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Conserved domains on  [gi|1153887943|ref|WP_078407187|]
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NAD(P)/FAD-dependent oxidoreductase [Elizabethkingia anophelis]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11422994)

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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0050660|GO:0016491
PubMed:  33684359

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-290 7.91e-57

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


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 185.32  E-value: 7.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPCNR--QTPYSHNFL-THDGKTPQEISQMAKVQVKQYPtVQFYEGEA 83
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQlaTTKEIENYPgFPEGISGPELAERLREQAERFG-AEILLEEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  84 VKGVKTDTGFIITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRNEKTGIIANGDRAVHMTSL 163
Cdd:COG0492    80 TSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 164 INNLTKDLTILTSGPaDFDAEQ--RAKLERH-GIPVI-EKKITEIeHQNGHIDNIVFEDG-----TKMNFKAVYAAIPFL 234
Cdd:COG0492   160 LTKFASKVTLIHRRD-ELRASKilVERLRANpKIEVLwNTEVTEI-EGDGRVEGVTLKNVktgeeKELEVDGVFVAIGLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1153887943 235 QNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS-MMRSVALAVASGNLAG 290
Cdd:COG0492   238 PNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDyKYRQAATAAGEGAIAA 294
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-290 7.91e-57

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 185.32  E-value: 7.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPCNR--QTPYSHNFL-THDGKTPQEISQMAKVQVKQYPtVQFYEGEA 83
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQlaTTKEIENYPgFPEGISGPELAERLREQAERFG-AEILLEEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  84 VKGVKTDTGFIITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRNEKTGIIANGDRAVHMTSL 163
Cdd:COG0492    80 TSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 164 INNLTKDLTILTSGPaDFDAEQ--RAKLERH-GIPVI-EKKITEIeHQNGHIDNIVFEDG-----TKMNFKAVYAAIPFL 234
Cdd:COG0492   160 LTKFASKVTLIHRRD-ELRASKilVERLRANpKIEVLwNTEVTEI-EGDGRVEGVTLKNVktgeeKELEVDGVFVAIGLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1153887943 235 QNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS-MMRSVALAVASGNLAG 290
Cdd:COG0492   238 PNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDyKYRQAATAAGEGAIAA 294
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-286 6.51e-36

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: 130.90  E-value: 6.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPC-NRQTPYSHNFL-----THDGKTPQEI-SQMAKVQVKQYPTVQFY 79
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLgaaeaPEIASLWADLyKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  80 EGEAVKGVKTDTGFIITTN----SGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRN--EKTGIIAN 153
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEElvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 154 GDRAVHMTSLINNLTKDLTILTSGP-------ADFDAEQRAKLERHGIPVI-EKKITEIEhQNGHIDNIVFEDGTKMNFK 225
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDrllrafdEEISAALEKALEKNGVEVRlGTSVKEII-GDGDGVEVILKDGTEIDAD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153887943 226 AVYAAIPFLQNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSM-MRSVALAVASG 286
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGgPELAQNAVAQG 301
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 6-273 3.24e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 60.56  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   6 VFDVIIIGGSYAGLSSAMSLGR-SLRNVLIID--GGkpcnrQ---TPYSHNFLT---HDGktPQEISQMAKvQVKQYPtV 76
Cdd:PRK15317  211 PYDVLVVGGGPAGAAAAIYAARkGIRTGIVAErfGG-----QvldTMGIENFISvpeTEG--PKLAAALEE-HVKEYD-V 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  77 QFYEGEAVKGVKTDTGFI-ITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRNEKTGIIANGD 155
Cdd:PRK15317  282 DIMNLQRASKLEPAAGLIeVELANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGN 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 156 RAVHMTSLINNLTKDLTILtsgpaDFDAEQRA------KLERHG-IPVI-EKKITEIEHQNGHIDNIVFEDGTKMNFKAV 227
Cdd:PRK15317  362 SGVEAAIDLAGIVKHVTVL-----EFAPELKAdqvlqdKLRSLPnVTIItNAQTTEVTGDGDKVTGLTYKDRTTGEEHHL 436

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1153887943 228 YAAIPFLQ-----NCDIAEQLgCELTEQGYIQVDSMQKTNVPGVFACGDST 273
Cdd:PRK15317  437 ELEGVFVQiglvpNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCT 486
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 181-286 2.72e-07

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: 51.51  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 181 FDAEQRAKLER----HGIPVI-EKKITEIEHQNGHIDNIVFEDGTKMNFKAVYAAI---PFLQNCDIaEQLGCELTEQGY 252
Cdd:TIGR01423 229 FDSTLRKELTKqlraNGINIMtNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIgrvPRTQTLQL-DKVGVELTKKGA 307

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1153887943 253 IQVDSMQKTNVPGVFACGDSTSMMRSVALAVASG 286
Cdd:TIGR01423 308 IQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEG 341
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-290 7.91e-57

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 185.32  E-value: 7.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPCNR--QTPYSHNFL-THDGKTPQEISQMAKVQVKQYPtVQFYEGEA 83
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQlaTTKEIENYPgFPEGISGPELAERLREQAERFG-AEILLEEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  84 VKGVKTDTGFIITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRNEKTGIIANGDRAVHMTSL 163
Cdd:COG0492    80 TSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 164 INNLTKDLTILTSGPaDFDAEQ--RAKLERH-GIPVI-EKKITEIeHQNGHIDNIVFEDG-----TKMNFKAVYAAIPFL 234
Cdd:COG0492   160 LTKFASKVTLIHRRD-ELRASKilVERLRANpKIEVLwNTEVTEI-EGDGRVEGVTLKNVktgeeKELEVDGVFVAIGLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1153887943 235 QNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS-MMRSVALAVASGNLAG 290
Cdd:COG0492   238 PNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDyKYRQAATAAGEGAIAA 294
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-286 6.51e-36

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: 130.90  E-value: 6.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPC-NRQTPYSHNFL-----THDGKTPQEI-SQMAKVQVKQYPTVQFY 79
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLgaaeaPEIASLWADLyKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  80 EGEAVKGVKTDTGFIITTN----SGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRN--EKTGIIAN 153
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEElvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 154 GDRAVHMTSLINNLTKDLTILTSGP-------ADFDAEQRAKLERHGIPVI-EKKITEIEhQNGHIDNIVFEDGTKMNFK 225
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDrllrafdEEISAALEKALEKNGVEVRlGTSVKEII-GDGDGVEVILKDGTEIDAD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153887943 226 AVYAAIPFLQNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSM-MRSVALAVASG 286
Cdd:pfam07992 240 LVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGgPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 95-274 1.58e-19

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: 86.79  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  95 ITTNSGEEFSSRKLILAAGIKDIMPDIKGfsesWGISVIHcpYCHGYEY-RNEKTGIIA-NGDRAV-HMTSLI-----NN 166
Cdd:COG0446    69 VTLRDGETLSYDKLVLATGARPRPPPIPG----LDLPGVF--TLRTLDDaDALREALKEfKGKRAVvIGGGPIglelaEA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 167 LTK---DLTI-------LTSGPADFDAEQRAKLERHGIPVI-EKKITEIEHQNGHIdnIVFEDGTKMNFKAVYAAIPFLQ 235
Cdd:COG0446   143 LRKrglKVTLveraprlLGVLDPEMAALLEEELREHGVELRlGETVVAIDGDDKVA--VTLTDGEEIPADLVVVAPGVRP 220

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1153887943 236 NCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS 274
Cdd:COG0446   221 NTELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAE 259
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
8-276 4.58e-17

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 80.56  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   8 DVIIIGGSYAGLSSAMSLGRSLRN---VLIIDggkpcnrQTPYsHNFLT--HD----GKTPQEISqmakvqvkqYPT--- 75
Cdd:COG1252     3 RIVIVGGGFAGLEAARRLRKKLGGdaeVTLID-------PNPY-HLFQPllPEvaagTLSPDDIA---------IPLrel 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  76 -----VQFYEGEaVKGVKTDTGfIITTNSGEEFSSRKLILAAGIKDIMPDIKGFSEsWGISVihCPYCHGYEYRN----- 145
Cdd:COG1252    66 lrragVRFIQGE-VTGIDPEAR-TVTLADGRTLSYDYLVIATGSVTNFFGIPGLAE-HALPL--KTLEDALALRErllaa 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 146 -EK----------------TGI--IANGDRAVHMTSLINNLTKD---LTILTSGP---ADFDAEQRAK----LERHGIPV 196
Cdd:COG1252   141 fERaerrrlltivvvgggpTGVelAGELAELLRKLLRYPGIDPDkvrITLVEAGPrilPGLGEKLSEAaekeLEKRGVEV 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 197 I-EKKITEIEHqnghiDNIVFEDGTKMNFKAVYAAIPFlQNCDIAEQLGCELTEQGYIQVDS-MQKTNVPGVFACGDSTS 274
Cdd:COG1252   221 HtGTRVTEVDA-----DGVTLEDGEEIPADTVIWAAGV-KAPPLLADLGLPTDRRGRVLVDPtLQVPGHPNVFAIGDCAA 294


                  ..
gi 1153887943 275 MM 276
Cdd:COG1252   295 VP 296
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
17-270 1.53e-12

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 66.48  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  17 AGLSSAMSLGRS-LRNVLIIDGGK--------PCNRQ--TPYSH---------NFLTHDGKTPQEIS-------QMAK-- 67
Cdd:pfam13738   2 AGIGCAIALKKAgLEDYLILEKGNignsfyryPTHMTffSPSFTsngfgipdlNAISPGTSPAFTFNrehpsgnEYAEyl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  68 ---VQVKQYPtVQFYEgeAVKGV-KTDTGFIITTnSGEEFSSRKLILAAGIKDImPDIKGFSEswgISVIHCPYCHGYEY 143
Cdd:pfam13738  82 rrvADHFELP-INLFE--EVTSVkKEDDGFVVTT-SKGTYQARYVIIATGEFDF-PNKLGVPE---LPKHYSYVKDFHPY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 144 RNEKTGIIANGDRAVHMTSLINNLTKDLTILTSGP------ADF------DAEQR-AKLERHGIPVIE--KKITEIEHQN 208
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSewedrdSDPsyslspDTLNRlEELVKNGKIKAHfnAEVKEITEVD 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1153887943 209 GHIDnIVFEDGTKM--NFKAVYaAIPFLQNCDIAEQLGCELTEQGYIQVDS-MQKTNVPGVFACG 270
Cdd:pfam13738 234 VSYK-VHTEDGRKVtsNDDPIL-ATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-290 2.98e-12

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: 66.65  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAM---SLGRSlrnVLIIDGGKP---C-NR----------------QTPYSHNF-LTHDGKTP--- 59
Cdd:COG1249     4 YDLVVIGAGPGGYVAAIraaQLGLK---VALVEKGRLggtClNVgcipskallhaaevahEARHAAEFgISAGAPSVdwa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  60 -------QEISQMAKVQVKQY--PTVQFYEGEA-VKGVKTdtgfiITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWG 129
Cdd:COG1249    81 almarkdKVVDRLRGGVEELLkkNGVDVIRGRArFVDPHT-----VEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 130 IS---------------VIhcpychGyeyrnekTGIIAngdraVHMTSLINNLTKDLTILTSGP---ADFDAEQRA---- 187
Cdd:COG1249   156 LTsdealeleelpkslvVI------G-------GGYIG-----LEFAQIFARLGSEVTLVERGDrllPGEDPEISEalek 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 188 KLERHGIPVIEK-KITEIEHQNGHIdNIVFEDGTK---MNFKAVYAAI---PFLQNCDIaEQLGCELTEQGYIQVDSMQK 260
Cdd:COG1249   218 ALEKEGIDILTGaKVTSVEKTGDGV-TVTLEDGGGeeaVEADKVLVATgrrPNTDGLGL-EAAGVELDERGGIKVDEYLR 295

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1153887943 261 TNVPGVFACGDSTS--MMRSVALA---VASGNLAG 290
Cdd:COG1249   296 TSVPGIYAIGDVTGgpQLAHVASAegrVAAENILG 330
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
8-295 3.75e-11

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 63.24  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   8 DVIIIGGSYAGLSSAmslgRSLRN------VLII--DGGKPCNRqTPYSHNFLthdGKTPQEisQMAKVQVKQY--PTVQ 77
Cdd:COG1251     3 RIVIIGAGMAGVRAA----EELRKldpdgeITVIgaEPHPPYNR-PPLSKVLA---GETDEE--DLLLRPADFYeeNGID 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  78 FYEGEAVKGVKTDTGfIITTNSGEEFSSRKLILAAGIKDIMPDIKGfseswgisvIHCPYCHGY----EYRNEKTgIIAN 153
Cdd:COG1251    73 LRLGTRVTAIDRAAR-TVTLADGETLPYDKLVLATGSRPRVPPIPG---------ADLPGVFTLrtldDADALRA-ALAP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 154 GDRAVhmtsLI----------NNLTK---DLTILTSGP------ADFDAEQ--RAKLERHGIPVI-EKKITEIEhQNGHI 211
Cdd:COG1251   142 GKRVV----VIgggligleaaAALRKrglEVTVVERAPrllprqLDEEAGAllQRLLEALGVEVRlGTGVTEIE-GDDRV 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 212 DNIVFEDGTKMNFKAVYAAI---PflqNCDIAEQLGCElTEQGyIQVDSMQKTNVPGVFACGDSTS---------MMRSV 279
Cdd:COG1251   217 TGVRLADGEELPADLVVVAIgvrP---NTELARAAGLA-VDRG-IVVDDYLRTSDPDIYAAGDCAEhpgpvygrrVLELV 291

                         330
                  ....*....|....*.
gi 1153887943 280 ALAVASGNLAGAmlNM 295
Cdd:COG1251   292 APAYEQARVAAA--NL 305
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 6-273 3.24e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 60.56  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   6 VFDVIIIGGSYAGLSSAMSLGR-SLRNVLIID--GGkpcnrQ---TPYSHNFLT---HDGktPQEISQMAKvQVKQYPtV 76
Cdd:PRK15317  211 PYDVLVVGGGPAGAAAAIYAARkGIRTGIVAErfGG-----QvldTMGIENFISvpeTEG--PKLAAALEE-HVKEYD-V 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  77 QFYEGEAVKGVKTDTGFI-ITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESWGISVIHCPYCHGYEYRNEKTGIIANGD 155
Cdd:PRK15317  282 DIMNLQRASKLEPAAGLIeVELANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGN 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 156 RAVHMTSLINNLTKDLTILtsgpaDFDAEQRA------KLERHG-IPVI-EKKITEIEHQNGHIDNIVFEDGTKMNFKAV 227
Cdd:PRK15317  362 SGVEAAIDLAGIVKHVTVL-----EFAPELKAdqvlqdKLRSLPnVTIItNAQTTEVTGDGDKVTGLTYKDRTTGEEHHL 436

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1153887943 228 YAAIPFLQ-----NCDIAEQLgCELTEQGYIQVDSMQKTNVPGVFACGDST 273
Cdd:PRK15317  437 ELEGVFVQiglvpNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCT 486
PRK06116 PRK06116
glutathione reductase; Validated
 100-273 2.66e-09

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 57.47  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 100 GEEFSSRKLILAAGIKDIMPDIKGfSEswgisviHCPYCHGYEYRNE---KTGIIANGDRAVHMTSLINNLTKDLTILTS 176
Cdd:PRK06116  127 GERYTADHILIATGGRPSIPDIPG-AE-------YGITSDGFFALEElpkRVAVVGAGYIAVEFAGVLNGLGSETHLFVR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 177 GPA---DFDAEQRAKL----ERHGIPVI-EKKITEIEHQNGHIDNIVFEDGTKMNFKAVYAAI---PFLQNCDIaEQLGC 245
Cdd:PRK06116  199 GDAplrGFDPDIRETLveemEKKGIRLHtNAVPKAVEKNADGSLTLTLEDGETLTVDCLIWAIgrePNTDGLGL-ENAGV 277

                         170       180
                  ....*....|....*....|....*...
gi 1153887943 246 ELTEQGYIQVDSMQKTNVPGVFACGDST 273
Cdd:PRK06116  278 KLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
PTZ00058 PTZ00058
glutathione reductase; Provisional
 98-271 5.57e-09

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 56.93  E-value: 5.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  98 NSGEEFSSRKLILAAGIKDIMPDIKGFS---ESWGISVIHCPychgyeyrnEKTGIIANGDRAVHMTSLINNLTKDLTIL 174
Cdd:PTZ00058  196 DDGQVIEGKNILIAVGNKPIFPDVKGKEftiSSDDFFKIKEA---------KRIGIAGSGYIAVELINVVNRLGAESYIF 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 175 TSG-------PADFDAEQRAKLERHGIPVIE----KKITEIEHQNghIDNIVFEDGTKMNFKAVYAAIPFLQNcdiAEQL 243
Cdd:PTZ00058  267 ARGnrllrkfDETIINELENDMKKNNINIIThanvEEIEKVKEKN--LTIYLSDGRKYEHFDYVIYCVGRSPN---TEDL 341

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1153887943 244 GCE----LTEQGYIQVDSMQKTNVPGVFACGD 271
Cdd:PTZ00058  342 NLKalniKTPKGYIKVDDNQRTSVKHIYAVGD 373
PRK07251 PRK07251
FAD-containing oxidoreductase;
101-271 1.89e-08

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 55.14  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 101 EEFSSRKLILAAGIKDIMPDIKGFSESWGisVIHCPYCHGYEYRNEKTGIIANGDRAVHMTSLINNLTKDLTILTSGPAD 180
Cdd:PRK07251  115 IELTAETIVINTGAVSNVLPIPGLADSKH--VYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 181 FDAE-----QRAK--LERHGIP-VIEKKITEIEHQNGHIdnIVFEDGTKMNFKAVYAAI-------PF-LQNCDIaeqlg 244
Cdd:PRK07251  193 LPREepsvaALAKqyMEEDGITfLLNAHTTEVKNDGDQV--LVVTEDETYRFDALLYATgrkpntePLgLENTDI----- 265

                         170       180
                  ....*....|....*....|....*..
gi 1153887943 245 cELTEQGYIQVDSMQKTNVPGVFACGD 271
Cdd:PRK07251  266 -ELTERGAIKVDDYCQTSVPGVFAVGD 291
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 7-154 2.28e-07

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 51.79  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPC------NR------QTP---YSHNFLTHDGKTPqeiSQMAKVQVK 71
Cdd:COG2072     7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVggtwrdNRypglrlDTPshlYSLPFFPNWSDDP---DFPTGDEIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  72 QY-----------PTVQFyeGEAVKGVKTDT---GFIITTNSGEEFSSRKLILAAGIKDI--MPDIKGfSESWGISVIH- 134
Cdd:COG2072    84 AYleayadkfglrRPIRF--GTEVTSARWDEadgRWTVTTDDGETLTARFVVVATGPLSRpkIPDIPG-LEDFAGEQLHs 160

                         170       180
                  ....*....|....*....|
gi 1153887943 135 CPYCHGYEYRNEKTGIIANG 154
Cdd:COG2072   161 ADWRNPVDLAGKRVLVVGTG 180
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 7-271 2.49e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 51.72  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKP---CNR-----------------QTPYSHNFLTHDGKTPQEISQ-M 65
Cdd:PRK06292    4 YDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLggtCLNvgcipskaliaaaeafhEAKHAEEFGIHADGPKIDFKKvM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  66 AKVQ-------------VKQYPTVQFYEGEAVkgvktdtgfIITTNS----GEEFSSRKLILAAGIKdiMPDIKGFSESW 128
Cdd:PRK06292   84 ARVRrerdrfvggvvegLEKKPKIDKIKGTAR---------FVDPNTvevnGERIEAKNIVIATGSR--VPPIPGVWLIL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 129 GISVI---------HCPychgyeyrnEKTGIIANGDRAVHMTSLINNLTKDLTILTSGP---ADFDAEQRAKLERH---G 193
Cdd:PRK06292  153 GDRLLtsddafeldKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDrilPLEDPEVSKQAQKIlskE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 194 IPVIEK-KITEIEHQNGHIDNIVFEDGTKM--NFKAVYAAI---PFLQNCDIaEQLGCELTEQGYIQVDSMQKTNVPGVF 267
Cdd:PRK06292  224 FKIKLGaKVTSVEKSGDEKVEELEKGGKTEtiEADYVLVATgrrPNTDGLGL-ENTGIELDERGRPVVDEHTQTSVPGIY 302


                  ....
gi 1153887943 268 ACGD 271
Cdd:PRK06292  303 AAGD 306
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 181-286 2.72e-07

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: 51.51  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 181 FDAEQRAKLER----HGIPVI-EKKITEIEHQNGHIDNIVFEDGTKMNFKAVYAAI---PFLQNCDIaEQLGCELTEQGY 252
Cdd:TIGR01423 229 FDSTLRKELTKqlraNGINIMtNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIgrvPRTQTLQL-DKVGVELTKKGA 307

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1153887943 253 IQVDSMQKTNVPGVFACGDSTSMMRSVALAVASG 286
Cdd:TIGR01423 308 IQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEG 341
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 7-288 3.44e-07

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: 51.39  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPcnrqTPYSHNF-----LTHDGKTPQEISQMAKVQVKQYPTVQFYEG 81
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTP----TPLGTRWgiggtCVNVGCIPKKLMHQAALLGQALKDSRNYGW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  82 EAVKGVKTDTGFIITT-----------------------------------------NSGEEF-SSRKLILAAGIKDIMP 119
Cdd:TIGR01438  79 KVEETVKHDWKRLVEAvqnhigslnwgyrvalrekkvkyenayaefvdkhrikatnkKGKEKIySAERFLIATGERPRYP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 120 DIKGFSEsWGIS---VIHCPYCHGyeyrneKTGIIANGDRAVHMTSLINNLTKDLT-----ILTSGpadFDAEQRAK--- 188
Cdd:TIGR01438 159 GIPGAKE-LCITsddLFSLPYCPG------KTLVVGASYVALECAGFLAGIGLDVTvmvrsILLRG---FDQDCANKvge 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 189 -LERHGIPVIE----KKITEIEhqnghiDNIVFEDGTKMN-----FKAVYAAIPFLQNCDIA--EQLGCELTEQ-GYIQV 255
Cdd:TIGR01438 229 hMEEHGVKFKRqfvpIKVEQIE------AKVLVEFTDSTNgieeeYDTVLLAIGRDACTRKLnlENVGVKINKKtGKIPA 302

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1153887943 256 DSMQKTNVPGVFACGDSTSMMRSVA-LAVASGNL 288
Cdd:TIGR01438 303 DEEEQTNVPYIYAVGDILEDKPELTpVAIQAGRL 336
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 241-280 8.35e-07

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 49.86  E-value: 8.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1153887943 241 EQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS--MMRSVA 280
Cdd:PRK07845  282 EEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGvlPLASVA 323
PRK07846 PRK07846
mycothione reductase; Reviewed
 74-280 1.53e-06

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 49.18  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  74 PTVQFYEGEAV-KGVKTdtgfiITTNSGEEFSSRKLILAAGIKDIMPDIKGFSESwgisvihcPYchgyeYRN------- 145
Cdd:PRK07846  102 PNIDVYRGHARfIGPKT-----LRTGDGEEITADQVVIAAGSRPVIPPVIADSGV--------RY-----HTSdtimrlp 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 146 ---EKTGIIANGDRAVHMTSLINNLTKDLTILTSGPadfdaeqraKLERHGIPVIEKKITEI---------------EHQ 207
Cdd:PRK07846  164 elpESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSG---------RLLRHLDDDISERFTELaskrwdvrlgrnvvgVSQ 234

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1153887943 208 NGHIDNIVFEDGTKMNFKAVYAAIPFLQNCDI--AEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS--MMRSVA 280
Cdd:PRK07846  235 DGSGVTLRLDDGSTVEADVLLVATGRVPNGDLldAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSpyQLKHVA 311
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 226-286 2.01e-06

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 48.59  E-value: 2.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153887943 226 AVYAAIPFLQNCD-IAEQLGCELTEQGYIQVDSM-QKTNVPGVFACGDSTSMMRSVALAVASG 286
Cdd:COG0493   362 LVILAIGQTPDPSgLEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEG 424
HI0933_like pfam03486
HI0933-like protein;
7-134 2.05e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 48.73  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   7 FDVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKP------------CN---RQTPYShNFLTHDGK------------TP 59
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKlgrkilisgggrCNvtnLSEEPD-NFLSRYPGnpkflksalsrfTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  60 QEISQMAK---VQVKQ------YPT-------------------VQFYEGEAVKGVKTDTG--FIITTNsGEEFSSRKLI 109
Cdd:pfam03486  80 WDFIAFFEslgVPLKEedhgrlFPDsdkasdivdallnelkelgVKIRLRTRVLSVEKDDDgrFRVKTG-GEELEADSLV 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1153887943 110 LAAGIKDiMP----DIKGFS--ESWGISVIH 134
Cdd:pfam03486 159 LATGGLS-WPktgsTGFGYPlaEQFGHTIIP 188
PLN02507 PLN02507
glutathione reductase
 76-286 3.48e-06

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 48.27  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  76 VQFYEGEAvKGVKTDTgFIITTNSGEE--FSSRKLILAAGIKDIMPDIKG----FSESWGISVIHCPychgyeyrnEKTG 149
Cdd:PLN02507  139 VKLYEGEG-KIVGPNE-VEVTQLDGTKlrYTAKHILIATGSRAQRPNIPGkelaITSDEALSLEELP---------KRAV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 150 IIANGDRAVHMTSLINNL--TKDLTILTSGP-ADFDAEQRA----KLERHGIPV-IEKKITEIEHQNGHIdNIVFEDGTK 221
Cdd:PLN02507  208 VLGGGYIAVEFASIWRGMgaTVDLFFRKELPlRGFDDEMRAvvarNLEGRGINLhPRTNLTQLTKTEGGI-KVITDHGEE 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153887943 222 MNFKAVYAAI---PFLQNCDIaEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSMMRSVALAVASG 286
Cdd:PLN02507  287 FVADVVLFATgraPNTKRLNL-EAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEG 353
PRK13748 PRK13748
putative mercuric reductase; Provisional
 241-295 3.59e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 48.22  E-value: 3.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1153887943 241 EQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSMMRSVALAVASGNLAGamLNM 295
Cdd:PRK13748  373 DAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAA--INM 425
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 146-290 6.39e-06

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 47.23  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 146 EKTGIIANGDRAVHMTSLINNLTKDLTILTSGP-----ADFDAEQRA--KLERHGIPVIEK-KITEIEhQNGHIDNIVFE 217
Cdd:PRK06327  184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEALPaflaaADEQVAKEAakAFTKQGLDIHLGvKIGEIK-TGGKGVSVAYT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 218 DGTKMNFKAVY----AAIPFLQNCD--IAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTS--MMRSVA----LAVAS 285
Cdd:PRK06327  263 DADGEAQTLEVdkliVSIGRVPNTDglGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRgpMLAHKAeeegVAVAE 342


                  ....*
gi 1153887943 286 gNLAG 290
Cdd:PRK06327  343 -RIAG 346
PRK10262 PRK10262
thioredoxin reductase; Provisional
 93-292 2.53e-05

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 45.05  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  93 FIITTNSGEeFSSRKLILAAGIKDI---MPDIKGFSeswGISVIHCPYCHGYEYRNEKTGIIANGDRAVHMTSLINNLTK 169
Cdd:PRK10262   95 FRLTGDSGE-YTCDALIIATGASARylgLPSEEAFK---GRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIAS 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 170 DLTILTSGPAdFDAEQ------RAKLERHGIPV-IEKKITEIEHQNGHIDNIVFEDGTK------MNFKAVYAAIPFLQN 236
Cdd:PRK10262  171 EVHLIHRRDG-FRAEKilikrlMDKVENGNIILhTNRTLEEVTGDQMGVTGVRLRDTQNsdniesLDVAGLFVAIGHSPN 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153887943 237 CDIAEqlGCELTEQGYIQVDS-----MQKTNVPGVFACGDSTSMMRSVALAVASGNLAGAM 292
Cdd:PRK10262  250 TAIFE--GQLELENGYIKVQSgihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAAL 308
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 189-281 4.54e-05

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 44.77  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 189 LERHGIPVieKKITEIEHQNGHIdnIVFEDGTKMNFKAVYAAIPFLQNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFA 268
Cdd:PRK13512  199 LDKREIPY--RLNEEIDAINGNE--VTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYA 274

                          90
                  ....*....|....
gi 1153887943 269 CGDS-TSMMRSVAL 281
Cdd:PRK13512  275 IGDIiTSHYRHVDL 288
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 9-291 5.71e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 44.26  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   9 VIIIGGSYAGLSSAMSLGRSLRNVLIIDGGK-------PCNrqTPY-SHNFLTHDG----KTPQE-ISQMAKVQVKQypt 75
Cdd:PRK09564    3 IIIIGGTAAGMSAAAKAKRLNKELEITVYEKtdivsfgACG--LPYfVGGFFDDPNtmiaRTPEEfIKSGIDVKTEH--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943  76 vqfyegEAVK-GVKTDTGFIITTNSGEEFSSR--KLILAAGIKDIMPDIKGFSESwgisvihcpycHGYEYRNEKTG--- 149
Cdd:PRK09564   78 ------EVVKvDAKNKTITVKNLKTGSIFNDTydKLMIATGARPIIPPIKNINLE-----------NVYTLKSMEDGlal 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 150 -------------IIANGDRAVHMTSLINNLTKDLTILTSG----PADFDAEQRAKLERHgipvIEKKITEIeHQNGHID 212
Cdd:PRK09564  141 kellkdeeiknivIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrilPDSFDKEITDVMEEE----LRENGVEL-HLNEFVK 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943 213 NIVFEDGT------KMNFKA--VYAAIPFLQNCDIAEQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSMMRSV----- 279
Cdd:PRK09564  216 SLIGEDKVegvvtdKGEYEAdvVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVsnknv 295

                         330       340
                  ....*....|....*....|..
gi 1153887943 280 --ALA--------VASGNLAGA 291
Cdd:PRK09564  296 yvPLAttanklgrMVGENLAGR 317
PRK06370 PRK06370
FAD-containing oxidoreductase;
241-271 2.68e-04

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 42.11  E-value: 2.68e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1153887943 241 EQLGCELTEQGYIQVDSMQKTNVPGVFACGD 271
Cdd:PRK06370  279 EAAGVETDARGYIKVDDQLRTTNPGIYAAGD 309
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 246-291 1.04e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 40.55  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1153887943 246 ELTEQGYIQVDSMQ-KTNVPGVFACGDSTSMMRSVALAVASGNLAGA 291
Cdd:PRK11749  399 ELNRWGTIIADDETgRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAE 445
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 238-271 1.52e-03

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 39.76  E-value: 1.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1153887943 238 DIAEQLGCELTEQGYIQVDSMQ-KTNVPGVFACGD 271
Cdd:PRK12810  404 GLLAQFGVELDERGRVAAPDNAyQTSNPKVFAAGD 438
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 241-289 2.29e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 39.20  E-value: 2.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1153887943 241 EQLGCELTEQGYIQVDSMQKTNVPGVFACGDSTSMMRSVALAVASGNLA 289
Cdd:PRK12770  293 ECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRA 341
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
9-115 2.86e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 38.74  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153887943   9 VIIIGGSYAGLSSAMSLGRSLRNVLIIDggkPCNRQTPyshnflthdGKTPQEISQMAKVQVKQYpTVQFYEGEAVKGV- 87
Cdd:PRK04965  144 VLVVGGGLIGTELAMDLCRAGKAVTLVD---NAASLLA---------SLMPPEVSSRLQHRLTEM-GVHLLLKSQLQGLe 210

                          90       100
                  ....*....|....*....|....*...
gi 1153887943  88 KTDTGFIITTNSGEEFSSRKLILAAGIK 115
Cdd:PRK04965  211 KTDSGIRATLDSGRSIEVDAVIAAAGLR 238
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 244-300 2.87e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 39.34  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1153887943 244 GCELTEQGYIQVDSMQKTNVPGVFACGDSTSMMRSVALAVASGNLAGAMLNMELVSE 300
Cdd:PRK12778  696 GLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
1-50 6.02e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 37.96  E-value: 6.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1153887943   1 MKTDIVFDVIIIGGSYAGLSSAMSLGRSLRNVLIIDggkpcnRQTPYSHN 50
Cdd:PRK07494    2 LMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVA------PEPPYADL 45
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 8-48 6.31e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 38.04  E-value: 6.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1153887943   8 DVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPCNRQTPYS 48
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWS 41
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 8-45 9.28e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 37.38  E-value: 9.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1153887943   8 DVIIIGGSYAGLSSAMSLGRSLRNVLIIDGGKPCNRQT 45
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
 
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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