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Conserved domains on  [gi|51476567|emb|CAH18266|]
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hypothetical protein [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 ...
 7-288 3.04e-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: 386.90  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567     7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 86
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    87 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPtHI 166
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   167 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 246
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 51476567   247 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 288
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 ...
 7-288 3.04e-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: 386.90  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567     7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 86
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    87 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPtHI 166
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   167 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 246
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 51476567   247 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 288
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGrdACT 281
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 7-284 2.77e-109

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 326.40  E-value: 2.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 85
Cdd:PTZ00052   5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   86 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRYPTH 165
Cdd:PTZ00052  85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  166 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 245
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 51476567  246 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAI 284
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYAT 274
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 21-284 1.29e-60

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: 199.54  E-value: 1.29e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  21 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 100
Cdd:COG1249  17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIVIATGGRPRYPTHIEGALEYGITSDDIF 180
Cdd:COG1249  87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 259
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241

                       250       260
                ....*....|....*....|....*
gi 51476567 260 LQVTWEDSttGKEDTGTFDTVLWAI 284
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVAT 264
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 21-284 1.21e-42

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: 148.62  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    21 ACAKEAAQLGRKVSVVDyvepspqgtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 100
Cdd:pfam07992  14 AAALTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIVIATGGRPRYPThIEGALEYG------I 174
Cdd:pfam07992  67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   175 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 253
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220

                         250       260       270
                  ....*....|....*....|....*....|.
gi 51476567   254 RLPDGQLQVtwedstTGKEDTGTFDTVLWAI 284
Cdd:pfam07992 221 GDGDGVEVI------LKDGTEIDADLVVVAI 245
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
26-215 1.12e-11

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 64.80  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   26 AAQLGRKVSVVDYVEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqNHVK 105
Cdd:NF040477  19 AATLAKAGWRVAIIEQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-GFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  106 SLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRYP-----THIEGALEygitSDDIF 180
Cdd:NF040477  80 DKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----STGLL 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 51476567  181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM 215
Cdd:NF040477 153 NLTQLPARLGILGGGYIGVEFASMFARFGSKVTIF 187
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 92-158 1.87e-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: 1.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51476567  92 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIVIATGG 158
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 ...
 7-288 3.04e-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: 386.90  E-value: 3.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567     7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 86
Cdd:TIGR01438   2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    87 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPtHI 166
Cdd:TIGR01438  82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   167 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 246
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 51476567   247 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIA--PCI 288
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGrdACT 281
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 7-284 2.77e-109

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 326.40  E-value: 2.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 85
Cdd:PTZ00052   5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   86 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRYPTH 165
Cdd:PTZ00052  85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  166 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 245
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 51476567  246 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAI 284
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYAT 274
PRK06116 PRK06116
glutathione reductase; Validated
 21-297 3.01e-68

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 219.26  E-value: 3.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   21 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 99
Cdd:PRK06116  18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  100 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIVIATGGRPRYPThIEGAlEYGITSDDI 179
Cdd:PRK06116  88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  180 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 258
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 51476567  259 QLQVTWEDsttGKEDtgTFDTVLWAIapcisARLPTTVG 297
Cdd:PRK06116 241 SLTLTLED---GETL--TVDCLIWAI-----GREPNTDG 269
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 21-284 1.29e-60

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: 199.54  E-value: 1.29e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  21 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 100
Cdd:COG1249  17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIVIATGGRPRYPTHIEGALEYGITSDDIF 180
Cdd:COG1249  87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 259
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241

                       250       260
                ....*....|....*....|....*
gi 51476567 260 LQVTWEDSttGKEDTGTFDTVLWAI 284
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVAT 264
gluta_reduc_1 TIGR01421
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ...
 21-297 6.97e-55

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: 184.66  E-value: 6.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    21 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 100
Cdd:TIGR01421  16 ASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIVIATGGRPRYPTHIEGAlEYGITSDDIF 180
Cdd:TIGR01421  87 DAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPENIPGA-ELGTDSDGFF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 259
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 51476567   260 LQVTWEDSTTgkedTGTFDTVLWAIapcisARLPTTVG 297
Cdd:TIGR01421 241 LVIHFEDGKS----IDDVDELIWAI-----GRKPNTKG 269
gluta_reduc_2 TIGR01424
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ...
 7-297 2.70e-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: 172.30  E-value: 2.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567     7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 86
Cdd:TIGR01424   2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    87 QpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIVIATGGRPRYPThI 166
Cdd:TIGR01424  73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-L 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   167 EGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLR 245
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 51476567   246 GCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWAiapciSARLPTTVG 297
Cdd:TIGR01424 227 EDSITSISKDDDGRLKA-----TLSKHEEIVADVVLFA-----TGRSPNTNG 268
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 21-284 1.21e-42

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: 148.62  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    21 ACAKEAAQLGRKVSVVDyvepspqgtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 100
Cdd:pfam07992  14 AAALTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIVIATGGRPRYPThIEGALEYG------I 174
Cdd:pfam07992  67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   175 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 253
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220

                         250       260       270
                  ....*....|....*....|....*....|.
gi 51476567   254 RLPDGQLQVtwedstTGKEDTGTFDTVLWAI 284
Cdd:pfam07992 221 GDGDGVEVI------LKDGTEIDADLVVVAI 245
PLN02507 PLN02507
glutathione reductase
 23-295 5.50e-41

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 148.43  E-value: 5.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   23 AKEAAQLGRKVSVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQ 101
Cdd:PLN02507  41 ARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  102 NHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPThIEGAlEYGITSDDIFW 181
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN-IPGK-ELAITSDEALS 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  182 LKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqL 260
Cdd:PLN02507 199 LEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-I 277

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 51476567  261 QVTwedSTTGKEDTGtfDTVLWAiapciSARLPTT 295
Cdd:PLN02507 278 KVI---TDHGEEFVA--DVVLFA-----TGRAPNT 302
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 22-284 2.19e-35

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: 132.77  E-value: 2.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    22 CAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 100
Cdd:TIGR01350  16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   101 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRY-PTHIEGALEYGITSDDI 179
Cdd:TIGR01350  85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   180 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 257
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242

                         250       260
                  ....*....|....*....|....*..
gi 51476567   258 gqlQVTWEDStTGKEDTGTFDTVLWAI 284
Cdd:TIGR01350 243 ---QVTYENK-GGETETLTGEKVLVAV 265
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 26-295 5.89e-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: 132.02  E-value: 5.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    26 AAQL-GRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 103
Cdd:TIGR01423  22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   104 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIVIATGGRPRYPThIEGaLEYGITS 176
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   177 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 252
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 51476567   253 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAIapcisARLPTT 295
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAI-----GRVPRT 290
PRK06370 PRK06370
FAD-containing oxidoreductase;
21-284 8.20e-33

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 125.70  E-value: 8.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   21 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 96
Cdd:PRK06370  19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   97 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIVIATGGRPRYPtHIEGALEYG- 173
Cdd:PRK06370  90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  174 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 251
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 51476567  252 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAI 284
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAV 267
PLN02546 PLN02546
glutathione reductase
 49-295 3.87e-32

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 124.99  E-value: 3.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   49 GLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKAS 128
Cdd:PLN02546 122 GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGK 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  129 FVDEHTvcgVAKGGKeiLLSADHIVIATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI 208
Cdd:PLN02546 202 IVDPHT---VDVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGL 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  209 GLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWAiapc 287
Cdd:PLN02546 275 KSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSL-----KTNKGTVEGFSHVMFA---- 345


                 ....*...
gi 51476567  288 iSARLPTT 295
Cdd:PLN02546 346 -TGRKPNT 352
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 6-284 5.19e-32

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 123.72  E-value: 5.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    6 RDYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEv 85
Cdd:PRK06416   3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   86 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRYPTH 165
Cdd:PRK06416  73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  166 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRF 243
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKI 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 51476567  244 LRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAI 284
Cdd:PRK06416 231 KTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAV 268
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 6-284 6.11e-30

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 117.97  E-value: 6.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    6 RDYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV 85
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   86 AQPVPhDWRKMAEAVQNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIVIATGGR-PRYP 163
Cdd:PRK06292  73 DGPKI-DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNT---VEVNGERI--EAKNIVIATGSRvPPIP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  164 ThIEGALEYGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHg 240
Cdd:PRK06292 147 G-VWLILGDRLlTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE- 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 51476567  241 TRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTGTFDTVLWAI 284
Cdd:PRK06292 224 FKIKLGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVAT 264
PTZ00058 PTZ00058
glutathione reductase; Provisional
 7-284 8.50e-29

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 115.48  E-value: 8.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    7 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 86
Cdd:PTZ00058  48 VYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   87 QPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI------------------- 145
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqld 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  146 ---LLSADHIVIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPL 221
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLL 273

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51476567  222 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAI 284
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCV 332
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 21-263 2.64e-28

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: 113.29  E-value: 2.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    21 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 100
Cdd:TIGR02053  14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   101 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIVIATGGRPRYPtHIEGA 169
Cdd:TIGR02053  83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   170 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 247
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228

                         250
                  ....*....|....*.
gi 51476567   248 APSRVRRLPDGQLQVT 263
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV 244
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
23-283 6.85e-25

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 103.70  E-value: 6.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   23 AKEAAQLGRKVSVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 99
Cdd:PRK05249  21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  100 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPTHIEGALEYGITSDDI 179
Cdd:PRK05249  92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  180 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 258
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248

                        250       260
                 ....*....|....*....|....*
gi 51476567  259 QLqVTWEDsttGKEDTGtfDTVLWA 283
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYA 267
PRK07846 PRK07846
mycothione reductase; Reviewed
 30-269 3.01e-22

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 96.18  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   30 GRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 108
Cdd:PRK07846  22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  109 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIVIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 184
Cdd:PRK07846  91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  185 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 261
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240


                 ....*...
gi 51476567  262 VTWEDSTT 269
Cdd:PRK07846 241 LRLDDGST 248
PRK13748 PRK13748
putative mercuric reductase; Provisional
 21-218 1.31e-19

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 89.06  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   21 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 100
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  101 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIVIATGGRPRYPThIEG 168
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51476567  169 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS 218
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARS 302
mycothione_red TIGR03452
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ...
 44-274 1.83e-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: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    44 QGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvkslnWGHRVQL------- 115
Cdd:TIGR03452  31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV--------FGDRIDPiaagged 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   116 -----QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIVIATGGRPRYPTHI-EGALEYgITSDDIFWLKESPGKT 189
Cdd:TIGR03452  98 yrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIaDSGVRY-HTNEDIMRLPELPESL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   190 LVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDST 268
Cdd:TIGR03452 173 VIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQDGDG-VTLTLDDGS 250


                  ....*.
gi 51476567   269 TGKEDT 274
Cdd:TIGR03452 251 TVTADV 256
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 131-269 1.03e-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: 76.00  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 131 DEHTVcgVAKGGKEIllSADHIVIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 201
Cdd:COG0446  65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51476567 202 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDSTT 269
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTDGEE 206
PRK07251 PRK07251
FAD-containing oxidoreductase;
23-297 1.08e-15

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 77.10  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   23 AKEAAQLGRKVSVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 102
Cdd:PRK07251  19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  103 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIVIATGGRPRYPThIEGALE--YGITSDDIF 180
Cdd:PRK07251  77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 259
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 51476567  260 LQVTWEDSTTgkedtgTFDTVLWAiapciSARLPTTVG 297
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYA-----TGRKPNTEP 257
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 188-263 2.48e-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: 69.54  E-value: 2.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51476567   188 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 263
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 5-297 2.37e-13

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 69.95  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567    5 QRDYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGW 83
Cdd:PRK06327   2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   84 EVAQpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEIlLSADHIVIATGGRP 160
Cdd:PRK06327  80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETV-ITAKHVIIATGSEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  161 RyptHIEGAL---EYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEH 235
Cdd:PRK06327 158 R---HLPGVPfdnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKA 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51476567  236 MASHGTRFLRGCAPSRVRRLPDGqLQVTWEDStTGKEDTGTFDTVLWAIapcisARLPTTVG 297
Cdd:PRK06327 234 FTKQGLDIHLGVKIGEIKTGGKG-VSVAYTDA-DGEAQTLEVDKLIVSI-----GRVPNTDG 288
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
26-215 1.12e-11

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 64.80  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   26 AAQLGRKVSVVDYVEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqNHVK 105
Cdd:NF040477  19 AATLAKAGWRVAIIEQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-GFLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  106 SLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIVIATGGRPRYP-----THIEGALEygitSDDIF 180
Cdd:NF040477  80 DKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----STGLL 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 51476567  181 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM 215
Cdd:NF040477 153 NLTQLPARLGILGGGYIGVEFASMFARFGSKVTIF 187
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
 21-209 2.54e-10

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 61.08  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   21 ACAKEAAQLGRKVSVVDYVEPSpqgtrwgLGGTCVNVGCIPKKLMHQAA------------LLGGLIQDAPNYGWE---- 84
Cdd:PTZ00153 130 AAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpve 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   85 ----VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHIV 153
Cdd:PTZ00153 203 rnqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNII 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 51476567  154 IATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIG 209
Cdd:PTZ00153 280 IATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALG 335
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
131-259 9.34e-10

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 59.00  E-value: 9.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 131 DEHTVcgVAKGGKEIllSADHIVIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKT-LVVGASYVALECAG 203
Cdd:COG1251  85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRvVVIGGGLIGLEAAA 159

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51476567 204 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR--------RLPDGQ 259
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEgddrvtgvRLADGE 225
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 51-215 9.79e-10

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 58.87  E-value: 9.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   51 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 129
Cdd:PRK08010  40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  130 VDEHTVcGVAKGGKEILLSADHIVIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 204
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176

                        170
                 ....*....|.
gi 51476567  205 LTGIGLDTTIM 215
Cdd:PRK08010 177 FANFGSKVTIL 187
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 26-276 1.63e-09

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 58.33  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567   26 AAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 105
Cdd:PRK07845  20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  106 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIVIATGGRPRYpthIEGALEYG---I 174
Cdd:PRK07845  89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  175 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 252
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244

                        250       260
                 ....*....|....*....|....
gi 51476567  253 RRLPDGQLqVTWEDsttGKEDTGT 276
Cdd:PRK07845 245 ERTGDGVV-VTLTD---GRTVEGS 264
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 106-240 1.10e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 46.57  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567  106 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIVIATGGRPRYPTHIEGALE--YGITS-DDIFWL 182
Cdd:PRK09564  72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51476567  183 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHG 240
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENG 205
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
138-284 7.83e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 40.49  E-value: 7.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 138 VAKGGKEILLSADHIVIATGGRPRYPThIEGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIG 209
Cdd:COG0492  90 RVTTDDGTEYEAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFA 164

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51476567 210 LDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrrLPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAI 284
Cdd:COG0492 165 SKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAI 234
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
131-283 1.84e-03

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 39.35  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 131 DEHTVcgVAKGGKEIllSADHIVIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 195
Cdd:COG1252  84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476567 196 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 261
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233

                       170       180
                ....*....|....*....|..
gi 51476567 262 VTWEDSTTGKedtgtFDTVLWA 283
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWA 250
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 92-158 1.87e-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: 1.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51476567  92 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIVIATGG 158
Cdd:cd08704   6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 188-240 7.79e-03

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 37.84  E-value: 7.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 51476567  188 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHG 240
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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