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Conserved domains on  [gi|15231702|ref|NP_190856|]
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monodehydroascorbate reductase 1 [Arabidopsis thaliana]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441266)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-396 8.34e-77

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 244.28  E-value: 8.34e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   7 KYIILGGGVSAGYAAKEFANQGVQpGELAVISKEAVAPYERPALSKGYLFPEGAARLPgfhccvgsggekLLPES-YKQK 85
Cdd:COG1251   3 RIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLL------------LRPADfYEEN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  86 GIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKAKKggk 165
Cdd:COG1251  70 GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVP---PIPGADLPGVFTLRTLDDADALRAALAPGKrvv 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 166 avvvgggYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAqpNGEVKEVQLK 245
Cdd:COG1251 147 v--igggLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG--DDRVTGVRLA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 246 DGRTLEADIVIVGVGAKPLTSLFKG---QVEedkGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDvRRVEHVDHSRKSA 322
Cdd:COG1251 223 DGEELPADLVVVAIGVRPNTELARAaglAVD---RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQA 298

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231702 323 EQAVKAIKaaegGAAVEEYDYLPFFYSRSFDLSWQFYGDNVGD--SVLFGDSnpsnPKPRFGAYWVQGGKVVGAFM 396
Cdd:COG1251 299 RVAAANLA----GGPAAYEGSVPSTKLKVFGVDVASAGDAEGDeeVVVRGDP----ARGVYKKLVLRDGRLVGAVL 366
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-396 8.34e-77

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 244.28  E-value: 8.34e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   7 KYIILGGGVSAGYAAKEFANQGVQpGELAVISKEAVAPYERPALSKGYLFPEGAARLPgfhccvgsggekLLPES-YKQK 85
Cdd:COG1251   3 RIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLL------------LRPADfYEEN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  86 GIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKAKKggk 165
Cdd:COG1251  70 GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVP---PIPGADLPGVFTLRTLDDADALRAALAPGKrvv 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 166 avvvgggYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAqpNGEVKEVQLK 245
Cdd:COG1251 147 v--igggLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG--DDRVTGVRLA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 246 DGRTLEADIVIVGVGAKPLTSLFKG---QVEedkGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDvRRVEHVDHSRKSA 322
Cdd:COG1251 223 DGEELPADLVVVAIGVRPNTELARAaglAVD---RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQA 298

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231702 323 EQAVKAIKaaegGAAVEEYDYLPFFYSRSFDLSWQFYGDNVGD--SVLFGDSnpsnPKPRFGAYWVQGGKVVGAFM 396
Cdd:COG1251 299 RVAAANLA----GGPAAYEGSVPSTKLKVFGVDVASAGDAEGDeeVVVRGDP----ARGVYKKLVLRDGRLVGAVL 366
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-322 4.33e-46

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: 161.33  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702     6 FKYIILGGGVsAGYAAKEFANQgvQPGELAVISKEAVAPYERPALSKGYLFPEGAARLPGFHCCVGSGGEKLLPESykQK 85
Cdd:pfam07992   1 YDVVVIGGGP-AGLAAALTLAQ--LGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRKEEVVKKL--NN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    86 GIELILSTEIVKAD-----LSAKSLVSATGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKA 160
Cdd:pfam07992  76 GIEVLLGTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLP---PIPGVELNVGFLVRTLDSAEALRLKLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   161 KKGGKAVVVgggYIGLELSAVLRINNLDVTMVFPEPWcMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTaqPNGEVK 240
Cdd:pfam07992 153 KRVVVVGGG---YIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEII--GDGDGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   241 EVQLKDGRTLEADIVIVGVGAKPLTSLFK-GQVEEDK-GGIKTDAFFKTSVPDVYAVGDVatfplkmygDVRRVEHVDHS 318
Cdd:pfam07992 227 EVILKDGTEIDADLVVVAIGRRPNTELLEaAGLELDErGGIVVDEYLRTSVPGIYAAGDC---------RVGGPELAQNA 297


                  ....
gi 15231702   319 RKSA 322
Cdd:pfam07992 298 VAQG 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-394 1.20e-30

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 121.96  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    1 MAEKSFkyIILGGGVSAGYAAKEFANQGVQpGELAVISKEAVAPYERPALSKGYLF-PEGAARlpgfhccvgsggeKLLP 79
Cdd:PRK09754   1 MKEKTI--IIVGGGQAAAMAAASLRQQGFT-GELHLFSDERHLPYERPPLSKSMLLeDSPQLQ-------------QVLP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   80 ES-YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTDFGVKGadsKNILYLREIDDADKLVEAI 158
Cdd:PRK09754  65 ANwWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALG---ERCFTLRHAGDAARLREVL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  159 KAKKGGKAVVVGGgyIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTvasGFTAQPNGE 238
Cdd:PRK09754 142 QPERSVVIVGAGT--IGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  239 VKEVQLKDGRTLEADIVIVGVGAKpltslFKGQVEED-----KGGIKTDAFFKTSVPDVYAVGDVATFPLKMyGDVRRVE 313
Cdd:PRK09754 217 KVELTLQSGETLQADVVIYGIGIS-----ANDQLAREanldtANGIVIDEACRTCDPAIFAGGDVAITRLDN-GALHRCE 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  314 HVDHSRKSAEQAVKAIKAAE---GGAaveeydylPFFYSRSFDLSWQFYGDNVGDSVLFgDSNPSNPKprfgAYWV--QG 388
Cdd:PRK09754 291 SWENANNQAQIAAAAMLGLPlplLPP--------PWFWSDQYSDNLQFIGDMRGDDWLC-RGNPETQK----AIWFnlQN 357


                 ....*.
gi 15231702  389 GKVVGA 394
Cdd:PRK09754 358 GVLIGA 363
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-372 6.21e-22

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 98.75  E-value: 6.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    82 YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTdfgVKGADSKNILYLREIDDADKLVEAikAK 161
Cdd:TIGR02374  64 YEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATGSYPFILP---IPGADKKGVYVFRTIEDLDAIMAM--AQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   162 KGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKII--KGTVASgftaQPNGEV 239
Cdd:TIGR02374 139 RFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLleKDTVEI----VGATKA 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   240 KEVQLKDGRTLEADIVIVGVGAKPLTSLFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDVR--------R 311
Cdd:TIGR02374 215 DRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAplyeqakvL 294

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231702   312 VEHV-DHSRKSAEQAVKAIK---------------AAEGGAAVEEYDYLPFFYSRSFdlswqFYGDNVGDSVLFGDS 372
Cdd:TIGR02374 295 ADHIcGVECEEYEGSDLSAKlkllgvdvwsagdaqETERTTSIKIYDEQKGIYKKLV-----LSDDKLLGAVLFGDT 366
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-396 8.34e-77

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 244.28  E-value: 8.34e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   7 KYIILGGGVSAGYAAKEFANQGVQpGELAVISKEAVAPYERPALSKGYLFPEGAARLPgfhccvgsggekLLPES-YKQK 85
Cdd:COG1251   3 RIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLL------------LRPADfYEEN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  86 GIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKAKKggk 165
Cdd:COG1251  70 GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVP---PIPGADLPGVFTLRTLDDADALRAALAPGKrvv 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 166 avvvgggYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAqpNGEVKEVQLK 245
Cdd:COG1251 147 v--igggLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG--DDRVTGVRLA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 246 DGRTLEADIVIVGVGAKPLTSLFKG---QVEedkGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDvRRVEHVDHSRKSA 322
Cdd:COG1251 223 DGEELPADLVVVAIGVRPNTELARAaglAVD---RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQA 298

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231702 323 EQAVKAIKaaegGAAVEEYDYLPFFYSRSFDLSWQFYGDNVGD--SVLFGDSnpsnPKPRFGAYWVQGGKVVGAFM 396
Cdd:COG1251 299 RVAAANLA----GGPAAYEGSVPSTKLKVFGVDVASAGDAEGDeeVVVRGDP----ARGVYKKLVLRDGRLVGAVL 366
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 32-361 3.13e-55

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: 185.79  E-value: 3.13e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  32 GELAVISKEAVAPYERPALSkgYLFPEGAARLpgfhccvgsggEKLL---PESYKQKGIELILSTEIVKADLSAKSLVSA 108
Cdd:COG0446   6 AEITVIEKGPHHSYQPCGLP--YYVGGGIKDP-----------EDLLvrtPESFERKGIDVRTGTEVTAIDPEAKTVTLR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 109 TGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKAKKGGKAVVVGGGYIGLELSAVLRINNLD 188
Cdd:COG0446  73 DGETLSYDKLVLATGARPRPP---PIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 189 VTMVFPEPWCMPRlFTADIAAFYETYYTNKGVKIIKGTVASGFTAQpngEVKEVQLKDGRTLEADIVIVGVGAKPLTSLF 268
Cdd:COG0446 150 VTLVERAPRLLGV-LDPEMAALLEEELREHGVELRLGETVVAIDGD---DKVAVTLTDGEEIPADLVVVAPGVRPNTELA 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 269 KG-QVEEDK-GGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDVRRVEHVDHSRKSAEQAVKAIKaaeGGAAveEYDYLPF 346
Cdd:COG0446 226 KDaGLALGErGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENIL---GGPA--PFPGLGT 300

                       330
                ....*....|....*
gi 15231702 347 FYSRSFDLSWQFYGD 361
Cdd:COG0446 301 FISKVFDLCIASTGT 315
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-322 4.33e-46

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: 161.33  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702     6 FKYIILGGGVsAGYAAKEFANQgvQPGELAVISKEAVAPYERPALSKGYLFPEGAARLPGFHCCVGSGGEKLLPESykQK 85
Cdd:pfam07992   1 YDVVVIGGGP-AGLAAALTLAQ--LGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRKEEVVKKL--NN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    86 GIELILSTEIVKAD-----LSAKSLVSATGDVFKYQTLIIATGSTVLRLtdfGVKGADSKNILYLREIDDADKLVEAIKA 160
Cdd:pfam07992  76 GIEVLLGTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLP---PIPGVELNVGFLVRTLDSAEALRLKLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   161 KKGGKAVVVgggYIGLELSAVLRINNLDVTMVFPEPWcMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTaqPNGEVK 240
Cdd:pfam07992 153 KRVVVVGGG---YIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEII--GDGDGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   241 EVQLKDGRTLEADIVIVGVGAKPLTSLFK-GQVEEDK-GGIKTDAFFKTSVPDVYAVGDVatfplkmygDVRRVEHVDHS 318
Cdd:pfam07992 227 EVILKDGTEIDADLVVVAIGRRPNTELLEaAGLELDErGGIVVDEYLRTSVPGIYAAGDC---------RVGGPELAQNA 297


                  ....
gi 15231702   319 RKSA 322
Cdd:pfam07992 298 VAQG 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-394 1.20e-30

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 121.96  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    1 MAEKSFkyIILGGGVSAGYAAKEFANQGVQpGELAVISKEAVAPYERPALSKGYLF-PEGAARlpgfhccvgsggeKLLP 79
Cdd:PRK09754   1 MKEKTI--IIVGGGQAAAMAAASLRQQGFT-GELHLFSDERHLPYERPPLSKSMLLeDSPQLQ-------------QVLP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   80 ES-YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTDFGVKGadsKNILYLREIDDADKLVEAI 158
Cdd:PRK09754  65 ANwWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALG---ERCFTLRHAGDAARLREVL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  159 KAKKGGKAVVVGGgyIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTvasGFTAQPNGE 238
Cdd:PRK09754 142 QPERSVVIVGAGT--IGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  239 VKEVQLKDGRTLEADIVIVGVGAKpltslFKGQVEED-----KGGIKTDAFFKTSVPDVYAVGDVATFPLKMyGDVRRVE 313
Cdd:PRK09754 217 KVELTLQSGETLQADVVIYGIGIS-----ANDQLAREanldtANGIVIDEACRTCDPAIFAGGDVAITRLDN-GALHRCE 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  314 HVDHSRKSAEQAVKAIKAAE---GGAaveeydylPFFYSRSFDLSWQFYGDNVGDSVLFgDSNPSNPKprfgAYWV--QG 388
Cdd:PRK09754 291 SWENANNQAQIAAAAMLGLPlplLPP--------PWFWSDQYSDNLQFIGDMRGDDWLC-RGNPETQK----AIWFnlQN 357


                 ....*.
gi 15231702  389 GKVVGA 394
Cdd:PRK09754 358 GVLIGA 363
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-372 6.21e-22

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 98.75  E-value: 6.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    82 YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTdfgVKGADSKNILYLREIDDADKLVEAikAK 161
Cdd:TIGR02374  64 YEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATGSYPFILP---IPGADKKGVYVFRTIEDLDAIMAM--AQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   162 KGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKII--KGTVASgftaQPNGEV 239
Cdd:TIGR02374 139 RFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLleKDTVEI----VGATKA 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   240 KEVQLKDGRTLEADIVIVGVGAKPLTSLFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDVR--------R 311
Cdd:TIGR02374 215 DRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAplyeqakvL 294

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231702   312 VEHV-DHSRKSAEQAVKAIK---------------AAEGGAAVEEYDYLPFFYSRSFdlswqFYGDNVGDSVLFGDS 372
Cdd:TIGR02374 295 ADHIcGVECEEYEGSDLSAKlkllgvdvwsagdaqETERTTSIKIYDEQKGIYKKLV-----LSDDKLLGAVLFGDT 366
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
9-343 7.14e-22

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 96.74  E-value: 7.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   9 IILGGGVsAG-YAAKEFANQGVQPGELAVISKEAVAPYeRPalskgyLFPE-GAARLPGFHCCVGsggeklLPESYKQKG 86
Cdd:COG1252   5 VIVGGGF-AGlEAARRLRKKLGGDAEVTLIDPNPYHLF-QP------LLPEvAAGTLSPDDIAIP------LRELLRRAG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  87 IELILStEIVKADLSAKSLVSATGDVFKYQTLIIATGStvlRLTDFGVKGADsKNILYLREIDDADKLVEAIKAKKGGKA 166
Cdd:COG1252  71 VRFIQG-EVTGIDPEARTVTLADGRTLSYDYLVIATGS---VTNFFGIPGLA-EHALPLKTLEDALALRERLLAAFERAE 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 167 VVVGGGYI-------GLELSAVL-------------RINNLDVTMVFPEPWCMPRlFTADIAAFYETYYTNKGVKIIKGT 226
Cdd:COG1252 146 RRRLLTIVvvgggptGVELAGELaellrkllrypgiDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGT 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 227 VASGFTAqpngevKEVQLKDGRTLEADIVIV--GVGAKPLTSLFKGQVEEdKGGIKTDAFFKT-SVPDVYAVGDVATFPL 303
Cdd:COG1252 225 RVTEVDA------DGVTLEDGEEIPADTVIWaaGVKAPPLLADLGLPTDR-RGRVLVDPTLQVpGHPNVFAIGDCAAVPD 297

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15231702 304 KMYGDVRRVEHvdHSRKSAEQAVKAIKAAEGGAAVEEYDY 343
Cdd:COG1252 298 PDGKPVPKTAQ--AAVQQAKVLAKNIAALLRGKPLKPFRY 335
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 79-300 1.29e-19

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 90.48  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   79 PESYKQKGIELILSTEIVKADLSAKSLV---SATGDVF--KYQTLIIATGStvlRLTDFGVKGADSKNILYLREIDDADK 153
Cdd:PRK09564  63 PEEFIKSGIDVKTEHEVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGA---RPIIPPIKNINLENVYTLKSMEDGLA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  154 LVEAIKAKKGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTA 233
Cdd:PRK09564 140 LKELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIG 219

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231702  234 qpNGEVKEVqLKDGRTLEADIVIVGVGAKPLTSLFKGQVEE--DKGGIKTDAFFKTSVPDVYAVGDVAT 300
Cdd:PRK09564 220 --EDKVEGV-VTDKGEYEADVVIVATGVKPNTEFLEDTGLKtlKNGAIIVDEYGETSIENIYAAGDCAT 285
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 3-302 7.43e-18

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: 85.14  E-value: 7.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   3 EKSFKYIILGGGvSAGYAAkefANQGVQPG-ELAVIskeavapyERPAL-----------SKGYLFP----EGAARLPGF 66
Cdd:COG1249   1 MKDYDLVVIGAG-PGGYVA---AIRAAQLGlKVALV--------EKGRLggtclnvgcipSKALLHAaevaHEARHAAEF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  67 HCCVGSGG-----------------EKLLPESYKQKGIELILST-EIVkadlSAKSLVSATGDVFKYQTLIIATGSTVLR 128
Cdd:COG1249  69 GISAGAPSvdwaalmarkdkvvdrlRGGVEELLKKNGVDVIRGRaRFV----DPHTVEVTGGETLTADHIVIATGSRPRV 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 129 LTDFGVKGA---DSKNILYLREIddADKLVeaikakkggkavvvgggYIGLELSAVLRinNL--DVTMVfpEPwcMPRL- 202
Cdd:COG1249 145 PPIPGLDEVrvlTSDEALELEEL--PKSLVvig------------ggYIGLEFAQIFA--RLgsEVTLV--ER--GDRLl 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 203 --FTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGevKEVQLKDGR---TLEADIVIVGVGAKPLTSLF---KGQVE- 273
Cdd:COG1249 205 pgEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG--VTVTLEDGGgeeAVEADKVLVATGRRPNTDGLgleAAGVEl 282

                       330       340
                ....*....|....*....|....*....
gi 15231702 274 EDKGGIKTDAFFKTSVPDVYAVGDVATFP 302
Cdd:COG1249 283 DERGGIKVDEYLRTSVPGIYAIGDVTGGP 311
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 82-298 7.32e-15

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: 76.14  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702    82 YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLT-DFGVKGA---DSKNILYLREIddADKLVea 157
Cdd:TIGR01350  99 LKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPgPFDFDGKvviTSTGALNLEEV--PESLV-- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   158 ikakkggkavVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPrLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNG 237
Cdd:TIGR01350 175 ----------IIGGGVIGIEFASIFASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQ 243

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231702   238 EVKEVQLKDGRTLEADIVIVGVGAKPLTS---LFKGQVEEDK-GGIKTDAFFKTSVPDVYAVGDV 298
Cdd:TIGR01350 244 VTYENKGGETETLTGEKVLVAVGRKPNTEglgLEKLGVELDErGRIVVDEYMRTNVPGIYAIGDV 308
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 110-299 5.20e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 73.64  E-value: 5.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  110 GDVFKYQTLIIATGSTVLRLTDFGVKG---ADSKNILYLREIddADKLVeaikakkggkavVVGGGYIGLELSAVLRinN 186
Cdd:PRK06416 130 EQTYTAKNIILATGSRPRELPGIEIDGrviWTSDEALNLDEV--PKSLV------------VIGGGYIGVEFASAYA--S 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  187 L--DVTMVfpEpwCMPRL---FTADIAAFYETYYTNKGVKIIKGTVASGftAQPNGEVKEVQLKDG---RTLEADIVIVG 258
Cdd:PRK06416 194 LgaEVTIV--E--ALPRIlpgEDKEISKLAERALKKRGIKIKTGAKAKK--VEQTDDGVTVTLEDGgkeETLEADYVLVA 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15231702  259 VGAKPLTS---LFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDVA 299
Cdd:PRK06416 268 VGRRPNTEnlgLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIV 311
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
217-344 6.42e-14

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 72.07  E-value: 6.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 217 NKGVKIIKGTVASGFTAqpNGEVKEVQLKDGRT-----LEADIVIVGVGAKPLTSLFKGQVEE--DKGGIKTDAFFKTSV 289
Cdd:COG0492 189 NPKIEVLWNTEVTEIEG--DGRVEGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLEldEDGYIVVDEDMETSV 266

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231702 290 PDVYAVGDVATFPLKmygdvrrvehvdhsrksaeQAVKAikAAEGG-AAVEEYDYL 344
Cdd:COG0492 267 PGVFAAGDVRDYKYR-------------------QAATA--AGEGAiAALSAARYL 301
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 79-300 1.31e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 69.04  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   79 PESYKQ-KGIELILSTEIVKADLSAKSLV---SATGDVFK--YQTLIIATGSTVLRLtdfgvkGADSKNILYLREIDDAD 152
Cdd:PRK13512  64 PEKFYDrKQITVKTYHEVIAINDERQTVTvlnRKTNEQFEesYDKLILSPGASANSL------GFESDITFTLRNLEDTD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  153 KLVEAIKAKKGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWcMPRLFTADI--AAFYE------TYYTNKGVKIIK 224
Cdd:PRK13512 138 AIDQFIKANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDK-INKLMDADMnqPILDEldkreiPYRLNEEIDAIN 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231702  225 GtvasgftaqpngevKEVQLKDGRTLEADIVIVGVGAKPLTSLFKGQ--VEEDKGGIKTDAFFKTSVPDVYAVGDVAT 300
Cdd:PRK13512 217 G--------------NEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSniKLDDKGFIPVNDKFETNVPNIYAIGDIIT 280
PRK06116 PRK06116
glutathione reductase; Validated
 173-298 1.47e-12

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 69.03  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVF--PEPWcmpRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKeVQLKDGRTL 250
Cdd:PRK06116 177 YIAVEFAGVLNGLGSETHLFVrgDAPL---RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLT-LTLEDGETL 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15231702  251 EADIVIVGVGAKPLTS---LFKGQVE-EDKGGIKTDAFFKTSVPDVYAVGDV 298
Cdd:PRK06116 253 TVDCLIWAIGREPNTDglgLENAGVKlNEKGYIIVDEYQNTNVPGIYAVGDV 304
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
174-299 2.64e-11

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 64.94  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  174 IGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVkeVQLKDGRTLEAD 253
Cdd:PRK04965 152 IGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIR--ATLDSGRSIEVD 229

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15231702  254 IVIVGVGAKPLTSLFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDVA 299
Cdd:PRK04965 230 AVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCA 275
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 116-303 2.54e-10

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 62.12  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  116 QTLIIATGSTVLRLTdfGVKGADSKNILYLREIDDADKLVE--AIKAKKggkavvvgggYIGLELSAVLRINNLDVTM-- 191
Cdd:PRK06292 132 KNIVIATGSRVPPIP--GVWLILGDRLLTSDDAFELDKLPKslAVIGGG----------VIGLELGQALSRLGVKVTVfe 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  192 ----VFPepwcmprLFTADIAAFYETYYtNKGVKIIKGTVASGFTaQPNGEVKEVQLKDG--RTLEADIVIVGVGAKPLT 265
Cdd:PRK06292 200 rgdrILP-------LEDPEVSKQAQKIL-SKEFKIKLGAKVTSVE-KSGDEKVEELEKGGktETIEADYVLVATGRRPNT 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15231702  266 ---SLFKGQVEEDKGG-IKTDAFFKTSVPDVYAVGDVATFPL 303
Cdd:PRK06292 271 dglGLENTGIELDERGrPVVDEHTQTSVPGIYAAGDVNGKPP 312
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 216-298 5.27e-09

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: 58.06  E-value: 5.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   216 TNKGVKIIKGTVASGFTAQPNGEvKEVQLKDGRTLEADIVIVGVGAKPLTS---LFKGQVE-EDKGGIKTDAFFKTSVPD 291
Cdd:TIGR01423 242 RANGINIMTNENPAKVTLNADGS-KHVTFESGKTLDVDVVMMAIGRVPRTQtlqLDKVGVElTKKGAIQVDEFSRTNVPN 320


                  ....*..
gi 15231702   292 VYAVGDV 298
Cdd:TIGR01423 321 IYAIGDV 327
PRK06370 PRK06370
FAD-containing oxidoreductase;
173-298 1.56e-08

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 56.36  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVFPEPWCMPRlFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKEVQLKDGR-TLE 251
Cdd:PRK06370 181 YIGLEFAQMFRRFGSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGGApEIT 259

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15231702  252 ADIVIVGVGAKPLTS---LFKGQVEEDK-GGIKTDAFFKTSVPDVYAVGDV 298
Cdd:PRK06370 260 GSHILVAVGRVPNTDdlgLEAAGVETDArGYIKVDDQLRTTNPGIYAAGDC 310
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 205-303 1.69e-08

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 56.41  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  205 ADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVkeVQLKDGRTLEADIVIVGVGAKPLTS---LFKGQVEEDKGG-IK 280
Cdd:PRK07845 218 ADAAEVLEEVFARRGMTVLKRSRAESVERTGDGVV--VTLTDGRTVEGSHALMAVGSVPNTAglgLEEAGVELTPSGhIT 295

                         90       100
                 ....*....|....*....|....
gi 15231702  281 TDAFFKTSVPDVYAVGDV-ATFPL 303
Cdd:PRK07845 296 VDRVSRTSVPGIYAAGDCtGVLPL 319
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 82-309 1.86e-08

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 56.67  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   82 YKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTdfgVKGADSKNILYLREIDDAdKLVEAiKAK 161
Cdd:PRK14989  69 YEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPP---IKGSETQDCFVYRTIEDL-NAIEA-CAR 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  162 KGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKE 241
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKT 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231702  242 VQLKDGRTLEADIVIVGVGAKPLTSLFKgQVEED---KGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDV 309
Cdd:PRK14989 224 MRFADGSELEVDFIVFSTGIRPQDKLAT-QCGLAvapRGGIVINDSCQTSDPDIYAIGECASWNNRVFGLV 293
PRK07846 PRK07846
mycothione reductase; Reviewed
 173-304 2.30e-08

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 55.73  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVFPEPwCMPRLFTADIAAFYeTYYTNKGVKIIKGTVASGFTAQPNGevKEVQLKDGRTLEA 252
Cdd:PRK07846 176 FIAAEFAHVFSALGVRVTVVNRSG-RLLRHLDDDISERF-TELASKRWDVRLGRNVVGVSQDGSG--VTLRLDDGSTVEA 251

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231702  253 DIVIVGVGAKP---LTSLFKGQVEEDKGG-IKTDAFFKTSVPDVYAVGDVAT-FPLK 304
Cdd:PRK07846 252 DVLLVATGRVPngdLLDAAAAGVDVDEDGrVVVDEYQRTSAEGVFALGDVSSpYQLK 308
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 174-303 1.41e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 53.39  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  174 IGLELSAVLRINNLDVTMVfpEpwCMPRLFTA---DIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKEVQLKDG--R 248
Cdd:PRK06327 194 IGLELGSVWRRLGAEVTIL--E--ALPAFLAAadeQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDADGeaQ 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231702  249 TLEADIVIVGVGAKPLTSLFK----GQVEEDKGGIKTDAFFKTSVPDVYAVGDVATFPL 303
Cdd:PRK06327 270 TLEVDKLIVSIGRVPNTDGLGleavGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPM 328
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
216-302 2.96e-07

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 52.47  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  216 TNKGVKIIKGTVASGFTAQPNGEVkeVQLKDGRTLEADIVIVGVGAKpltslfkGQVEE-----------DKGGIKTDAF 284
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGGDDGVI--VHLKSGKKIKADCLLYANGRT-------GNTDGlnlenagleadSRGQLKVNEN 297

                         90
                 ....*....|....*...
gi 15231702  285 FKTSVPDVYAVGDVATFP 302
Cdd:PRK05249 298 YQTAVPHIYAVGDVIGFP 315
PLN02507 PLN02507
glutathione reductase
 173-298 1.02e-06

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 50.97  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVFPEPwcMP-RLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGeVKeVQLKDGRTLE 251
Cdd:PLN02507 213 YIAVEFASIWRGMGATVDLFFRKE--LPlRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IK-VITDHGEEFV 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15231702  252 ADIVIVGVGAKPLTS---LFKGQVEEDK-GGIKTDAFFKTSVPDVYAVGDV 298
Cdd:PLN02507 289 ADVVLFATGRAPNTKrlnLEAVGVELDKaGAVKVDEYSRTNIPSIWAIGDV 339
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 173-247 1.66e-06

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: 45.66  E-value: 1.66e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231702   173 YIGLELSAVLRINNLDVTMVFPEPWCMPrLFTADIAAFYETYYTNKGVKIIKGTVASGFTAqpNGEVKEVQLKDG 247
Cdd:pfam00070   9 YIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEG--NGDGVVVVLTDG 80
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 219-300 3.81e-06

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: 48.98  E-value: 3.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 219 GVKIIKGTVASGFTAQPNGEVKEVQL---------KDGR-----------TLEADIVIVGVGAKPLTSLFKGQVE---ED 275
Cdd:COG0493 307 GVEFLFLVAPVEIIGDENGRVTGLECvrmelgepdESGRrrpvpiegsefTLPADLVILAIGQTPDPSGLEEELGlelDK 386

                        90       100
                ....*....|....*....|....*.
gi 15231702 276 KGGIKTDAF-FKTSVPDVYAVGDVAT 300
Cdd:COG0493 387 RGTIVVDEEtYQTSLPGVFAGGDAVR 412
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 248-333 7.65e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 47.87  E-value: 7.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  248 RTLEADIVIVGVGAKPLTSLFKGQVE---EDKGGIKTD-AFFKTSVPDVYAVGDVATfplkmyGDVRRVEHVDHSRKSAE 323
Cdd:PRK11749 372 FTLPADLVIKAIGQTPNPLILSTTPGlelNRWGTIIADdETGRTSLPGVFAGGDIVT------GAATVVWAVGDGKDAAE 445

                         90
                 ....*....|
gi 15231702  324 QAVKAIKAAE 333
Cdd:PRK11749 446 AIHEYLEGAA 455
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 248-304 8.26e-05

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 44.76  E-value: 8.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231702  248 RTLEADIVIVGVGAKPLTSLFKGQVEEDKGG-IKTDAFFKTSVPDVYAVGDVATFPLK 304
Cdd:PRK15317 434 HHLELEGVFVQIGLVPNTEWLKGTVELNRRGeIIVDARGATSVPGVFAAGDCTTVPYK 491
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 112-300 8.48e-05

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 44.76  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  112 VFKYQTLIIATGStvlRLTDFGVKGADsKNILYLREIDDA----DKLVEAIKAKKGGKAVVVGGG-----------YIGL 176
Cdd:PTZ00318 111 SVPYDKLVVAHGA---RPNTFNIPGVE-ERAFFLKEVNHArgirKRIVQCIERASLPTTSVEERKrllhfvvvgggPTGV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  177 ELSAVLriNNL---DVTMVFPE--PWCMPRLFTA--DIAAFYETYYTNKGVKIIKgtvASGFTAQPNGEVKEVQ-----L 244
Cdd:PTZ00318 187 EFAAEL--ADFfrdDVRNLNPElvEECKVTVLEAgsEVLGSFDQALRKYGQRRLR---RLGVDIRTKTAVKEVLdkevvL 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  245 KDGRTLEADIVI--VGVGAKPLTSLFKgqVEED-KGGIKTDAFFKTS-VPDVYAVGDVAT 300
Cdd:PTZ00318 262 KDGEVIPTGLVVwsTGVGPGPLTKQLK--VDKTsRGRISVDDHLRVKpIPNVFALGDCAA 319
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 170-299 1.21e-04

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: 44.07  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702   170 GGGYIGLELSAVLRINNLDVT-MVFPEPWcmpRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQpnGEVKEVQLKD-- 246
Cdd:TIGR01438 187 GASYVALECAGFLAGIGLDVTvMVRSILL---RGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQI--EAKVLVEFTDst 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231702   247 -GRTLEADIVIVGVGAKPLTSLFK-----GQVEEDKGGIKTDAFFKTSVPDVYAVGDVA 299
Cdd:TIGR01438 262 nGIEEEYDTVLLAIGRDACTRKLNlenvgVKINKKTGKIPADEEEQTNVPYIYAVGDIL 320
PRK07251 PRK07251
FAD-containing oxidoreductase;
174-298 1.38e-04

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 43.97  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  174 IGLELSAVLRINNLDVTMVFPEPWCMPRlFTADIAAFYETYYTNKGVKIIKGtvaSGFTAQPNGEVKEVQLKDGRTLEAD 253
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPR-EEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQVLVVTEDETYRFD 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15231702  254 IVIVGVGAKPLTS---LFKGQVE-EDKGGIKTDAFFKTSVPDVYAVGDV 298
Cdd:PRK07251 244 ALLYATGRKPNTEplgLENTDIElTERGAIKVDDYCQTSVPGVFAVGDV 292
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 249-311 3.42e-04

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 43.19  E-value: 3.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  249 TLEADIVIVGVGAKP---LTSLFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDV----ATFPLKMyGDVRR 311
Cdd:PRK12778 672 TVDVDLVIVSVGVSPnplVPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDIvrggATVILAM-GDGKR 740
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 231-297 4.79e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 42.46  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  231 FTAQP------NGEVK-----EVQLKDG---------RTLEADIVIVGVG-AKPLTSLFK-GQVEEDK-GGIK-TDAFFK 286
Cdd:PRK12810 348 FNVQTkefegeNGKVTgvkvvRTELGEGdfepvegseFVLPADLVLLAMGfTGPEAGLLAqFGVELDErGRVAaPDNAYQ 427

                         90
                 ....*....|.
gi 15231702  287 TSVPDVYAVGD 297
Cdd:PRK12810 428 TSNPKVFAAGD 438
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 173-298 8.92e-04

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 41.54  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVFPEPWCMPRLfTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGevKEVQLKDGRTLeA 252
Cdd:PRK08010 168 YIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQ--VQVHSEHAQLA-V 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15231702  253 DIVIVGVGAKPLTSLFK----GQVEEDKGGIKTDAFFKTSVPDVYAVGDV 298
Cdd:PRK08010 244 DALLIASGRQPATASLHpenaGIAVNERGAIVVDKYLHTTADNIWAMGDV 293
PTZ00058 PTZ00058
glutathione reductase; Provisional
 173-297 1.67e-03

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 40.75  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDvTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKEVQLKDGRTLEA 252
Cdd:PTZ00058 247 YIAVELINVVNRLGAE-SYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEHF 325

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15231702  253 DIVIVGVGAKPLTSLFKGQ---VEEDKGGIKTDAFFKTSVPDVYAVGD 297
Cdd:PTZ00058 326 DYVIYCVGRSPNTEDLNLKalnIKTPKGYIKVDDNQRTSVKHIYAVGD 373
Trp_halogenase pfam04820
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form ...
 208-256 1.92e-03

Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent.


Pssm-ID: 398475 [Multi-domain]  Cd Length: 457  Bit Score: 40.39  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15231702   208 AAFYETYYTNKGVKIIKGTVASGfTAQPNGEVKEVQLKDGRTLEADIVI 256
Cdd:pfam04820 160 ARFLRRNAEARGVTRVEGKVVDV-QLDADGFVTSLRLEDGREVEADLFI 207
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 173-299 2.27e-03

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 40.19  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702  173 YIGLELSAVLRINNLDVTMVFPEpwCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTaQPNGEVKeVQLKDGRTLEA 252
Cdd:PTZ00052 192 YIGLETAGFLNELGFDVTVAVRS--IPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIE-KMDDKIK-VLFSDGTTELF 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15231702  253 DIVIVGVGAKPLTSLFKGQ---VEEDKGGIKTDAFFKTSVPDVYAVGDVA 299
Cdd:PTZ00052 268 DTVLYATGRKPDIKGLNLNaigVHVNKSNKIIAPNDCTNIPNIFAVGDVV 317
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
210-296 2.39e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.23  E-value: 2.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231702 210 FYETYYT---NKGVKIIKGTVASgFTAQPNGEVKeVQLKD---GRTLE--ADIVIVGVGAKP------LTSLFKGQVEED 275
Cdd:COG1148 352 KYEEFYRrarEDGVRFIRGRVAE-IEEDEGGKLV-VTVEDtllGEPVEieADLVVLATGMVPsedneeLAKLLKLPLDQD 429

                        90       100
                ....*....|....*....|....*.
gi 15231702 276 kgGIKTDAFFK-----TSVPDVYAVG 296
Cdd:COG1148 430 --GFFLEAHPKlrpveTATDGIFLAG 453
PRK10262 PRK10262
thioredoxin reductase; Provisional
 239-298 3.00e-03

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 39.66  E-value: 3.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231702  239 VKEVQLKDG-RTLEADIVIVGVGAKPLTSLFKGQVEEDKGGIKTDAFF-----KTSVPDVYAVGDV 298
Cdd:PRK10262 223 LRDTQNSDNiESLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIhgnatQTSIPGVFAAGDV 288
PRK13984 PRK13984
putative oxidoreductase; Provisional
 245-302 8.72e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 38.59  E-value: 8.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231702  245 KDGRTLEADIVIVGVGAKPLTSLF----KGQVEEDKGGIKTDAFFKTSVPDVYAVGDVATFP 302
Cdd:PRK13984 520 SDQIIVEADMVVEAIGQAPDYSYLpeelKSKLEFVRGRILTNEYGQTSIPWLFAGGDIVHGP 581
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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