGLQFTYISLDDYRI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 421 VVEQV--SGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEkegfKVSVVKTSFKANTKALAENEGEGIAKMIYRPD 498
Cdd:PRK08010 310 VRDELlgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGA----DIQVVTLPVAAIPRARVMNDTRGVLKAIVDNK 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 145332599 499 NGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAAK 554
Cdd:PRK08010 386 TQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK 441
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
437-549 |
5.01e-37 |
|
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: 133.45 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 437 IPAACFTHPEISMVGLTEPQAKEKGekegFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLI 516
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKG----GEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 145332599 517 HEASNAIALGTRIQDIKLAVHAHPTLSEVLDEL 549
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
120-550 |
1.54e-34 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 137.26 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 120 VGGTCVNRGCVPSKaLLAVSGRMRELQnEHHMKSFGLQVSAA---GYDRQGVADHANNLATKIRNNLTNSmkaiGVDILT 196
Cdd:PTZ00052 48 LGGTCVNVGCVPKK-LMHYAANIGSIF-HHDSQMYGWKTSSSfnwGKLVTTVQNHIRSLNFSYRTGLRSS----KVEYIN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 197 GFGSVLGPQKVKYG---KDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVY 273
Cdd:PTZ00052 122 GLAKLKDEHTVSYGdnsQEETITAKYILIATGGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 274 TALGSEVTfIEALDQLMPGFDPEISkLAQRVLINPRKIDYHTGVFASKITPARDgkPVLIELIDAKTKepkdtlEVDAAL 353
Cdd:PTZ00052 202 NELGFDVT-VAVRSIPLRGFDRQCS-EKVVEYMKEQGTLFLEGVVPINIEKMDD--KIKVLFSDGTTE------LFDTVL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 354 IATGRAPFTNGLGLENVNV-VTQRGFIpvdermrVIDGKGTLVPNLYCIGD-ANGKLMLAHAASAQGISVVEQV-SGRDH 430
Cdd:PTZ00052 272 YATGRKPDIKGLNLNAIGVhVNKSNKI-------IAPNDCTNIPNIFAVGDvVEGRPELTPVAIKAGILLARRLfKQSNE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 431 VLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSV-------VKTSFKANTKALAENEGE------GIAKMI-YR 496
Cdd:PTZ00052 345 FIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLqefntleIAAVHREKHERARKDEYDfdvssnCLAKLVcVK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145332599 497 PDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELF 550
Cdd:PTZ00052 425 SEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNLS 478
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
221-429 |
3.59e-28 |
|
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: 115.29 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 221 IIATGSVPFVP--KGIEVDG-KTVITSDHALKL-ESVPEW----IAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPG 292
Cdd:COG0446 83 VLATGARPRPPpiPGLDLPGvFTLRTLDDADALrEALKEFkgkrAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 293 FDPEISKLAQRVLINpRKIDYHTGVFASKITParDGKpVLIELIDaktkepKDTLEVDAALIATGRAPFTN---GLGLEn 369
Cdd:COG0446 163 LDPEMAALLEEELRE-HGVELRLGETVVAIDG--DDK-VAVTLTD------GEEIPADLVVVAPGVRPNTElakDAGLA- 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 370 vnvVTQRGFIPVDERMRvidgkgTLVPNLYCIGDA-------NGK---LMLAHAASAQGISVVEQVSGRD 429
Cdd:COG0446 232 ---LGERGWIKVDETLQ------TSDPDVYAAGDCaevphpvTGKtvyIPLASAANKQGRVAAENILGGP 292
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
221-429 |
3.77e-20 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 92.90 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 221 IIATGSVPFVP--KGIEVDG-KTVITSDHALKLEsvpEW------IAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMP 291
Cdd:COG1251 103 VLATGSRPRVPpiPGADLPGvFTLRTLDDADALR---AAlapgkrVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 292 G-FDPEISKLAQRVLINpRKIDYHTGVFASKITpaRDGKPVLIELIDAktkepkDTLEVDAALIATGRAPFTnGLgLENV 370
Cdd:COG1251 180 RqLDEEAGALLQRLLEA-LGVEVRLGTGVTEIE--GDDRVTGVRLADG------EELPADLVVVAIGVRPNT-EL-ARAA 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332599 371 NVVTQRGfIPVDERMRvidgkgTLVPNLYCIGD-------ANGKLMLAHAASA--QGISVVEQVSGRD 429
Cdd:COG1251 249 GLAVDRG-IVVDDYLR------TSDPDIYAAGDcaehpgpVYGRRVLELVAPAyeQARVAAANLAGGP 309
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
257-334 |
2.22e-16 |
|
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: 74.16 E-value: 2.22e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332599 257 IAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKPVLIE 334
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEK-NGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
211-544 |
3.65e-16 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 81.24 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 211 KDNIITAKDI-------------IIATGSVPFVPKGIEVDGKTVIT----SD-----HALKLESVPEwIAIVGSGYIGLE 268
Cdd:PRK09564 85 KNKTITVKNLktgsifndtydklMIATGARPIIPPIKNINLENVYTlksmEDglalkELLKDEEIKN-IVIIGAGFIGLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 269 FSDVYTALGSEVTFIEALDQLMPG-FDPEISKLAQRVLINpRKIDYHTGVFASKITPARDGKPVLIElidaktkepKDTL 347
Cdd:PRK09564 164 AVEAAKHLGKNVRIIQLEDRILPDsFDKEITDVMEEELRE-NGVELHLNEFVKSLIGEDKVEGVVTD---------KGEY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 348 EVDAALIATGRAP---FTNGLGLEnvnvVTQRGFIPVDERMRvidgkgTLVPNLYCIGD-------ANGKLM---LAHAA 414
Cdd:PRK09564 234 EADVVIVATGVKPnteFLEDTGLK----TLKNGAIIVDEYGE------TSIENIYAAGDcatiyniVSNKNVyvpLATTA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 415 SAQGISVVEQVSGRDHV---------LNHLSIPAACfthpeismVGLTEPQAKEKGEKegFKVSVVKtsfKANTKALAEN 485
Cdd:PRK09564 304 NKLGRMVGENLAGRHVSfkgtlgsacIKVLDLEAAR--------TGLTEEEAKKLGID--YKTVFIK---DKNHTNYYPG 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 145332599 486 EGEGIAKMIYRPDNGEILGVHIFGLHAADLiheasnaialgtRIQDIKLAVHAHPTLSE 544
Cdd:PRK09564 371 QEDLYVKLIYEADTKVILGGQIIGKKGAVL------------RIDALAVAIYAKLTTQE 417
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
221-425 |
6.56e-16 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 79.79 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 221 IIATGSVP--FVPKGIEVDGKTVITSDHALKL----------ESVPEW--IAIVGSGYIGLEFS----------DVYTAL 276
Cdd:COG1252 102 VIATGSVTnfFGIPGLAEHALPLKTLEDALALrerllaaferAERRRLltIVVVGGGPTGVELAgelaellrklLRYPGI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 277 GS---EVTFIEALDQLMPGFDPEISKLAQRVLINpRKIDYHTGVFASKITPARdgkpvlIELIDAktkepkDTLEVDAAL 353
Cdd:COG1252 182 DPdkvRITLVEAGPRILPGLGEKLSEAAEKELEK-RGVEVHTGTRVTEVDADG------VTLEDG------EEIPADTVI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 354 IATG-RA-PFTNGLGLEnvnvVTQRGFIPVDERMRVIDgkgtlVPNLYCIGDA------NGKLM--LAHAASAQGISVVE 423
Cdd:COG1252 249 WAAGvKApPLLADLGLP----TDRRGRVLVDPTLQVPG-----HPNVFAIGDCaavpdpDGKPVpkTAQAAVQQAKVLAK 319
|
..
gi 145332599 424 QV 425
Cdd:COG1252 320 NI 321
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
103-418 |
7.91e-15 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 75.54 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 103 LHAVEKGLKTAIIEGDVVGGTCVNRGCV------PSKallaVSG-----RMRElqnehHMKSFGLQVSAAgydrqgvadh 171
Cdd:COG0492 17 IYAARAGLKTLVIEGGEPGGQLATTKEIenypgfPEG----ISGpelaeRLRE-----QAERFGAEILLE---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 172 annlatkirnnltnsmKAIGVDiLTGfgsvlGPQKVKYGKDNIITAKDIIIATGSVP----------FVPKGI------- 234
Cdd:COG0492 78 ----------------EVTSVD-KDD-----GPFRVTTDDGTEYEAKAVIIATGAGPrklglpgeeeFEGRGVsycatcd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 235 --EVDGKTVitsdhalklesvpewiAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDpeiskLAQRVLINPrKID 312
Cdd:COG0492 136 gfFFRGKDV----------------VVVGGGDSALEEALYLTKFASKVTLIHRRDELRASKI-----LVERLRANP-KIE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 313 YHTGvfaSKITPARdGKPVL--IELIDAKTKEPKdTLEVDAALIATGRAP---FTNGLGLEnvnvVTQRGFIPVDERMRv 387
Cdd:COG0492 194 VLWN---TEVTEIE-GDGRVegVTLKNVKTGEEK-ELEVDGVFVAIGLKPnteLLKGLGLE----LDEDGYIVVDEDME- 263
|
330 340 350
....*....|....*....|....*....|..
gi 145332599 388 idgkgTLVPNLYCIGD-ANGKLMLAHAASAQG 418
Cdd:COG0492 264 -----TSVPGVFAAGDvRDYKYRQAATAAGEG 290
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
221-409 |
1.46e-08 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 57.23 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 221 IIATGSVPFVPkgiEVDGKTVItsdhaLKLESVPEW------------IAIVGSGYIGLEFS-DVYTAlGSEVTFIEALD 287
Cdd:PRK04965 104 VLATGASAFVP---PIPGRELM-----LTLNSQQEYraaetqlrdaqrVLVVGGGLIGTELAmDLCRA-GKAVTLVDNAA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 288 QLMPGFDPEI--SKLAQRVLINPRKIDYHTGVfaSKITPARDGkpVLIELIDAKtkepkdTLEVDAALIATGRAPFTnGL 365
Cdd:PRK04965 175 SLLASLMPPEvsSRLQHRLTEMGVHLLLKSQL--QGLEKTDSG--IRATLDSGR------SIEVDAVIAAAGLRPNT-AL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 145332599 366 GLEnVNVVTQRGfIPVDERMRvidgkgTLVPNLYCIGDA---NGKLM 409
Cdd:PRK04965 244 ARR-AGLAVNRG-IVVDSYLQ------TSAPDIYALGDCaeiNGQVL 282
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
240-403 |
7.77e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 48.77 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 240 TVITSDHALKLESV--PE-WIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPeisKLAQRVLINPRKidyHTG 316
Cdd:PRK09754 127 TLRHAGDAARLREVlqPErSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAP---PPVQRYLLQRHQ---QAG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 317 V---FASKITPARDGKPVLIELidaktkEPKDTLEVDAALIATGrAPFTNGLGLEnVNVVTQRGfIPVDERMRVIDgkgt 393
Cdd:PRK09754 201 VrilLNNAIEHVVDGEKVELTL------QSGETLQADVVIYGIG-ISANDQLARE-ANLDTANG-IVIDEACRTCD---- 267
|
170
....*....|
gi 145332599 394 lvPNLYCIGD 403
Cdd:PRK09754 268 --PAIFAGGD 275
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
259-431 |
1.07e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 45.16 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 259 IVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLiNPRKIDYHTGVFASKItparDGKPVlielida 338
Cdd:PRK13512 153 VVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDEL-DKREIPYRLNEEIDAI----NGNEV------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 339 kTKEPKDTLEVDAALIATGRAPftNGLGLENVNV-VTQRGFIPVDERMRvidgkgTLVPNLYCIGDA----------NGK 407
Cdd:PRK13512 221 -TFKSGKVEHYDMIIEGVGTHP--NSKFIESSNIkLDDKGFIPVNDKFE------TNVPNIYAIGDIitshyrhvdlPAS 291
|
170 180
....*....|....*....|....*
gi 145332599 408 LMLAHAASaQGISVV-EQVSGRDHV 431
Cdd:PRK13512 292 VPLAWGAH-RAASIVaEQIAGNDTI 315
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
214-403 |
2.36e-04 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 44.43 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 214 IITAKD-------IIIATGSVPFVP--KGIEVDGKTVI-TSDHALKLESVPEWI---AIVGSGYIGLEFSDVYTALGSEV 280
Cdd:TIGR02374 87 VITDAGrtlsydkLILATGSYPFILpiPGADKKGVYVFrTIEDLDAIMAMAQRFkkaAVIGGGLLGLEAAVGLQNLGMDV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332599 281 TFIEALDQLMpgfDPEISKLAQRVL---INPRKIDYHTGVFASKITpaRDGKPVLIELIDAktkepkDTLEVDAALIATG 357
Cdd:TIGR02374 167 SVIHHAPGLM---AKQLDQTAGRLLqreLEQKGLTFLLEKDTVEIV--GATKADRIRFKDG------SSLEADLIVMAAG 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145332599 358 RAPftnglgleNVNVVTQRGfIPVDERMRVIDGKGTLVPNLYCIGD 403
Cdd:TIGR02374 236 IRP--------NDELAVSAG-IKVNRGIIVNDSMQTSDPDIYAVGE 272
|
|
| |
