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Conserved domains on  [gi|542029077|ref|NP_001269441|]
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thioredoxin reductase 2, mitochondrial isoform 5 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TGR super family cl36907
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 39-320 4.75e-133

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.


The actual alignment was detected with superfamily member TIGR01438:

Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 387.67  E-value: 4.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 118
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  119 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 198
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  199 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 278
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 542029077  279 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 320
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGrdACT 281
 
Name Accession Description Interval E-value
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 39-320 4.75e-133

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: 387.67  E-value: 4.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 118
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  119 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 198
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  199 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 278
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 542029077  279 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 320
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGrdACT 281
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 39-316 1.65e-109

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 328.32  E-value: 1.65e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 117
Cdd:PTZ00052   5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 118 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 197
Cdd:PTZ00052  85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 198 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 277
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 542029077 278 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAI 316
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYAT 274
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 53-316 1.01e-61

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: 203.39  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 132
Cdd:COG1249   17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 133 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 212
Cdd:COG1249   87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 213 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 291
Cdd:COG1249  163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241

                        250       260
                 ....*....|....*....|....*
gi 542029077 292 LQVTWEDSttGKEDTGTFDTVLWAI 316
Cdd:COG1249  242 VTVTLEDG--GGEEAVEADKVLVAT 264
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 51-316 1.15e-41

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: 147.08  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   51 GLACAKEAAQLGRKVAVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAE 130
Cdd:pfam07992  12 GLAAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  131 AVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCgvakgGKEILLSADHIIIATGGRPRYPThIEGALEYG----- 205
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVD-----GDGETITYDRLVIATGARPRLPP-IPGVELNVgflvr 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  206 -ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 283
Cdd:pfam07992 139 tLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKE 218

                         250       260       270
                  ....*....|....*....|....*....|...
gi 542029077  284 VRRLPDGQLQVtwedstTGKEDTGTFDTVLWAI 316
Cdd:pfam07992 219 IIGDGDGVEVI------LKDGTEIDADLVVVAI 245
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
55-247 1.32e-11

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 65.19  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  55 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqN 134
Cdd:NF040477  19 AATLAKAGWRVAII---EQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 135 HVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSD 209
Cdd:NF040477  77 FLRDKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----ST 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 542029077 210 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM 247
Cdd:NF040477 150 GLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIF 187
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 124-190 2.20e-03

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 36.74  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542029077 124 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 190
Cdd:cd08704    6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
 
Name Accession Description Interval E-value
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 39-320 4.75e-133

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: 387.67  E-value: 4.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 118
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  119 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 198
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  199 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 278
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 542029077  279 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 320
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGrdACT 281
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 39-316 1.65e-109

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 328.32  E-value: 1.65e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 117
Cdd:PTZ00052   5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 118 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 197
Cdd:PTZ00052  85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 198 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 277
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 542029077 278 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAI 316
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYAT 274
PRK06116 PRK06116
glutathione reductase; Validated
 53-316 1.05e-68

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 221.57  E-value: 1.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 131
Cdd:PRK06116  18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 132 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGRPRYPThIEGAlEYGITSDDI 211
Cdd:PRK06116  88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 212 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 290
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240

                        250       260
                 ....*....|....*....|....*.
gi 542029077 291 QLQVTWEDsttGKEDtgTFDTVLWAI 316
Cdd:PRK06116 241 SLTLTLED---GETL--TVDCLIWAI 261
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 53-316 1.01e-61

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: 203.39  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 132
Cdd:COG1249   17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 133 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 212
Cdd:COG1249   87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 213 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 291
Cdd:COG1249  163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241

                        250       260
                 ....*....|....*....|....*
gi 542029077 292 LQVTWEDSttGKEDTGTFDTVLWAI 316
Cdd:COG1249  242 VTVTLEDG--GGEEAVEADKVLVAT 264
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
 53-316 1.05e-54

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: 185.04  E-value: 1.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   53 ACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 132
Cdd:TIGR01421  16 ASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  133 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGAlEYGITSDDIF 212
Cdd:TIGR01421  87 DAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPENIPGA-ELGTDSDGFF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  213 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 291
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240

                         250       260
                  ....*....|....*....|....*
gi 542029077  292 LQVTWEDSTTgkedTGTFDTVLWAI 316
Cdd:TIGR01421 241 LVIHFEDGKS----IDDVDELIWAI 261
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
 39-315 5.34e-50

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: 172.69  E-value: 5.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 118
Cdd:TIGR01424   2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  119 QpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIIIATGGRPRYPThI 198
Cdd:TIGR01424  73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-L 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  199 EGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLR 277
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 542029077  278 GCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWA 315
Cdd:TIGR01424 227 EDSITSISKDDDGRLKA-----TLSKHEEIVADVVLFA 259
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 51-316 1.15e-41

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: 147.08  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   51 GLACAKEAAQLGRKVAVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAE 130
Cdd:pfam07992  12 GLAAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  131 AVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCgvakgGKEILLSADHIIIATGGRPRYPThIEGALEYG----- 205
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVD-----GDGETITYDRLVIATGARPRLPP-IPGVELNVgflvr 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  206 -ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 283
Cdd:pfam07992 139 tLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKE 218

                         250       260       270
                  ....*....|....*....|....*....|...
gi 542029077  284 VRRLPDGQLQVtwedstTGKEDTGTFDTVLWAI 316
Cdd:pfam07992 219 IIGDGDGVEVI------LKDGTEIDADLVVVAI 245
PLN02507 PLN02507
glutathione reductase
 55-274 5.05e-41

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 149.58  E-value: 5.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  55 AKEAAQLGRKVAVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQ 133
Cdd:PLN02507  41 ARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 134 NHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEGAlEYGITSDDIFW 213
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN-IPGK-ELAITSDEALS 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542029077 214 LKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTR 274
Cdd:PLN02507 199 LEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLEGRGIN 260
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 54-316 2.00e-36

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: 136.62  E-value: 2.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   54 CAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 132
Cdd:TIGR01350  16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  133 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRY-PTHIEGALEYGITSDDI 211
Cdd:TIGR01350  85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  212 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 289
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242

                         250       260
                  ....*....|....*....|....*..
gi 542029077  290 gqlQVTWEDStTGKEDTGTFDTVLWAI 316
Cdd:TIGR01350 243 ---QVTYENK-GGETETLTGEKVLVAV 265
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 58-316 9.36e-35

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: 132.40  E-value: 9.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   58 AAQL-GRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 135
Cdd:TIGR01423  22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  136 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIIIATGGRPRYPThIEGaLEYGITS 208
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  209 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 284
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257

                         250       260       270
                  ....*....|....*....|....*....|..
gi 542029077  285 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAI 316
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAI 284
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 38-316 3.77e-33

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 127.57  E-value: 3.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  38 RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEv 117
Cdd:PRK06416   3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 118 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 197
Cdd:PRK06416  73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 198 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRF 275
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKI 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 542029077 276 LRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAI 316
Cdd:PRK06416 231 KTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAV 268
PRK06370 PRK06370
FAD-containing oxidoreductase;
53-316 4.97e-33

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 127.24  E-value: 4.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 128
Cdd:PRK06370  19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 129 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIIIATGGRPRYPtHIEGALEYG- 205
Cdd:PRK06370  90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 206 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 283
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 542029077 284 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAI 316
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAV 267
PLN02546 PLN02546
glutathione reductase
 81-315 1.48e-31

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 124.22  E-value: 1.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  81 GLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKAS 160
Cdd:PLN02546 122 GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGK 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 161 FVDEHTvcgVAKGGKeiLLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI 240
Cdd:PLN02546 202 IVDPHT---VDVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGL 274

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542029077 241 GLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWA 315
Cdd:PLN02546 275 KSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSL-----KTNKGTVEGFSHVMFA 345
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 38-316 6.52e-31

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 121.44  E-value: 6.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  38 RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV 117
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 118 AQPVPhDWRKMAEAVQNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGR-PRYP 195
Cdd:PRK06292  73 DGPKI-DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNT---VEVNGERI--EAKNIVIATGSRvPPIP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 196 ThIEGALEYGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHg 272
Cdd:PRK06292 147 G-VWLILGDRLlTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE- 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 542029077 273 TRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTGTFDTVLWAI 316
Cdd:PRK06292 224 FKIKLGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVAT 264
PTZ00058 PTZ00058
glutathione reductase; Provisional
 39-316 4.85e-29

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 117.02  E-value: 4.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  39 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 118
Cdd:PTZ00058  48 VYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 119 QPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI------------------- 177
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqld 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 178 ---LLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPL 253
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLL 273

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542029077 254 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAI 316
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCV 332
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 53-295 5.39e-29

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: 115.98  E-value: 5.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   53 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 132
Cdd:TIGR02053  14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  133 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIIIATGGRPRYPtHIEGA 201
Cdd:TIGR02053  83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  202 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 279
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228

                         250
                  ....*....|....*.
gi 542029077  280 APSRVRRLPDGQLQVT 295
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV 244
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
55-315 1.54e-25

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 106.39  E-value: 1.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  55 AKEAAQLGRKVAVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 131
Cdd:PRK05249  21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 132 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 211
Cdd:PRK05249  92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 212 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 290
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248

                        250       260
                 ....*....|....*....|....*
gi 542029077 291 QLqVTWEDsttGKEDTGtfDTVLWA 315
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYA 267
PRK07846 PRK07846
mycothione reductase; Reviewed
 62-301 4.27e-22

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 96.18  E-value: 4.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  62 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 140
Cdd:PRK07846  22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 141 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 216
Cdd:PRK07846  91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 217 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 293
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240


                 ....*...
gi 542029077 294 VTWEDSTT 301
Cdd:PRK07846 241 LRLDDGST 248
mycothione_red TIGR03452
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ...
 62-306 3.68e-19

mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.


Pssm-ID: 132493 [Multi-domain]  Cd Length: 452  Bit Score: 87.89  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077   62 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvksln 140
Cdd:TIGR03452  23 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV-------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  141 WGHRVQL------------QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHI-EGALEYgIT 207
Cdd:TIGR03452  84 FGDRIDPiaaggedyrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIaDSGVRY-HT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  208 SDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRR 286
Cdd:TIGR03452 159 NEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQ 237

                         250       260
                  ....*....|....*....|
gi 542029077  287 LPDGqLQVTWEDSTTGKEDT 306
Cdd:TIGR03452 238 DGDG-VTLTLDDGSTVTADV 256
PRK13748 PRK13748
putative mercuric reductase; Provisional
 53-250 4.89e-19

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 87.90  E-value: 4.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 132
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 133 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEG 200
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 542029077 201 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS 250
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARS 302
PRK07251 PRK07251
FAD-containing oxidoreductase;
55-315 8.05e-16

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 77.87  E-value: 8.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  55 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 134
Cdd:PRK07251  19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 135 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIF 212
Cdd:PRK07251  77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 213 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 291
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230

                        250       260
                 ....*....|....*....|....
gi 542029077 292 LQVTWEDSTTgkedtgTFDTVLWA 315
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYA 248
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 163-301 2.10e-15

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: 75.62  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 163 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 233
Cdd:COG0446   65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542029077 234 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDSTT 301
Cdd:COG0446  140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTDGEE 206
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 220-295 2.55e-15

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: 69.93  E-value: 2.55e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542029077  220 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 295
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 37-316 3.24e-14

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 73.04  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  37 QRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGW 115
Cdd:PRK06327   2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 116 EVAQpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEIlLSADHIIIATGGRP 192
Cdd:PRK06327  80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETV-ITAKHVIIATGSEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 193 RyptHIEGAL---EYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEH 267
Cdd:PRK06327 158 R---HLPGVPfdnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKA 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 542029077 268 MASHGTRFLRGCAPSRVRRLPDGqLQVTWEDStTGKEDTGTFDTVLWAI 316
Cdd:PRK06327 234 FTKQGLDIHLGVKIGEIKTGGKG-VSVAYTDA-DGEAQTLEVDKLIVSI 280
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
55-247 1.32e-11

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 65.19  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  55 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqN 134
Cdd:NF040477  19 AATLAKAGWRVAII---EQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 135 HVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSD 209
Cdd:NF040477  77 FLRDKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----ST 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 542029077 210 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM 247
Cdd:NF040477 150 GLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIF 187
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
 53-241 6.31e-11

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 63.39  E-value: 6.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  53 ACAKEAAQLGRKVAVVDYVEPSpqgtrwgLGGTCVNVGCIPKKLMHQAA------------LLGGLIQDAPNYGWE---- 116
Cdd:PTZ00153 130 AAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpve 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 117 ----VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHII 185
Cdd:PTZ00153 203 rnqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNII 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 542029077 186 IATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIG 241
Cdd:PTZ00153 280 IATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALG 335
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 83-247 1.04e-09

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 59.26  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  83 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 161
Cdd:PRK08010  40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 162 VDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 236
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176

                        170
                 ....*....|.
gi 542029077 237 LTGIGLDTTIM 247
Cdd:PRK08010 177 FANFGSKVTIL 187
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
163-291 3.62e-09

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 57.46  E-value: 3.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 163 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKT-LVVGASYVALECAG 235
Cdd:COG1251   85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRvVVIGGGLIGLEAAA 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542029077 236 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR--------RLPDGQ 291
Cdd:COG1251  160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEgddrvtgvRLADGE 225
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 58-301 4.23e-09

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 57.56  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  58 AAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 137
Cdd:PRK07845  20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 138 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---I 206
Cdd:PRK07845  89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 207 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 284
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244

                        250
                 ....*....|....*..
gi 542029077 285 RRLPDGQLqVTWEDSTT 301
Cdd:PRK07845 245 ERTGDGVV-VTLTDGRT 260
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 138-272 2.54e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 45.80  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 138 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 214
Cdd:PRK09564  72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542029077 215 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHG 272
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENG 205
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
57-316 3.35e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 42.03  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077  57 EAAQLGRKVAVVDYVEPSPQGTRWglggTCV-NVGCIPKKLMhQAALLGGLIQDAPNYGwevaqpvphdwrkmAEAVQNH 135
Cdd:COG0492   18 YAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS-GPELAERLREQAERFG--------------AEILLEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 136 VKSLnwghrvqlqDRKVKYFNIKASfvdehtvcgvakGGKEIllSADHIIIATGGRPRYPThIEGALE-------YGITS 208
Cdd:COG0492   79 VTSV---------DKDDGPFRVTTD------------DGTEY--EAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATC 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 209 DDIFWlkesPGKT-LVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrr 286
Cdd:COG0492  135 DGFFF----RGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI-- 203

                        250       260       270
                 ....*....|....*....|....*....|.
gi 542029077 287 LPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAI 316
Cdd:COG0492  204 EGDGRVEgVTLKNVKTGEEKELEVDGVFVAI 234
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 124-190 2.20e-03

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 36.74  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542029077 124 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 190
Cdd:cd08704    6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
163-315 6.12e-03

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 38.19  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 163 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 227
Cdd:COG1252   84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542029077 228 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 293
Cdd:COG1252  159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233

                        170       180
                 ....*....|....*....|..
gi 542029077 294 VTWEDSTTGKedtgtFDTVLWA 315
Cdd:COG1252  234 VTLEDGEEIP-----ADTVIWA 250
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 220-272 9.20e-03

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 37.84  E-value: 9.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 542029077 220 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHG 272
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKRE 203
 
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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