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Conserved domains on  [gi|19115108|ref|NP_594196|]
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NADH dehydrogenase [Schizosaccharomyces pombe]

Protein Classification

NAD(P)H-binding domain containing protein( domain architecture ID 1001497)

NAD(P)H-binding domain containing protein similar to the mitochondrial internal alternative NAD(P)H-ubiquinone oxidoreductase A, an NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH, but does not translocate protons across the inner mitochondrial membrane

EC:  1.6.-.-
Gene Ontology:  GO:0003959|GO:0016491
PubMed:  8805537

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00318 super family cl33177
NADH dehydrogenase-like protein; Provisional
 91-551 3.78e-133

NADH dehydrogenase-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00318:

Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 394.13  E-value: 3.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   91 KKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKScyVKFYEAECTDV 170
Cdd:PTZ00318  10 KPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLP--NRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  171 DADKKVI--HIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPA 248
Cdd:PTZ00318  88 DFEEKRVkcGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  249 ETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRT 328
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  329 NTALKKVTAEnihvEVKNPDGskqeEVIPYGLLVWAGGNRARPLTKKLmegSEEQNNRRGLVVDEYLKLKGYKDIFALGD 408
Cdd:PTZ00318 248 KTAVKEVLDK----EVVLKDG----EVIPTGLVVWSTGVGPGPLTKQL---KVDKTSRGRISVDDHLRVKPIPNVFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  409 CT---HTAYAPTAQVASQQGAYLGQLFNKLGSLNfekpsedrhialgdemdsstlislanekhASTKvflPFKYSHQGSL 485
Cdd:PTZ00318 317 CAaneERPLPTLAQVASQQGVYLAKEFNNELKGK-----------------------------PMSK---PFVYRSLGSL 364

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115108  486 AYVGHEKAIADIEVpwfgkqLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL 551
Cdd:PTZ00318 365 AYLGNYSAIVQLGA------FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 91-551 3.78e-133

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 394.13  E-value: 3.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   91 KKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKScyVKFYEAECTDV 170
Cdd:PTZ00318  10 KPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLP--NRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  171 DADKKVI--HIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPA 248
Cdd:PTZ00318  88 DFEEKRVkcGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  249 ETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRT 328
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  329 NTALKKVTAEnihvEVKNPDGskqeEVIPYGLLVWAGGNRARPLTKKLmegSEEQNNRRGLVVDEYLKLKGYKDIFALGD 408
Cdd:PTZ00318 248 KTAVKEVLDK----EVVLKDG----EVIPTGLVVWSTGVGPGPLTKQL---KVDKTSRGRISVDDHLRVKPIPNVFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  409 CT---HTAYAPTAQVASQQGAYLGQLFNKLGSLNfekpsedrhialgdemdsstlislanekhASTKvflPFKYSHQGSL 485
Cdd:PTZ00318 317 CAaneERPLPTLAQVASQQGVYLAKEFNNELKGK-----------------------------PMSK---PFVYRSLGSL 364

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115108  486 AYVGHEKAIADIEVpwfgkqLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL 551
Cdd:PTZ00318 365 AYLGNYSAIVQLGA------FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
91-536 2.92e-97

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 300.51  E-value: 2.92e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  91 KKTLVVLGAGWGATSILRTIDTSL---FNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKScyVKFYEAEC 167
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 168 TDVDADKKVIhikkTTTDGvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAqfkdlp 247
Cdd:COG1252  79 TGIDPEARTV----TLADG----RTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 248 aeTRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKswYPEL-ADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKI 326
Cdd:COG1252 145 --ERRRLLTIVVVGGGPTGVELAGELAELLRKLLR--YPGIdPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEV 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 327 RTNTALKKVTAENIHVEvknpDGskqeEVIPYGLLVWAGGNRARPLTKklmeGSEEQNNRRG-LVVDEYLKLKGYKDIFA 405
Cdd:COG1252 221 HTGTRVTEVDADGVTLE----DG----EEIPADTVIWAAGVKAPPLLA----DLGLPTDRRGrVLVDPTLQVPGHPNVFA 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 406 LGDCTH------TAYAPTAQVASQQGAYLGQlfnklgslnfekpsedrhialgdemdssTLISLANEKHAStkvflPFKY 479
Cdd:COG1252 289 IGDCAAvpdpdgKPVPKTAQAAVQQAKVLAK----------------------------NIAALLRGKPLK-----PFRY 335

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19115108 480 SHQGSLAYVGHEKAIADievpWFGkqLHASGALAFYFWRSVYLSELYSLRNRTNVTL 536
Cdd:COG1252 336 RDKGCLASLGRGAAVAD----VGG--LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 94-425 7.77e-45

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: 160.18  E-value: 7.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108    94 LVVLGAGWGATSILRTIDTSLFNVIVVS-PRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEA------- 165
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRKEEVVKKLNNgievllg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   166 -ECTDVDADKKVIHIKKTTTDGvdlEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIW-DAQKIRarilhcleqaqF 243
Cdd:pfam07992  83 tEVVSIDPGAKKVVLEELVDGD---GETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLdSAEALR-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   244 KDLPAetrrryvHTVVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSH 323
Cdd:pfam07992 149 KLLPK-------RVVVVGGGYIGVELAAALAKLGKE--------------VTLIEALDRLLRAFDEEISAALEKALEKNG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   324 IKIRTNTALKKVTAENIHVEVKNPDGskqeEVIPYGLLVWAGGnrARPLTKKLMEGSEEQNNRRGLVVDEYLKLKgYKDI 403
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVILKDG----TEIDADLVVVAIG--RRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGI 280

                         330       340
                  ....*....|....*....|..
gi 19115108   404 FALGDCTHTAYApTAQVASQQG 425
Cdd:pfam07992 281 YAAGDCRVGGPE-LAQNAVAQG 301
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
 160-416 5.85e-13

pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.


Pssm-ID: 274465  Cd Length: 364  Bit Score: 70.31  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   160 VKFYEAECTDVDADKKVIHIKKTttdgvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIwdaqkirarilhcle 239
Cdd:TIGR03169  69 ARLILDRAIGLDLAAKQVICAGR--------PPIAYDVLSIDIGSTPALPDVPGFAEHAIPAKPL--------------- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   240 qAQFKDLPAETRRRY-----VHTVVVGGGPTGMEFAGEMADFIEDDLKSwyPEladdfaVTLVEALPSVLPMFSAKLRDY 314
Cdd:TIGR03169 126 -GQFAQRWQRFLERAkpqqpPRIAVIGGGAAGVELALAMAHRLRQLGRN--AE------VTLIDRGNVLLPGHNARVRRR 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   315 TQSLFDSSHIKIRTNTALKKVTAENIHVEvknpDGskqeEVIPYGLLVWAGGNRARPLTKKlmegSEEQNNRRGLV-VDE 393
Cdd:TIGR03169 197 LERALQERGVTLHLGATVAEVTADAVRLE----DG----QTLPADFTFWATGARPPGWLAE----SGLALDEDGFIrVGP 264

                         250       260
                  ....*....|....*....|...
gi 19115108   394 YLKLKGYKDIFALGDCTHTAYAP 416
Cdd:TIGR03169 265 TLQSLSHPDIFAAGDCAHLVHAP 287
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 91-551 3.78e-133

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 394.13  E-value: 3.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   91 KKTLVVLGAGWGATSILRTIDTSLFNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKScyVKFYEAECTDV 170
Cdd:PTZ00318  10 KPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLP--NRYLRAVVYDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  171 DADKKVI--HIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAQFKDLPA 248
Cdd:PTZ00318  88 DFEEKRVkcGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  249 ETRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKSWYPELADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRT 328
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  329 NTALKKVTAEnihvEVKNPDGskqeEVIPYGLLVWAGGNRARPLTKKLmegSEEQNNRRGLVVDEYLKLKGYKDIFALGD 408
Cdd:PTZ00318 248 KTAVKEVLDK----EVVLKDG----EVIPTGLVVWSTGVGPGPLTKQL---KVDKTSRGRISVDDHLRVKPIPNVFALGD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  409 CT---HTAYAPTAQVASQQGAYLGQLFNKLGSLNfekpsedrhialgdemdsstlislanekhASTKvflPFKYSHQGSL 485
Cdd:PTZ00318 317 CAaneERPLPTLAQVASQQGVYLAKEFNNELKGK-----------------------------PMSK---PFVYRSLGSL 364

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115108  486 AYVGHEKAIADIEVpwfgkqLHASGALAFYFWRSVYLSELYSLRNRTNVTLDWIRVKLFGRDISSL 551
Cdd:PTZ00318 365 AYLGNYSAIVQLGA------FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
91-536 2.92e-97

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 300.51  E-value: 2.92e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  91 KKTLVVLGAGWGATSILRTIDTSL---FNVIVVSPRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKScyVKFYEAEC 167
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 168 TDVDADKKVIhikkTTTDGvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIWDAQKIRARILHCLEQAqfkdlp 247
Cdd:COG1252  79 TGIDPEARTV----TLADG----RTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 248 aeTRRRYVHTVVVGGGPTGMEFAGEMADFIEDDLKswYPEL-ADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKI 326
Cdd:COG1252 145 --ERRRLLTIVVVGGGPTGVELAGELAELLRKLLR--YPGIdPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEV 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 327 RTNTALKKVTAENIHVEvknpDGskqeEVIPYGLLVWAGGNRARPLTKklmeGSEEQNNRRG-LVVDEYLKLKGYKDIFA 405
Cdd:COG1252 221 HTGTRVTEVDADGVTLE----DG----EEIPADTVIWAAGVKAPPLLA----DLGLPTDRRGrVLVDPTLQVPGHPNVFA 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 406 LGDCTH------TAYAPTAQVASQQGAYLGQlfnklgslnfekpsedrhialgdemdssTLISLANEKHAStkvflPFKY 479
Cdd:COG1252 289 IGDCAAvpdpdgKPVPKTAQAAVQQAKVLAK----------------------------NIAALLRGKPLK-----PFRY 335

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19115108 480 SHQGSLAYVGHEKAIADievpWFGkqLHASGALAFYFWRSVYLSELYSLRNRTNVTL 536
Cdd:COG1252 336 RDKGCLASLGRGAAVAD----VGG--LKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 94-425 7.77e-45

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: 160.18  E-value: 7.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108    94 LVVLGAGWGATSILRTIDTSLFNVIVVS-PRNYFLFTSLLPSTATGSVHTRSIVQPIRYMLRHKSCYVKFYEA------- 165
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRKEEVVKKLNNgievllg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   166 -ECTDVDADKKVIHIKKTTTDGvdlEQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIW-DAQKIRarilhcleqaqF 243
Cdd:pfam07992  83 tEVVSIDPGAKKVVLEELVDGD---GETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLdSAEALR-----------L 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   244 KDLPAetrrryvHTVVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSH 323
Cdd:pfam07992 149 KLLPK-------RVVVVGGGYIGVELAAALAKLGKE--------------VTLIEALDRLLRAFDEEISAALEKALEKNG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   324 IKIRTNTALKKVTAENIHVEVKNPDGskqeEVIPYGLLVWAGGnrARPLTKKLMEGSEEQNNRRGLVVDEYLKLKgYKDI 403
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVILKDG----TEIDADLVVVAIG--RRPNTELLEAAGLELDERGGIVVDEYLRTS-VPGI 280

                         330       340
                  ....*....|....*....|..
gi 19115108   404 FALGDCTHTAYApTAQVASQQG 425
Cdd:pfam07992 281 YAAGDCRVGGPE-LAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 164-430 8.21e-31

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: 122.23  E-value: 8.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 164 EAECTDVDADKKVIhikkTTTDGvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCF-LKEIWDAQKIRARIlhcleqaq 242
Cdd:COG0446  56 GTEVTAIDPEAKTV----TLRDG----ETLSYDKLVLATGARPRPPPIPGLDLPGVFtLRTLDDADALREAL-------- 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 243 fKDLPAEtrrryvHTVVVGGGPTGMEfageMAD-FIEDDLKswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDS 321
Cdd:COG0446 120 -KEFKGK------RAVVIGGGPIGLE----LAEaLRKRGLK-----------VTLVERAPRLLGVLDPEMAALLEEELRE 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 322 SHIKIRTNTALKKVTAENiHVEVKNPDGskqeEVIPYGLLVWAGGnrARPLTkKLMEGSE-EQNNRRGLVVDEYLKLkGY 400
Cdd:COG0446 178 HGVELRLGETVVAIDGDD-KVAVTLTDG----EEIPADLVVVAPG--VRPNT-ELAKDAGlALGERGWIKVDETLQT-SD 248

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 19115108 401 KDIFALGDCT--------HTAYAPTAQVASQQGAYLGQ 430
Cdd:COG0446 249 PDVYAAGDCAevphpvtgKTVYIPLASAANKQGRVAAE 286
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
168-410 6.89e-18

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 85.96  E-value: 6.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 168 TDVDADKKVIhikkTTTDGvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCF-LKEIWDAQKIRARilhcLEQAQfkdl 246
Cdd:COG1251  80 TAIDRAARTV----TLADG----ETLPYDKLVLATGSRPRVPPIPGADLPGVFtLRTLDDADALRAA----LAPGK---- 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 247 paetrrryvHTVVVGGGPTGMEFAGEMADFieddlkswypeladDFAVTLVEALPSVLP-MFSAKLRDYTQSLFDSSHIK 325
Cdd:COG1251 144 ---------RVVVIGGGLIGLEAAAALRKR--------------GLEVTVVERAPRLLPrQLDEEAGALLQRLLEALGVE 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 326 IRTNTALKKVTAENIHVEVKNPDGskqeEVIPYGLLVWAGGnrARPLTkKLMEGSE-EQNnrRGLVVDEYLKlKGYKDIF 404
Cdd:COG1251 201 VRLGTGVTEIEGDDRVTGVRLADG----EELPADLVVVAIG--VRPNT-ELARAAGlAVD--RGIVVDDYLR-TSDPDIY 270


                ....*.
gi 19115108 405 ALGDCT 410
Cdd:COG1251 271 AAGDCA 276
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 190-429 1.97e-17

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: 84.75  E-value: 1.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 190 EQEIKYDYLVCSHGAETQTFNIPGIAEygcflKEIWDAqkirarilhclEQA-QFKDLPAetrrryvHTVVVGGGPTGME 268
Cdd:COG1249 126 GETLTADHIVIATGSRPRVPPIPGLDE-----VRVLTS-----------DEAlELEELPK-------SLVVIGGGYIGLE 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 269 FAGEMADF-IEddlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNP 347
Cdd:COG1249 183 FAQIFARLgSE---------------VTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLE 247

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 348 DGsKQEEVIPYGLLVWAGGnRaRPLTKKLmeGSEEQ----NNRRGLVVDEYLKLkGYKDIFALGDCTHTayAPTAQVASQ 423
Cdd:COG1249 248 DG-GGEEAVEADKVLVATG-R-RPNTDGL--GLEAAgvelDERGGIKVDEYLRT-SVPGIYAIGDVTGG--PQLAHVASA 319


                ....*.
gi 19115108 424 QGAYLG 429
Cdd:COG1249 320 EGRVAA 325
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
 160-416 5.85e-13

pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.


Pssm-ID: 274465  Cd Length: 364  Bit Score: 70.31  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   160 VKFYEAECTDVDADKKVIHIKKTttdgvdleQEIKYDYLVCSHGAETQTFNIPGIAEYGCFLKEIwdaqkirarilhcle 239
Cdd:TIGR03169  69 ARLILDRAIGLDLAAKQVICAGR--------PPIAYDVLSIDIGSTPALPDVPGFAEHAIPAKPL--------------- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   240 qAQFKDLPAETRRRY-----VHTVVVGGGPTGMEFAGEMADFIEDDLKSwyPEladdfaVTLVEALPSVLPMFSAKLRDY 314
Cdd:TIGR03169 126 -GQFAQRWQRFLERAkpqqpPRIAVIGGGAAGVELALAMAHRLRQLGRN--AE------VTLIDRGNVLLPGHNARVRRR 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   315 TQSLFDSSHIKIRTNTALKKVTAENIHVEvknpDGskqeEVIPYGLLVWAGGNRARPLTKKlmegSEEQNNRRGLV-VDE 393
Cdd:TIGR03169 197 LERALQERGVTLHLGATVAEVTADAVRLE----DG----QTLPADFTFWATGARPPGWLAE----SGLALDEDGFIrVGP 264

                         250       260
                  ....*....|....*....|...
gi 19115108   394 YLKLKGYKDIFALGDCTHTAYAP 416
Cdd:TIGR03169 265 TLQSLSHPDIFAAGDCAHLVHAP 287
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 258-425 9.40e-13

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 70.17  E-value: 9.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  258 VVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTA 337
Cdd:PRK06416 176 VVIGGGYIGVEFASAYASLGAE--------------VTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  338 ENIHVEVKNPDGSKQEEVIPYGLLVWAGgnRaRPLTKKLmeGSEEQN---NRRGLVVDEYLKlKGYKDIFALGDCthTAY 414
Cdd:PRK06416 242 TDDGVTVTLEDGGKEETLEADYVLVAVG--R-RPNTENL--GLEELGvktDRGFIEVDEQLR-TNVPNIYAIGDI--VGG 313

                        170
                 ....*....|.
gi 19115108  415 APTAQVASQQG 425
Cdd:PRK06416 314 PMLAHKASAEG 324
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 258-425 3.02e-11

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: 65.74  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   258 VVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTA 337
Cdd:TIGR01350 174 VIIGGGVIGIEFASIFASLGSK--------------VTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   338 ENIHVEVKNpDGSKQEEVIPYGLLVWAGgnRaRPLTKKLmeGSE----EQNNRRGLVVDEYLKlKGYKDIFALGDCthTA 413
Cdd:TIGR01350 240 NDDQVTYEN-KGGETETLTGEKVLVAVG--R-KPNTEGL--GLEklgvELDERGRIVVDEYMR-TNVPGIYAIGDV--IG 310

                         170
                  ....*....|..
gi 19115108   414 YAPTAQVASQQG 425
Cdd:TIGR01350 311 GPMLAHVASHEG 322
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 256-345 4.63e-11

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: 58.75  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   256 HTVVVGGGPTGMEFAGEMADfieddlkswypeLADDfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKV 335
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALAR------------LGSK--VTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAI 66

                          90
                  ....*....|
gi 19115108   336 TAENIHVEVK 345
Cdd:pfam00070  67 EGNGDGVVVV 76
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 258-414 7.51e-11

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 64.43  E-value: 7.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  258 VVVGGGPTGMEFAgemadfieddlkSWYPELADDfaVTLVEALPSVLPMFSAKLRDYTQSLFdSSHIKIRTNTALKKVTA 337
Cdd:PRK06292 173 AVIGGGVIGLELG------------QALSRLGVK--VTVFERGDRILPLEDPEVSKQAQKIL-SKEFKIKLGAKVTSVEK 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  338 ENIH-VEVKNPDGSKQEEVIPYgLLVWAGgnRaRPLTKKLmeGSEE---QNNRRGLV-VDEYLKlKGYKDIFALGDCT-- 410
Cdd:PRK06292 238 SGDEkVEELEKGGKTETIEADY-VLVATG--R-RPNTDGL--GLENtgiELDERGRPvVDEHTQ-TSVPGIYAAGDVNgk 310


                 ....*...
gi 19115108  411 ----HTAY 414
Cdd:PRK06292 311 ppllHEAA 318
PRK06370 PRK06370
FAD-containing oxidoreductase;
256-415 1.41e-08

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 57.13  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  256 HTVVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKV 335
Cdd:PRK06370 173 HLVIIGGGYIGLEFAQMFRRFGSE--------------VTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRV 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  336 --TAENIHVEVKNPDGSKQEEVipYGLLVWAGgnRaRPLTKKLmeGSE----EQNNRRGLVVDEYLKLKGyKDIFALGDC 409
Cdd:PRK06370 239 erDGDGIAVGLDCNGGAPEITG--SHILVAVG--R-VPNTDDL--GLEaagvETDARGYIKVDDQLRTTN-PGIYAAGDC 310

                        170
                 ....*....|..
gi 19115108  410 ------THTAYA 415
Cdd:PRK06370 311 ngrgafTHTAYN 322
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
160-418 9.36e-08

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 53.97  E-value: 9.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 160 VKFYEAECTDVDADKKVIHIkkTTTDGvdleQEIKYDYLVCSHGAETQTFNIPGIAEYgcflkeiwdaqkIRARILHC-- 237
Cdd:COG0492  72 AEILLEEVTSVDKDDGPFRV--TTDDG----TEYEAKAVIIATGAGPRKLGLPGEEEF------------EGRGVSYCat 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 238 LEQAQFKDLpaetrrryvHTVVVGGGPTGMEFAGEMADFieddlkswypelADDfaVTLVealpsvlpMFSAKLR--DYT 315
Cdd:COG0492 134 CDGFFFRGK---------DVVVVGGGDSALEEALYLTKF------------ASK--VTLI--------HRRDELRasKIL 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108 316 QS-LFDSSHIKIRTNTALKKVTAENI--HVEVKNPDgSKQEEVIPY-GLLVwAGGnrARPLTkKLMEGSE-EQNNRRGLV 390
Cdd:COG0492 183 VErLRANPKIEVLWNTEVTEIEGDGRveGVTLKNVK-TGEEKELEVdGVFV-AIG--LKPNT-ELLKGLGlELDEDGYIV 257

                       250       260       270
                ....*....|....*....|....*....|..
gi 19115108 391 VDEYLK--LKGykdIFALGDCTHTAY--APTA 418
Cdd:COG0492 258 VDEDMEtsVPG---VFAAGDVRDYKYrqAATA 286
PRK07251 PRK07251
FAD-containing oxidoreductase;
175-408 2.70e-06

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 49.75  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  175 KVIHIkkttTDGVDlEQEIKYDYLVCSHGAETQTFNIPGIAEYgcflKEIWDAQKIRarilhcleqaQFKDLPAETrrry 254
Cdd:PRK07251 104 KVIEV----QAGDE-KIELTAETIVINTGAVSNVLPIPGLADS----KHVYDSTGIQ----------SLETLPERL---- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  255 vhtVVVGGGPTGMEFAGemadfieddlksWYPELADDfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKK 334
Cdd:PRK07251 161 ---GIIGGGNIGLEFAG------------LYNKLGSK--VTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTE 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115108  335 VTAENIHVEVKNPDGSKQeevipYGLLVWAGGNraRPLTKKL-MEGSE-EQNNRRGLVVDEYLKlKGYKDIFALGD 408
Cdd:PRK07251 224 VKNDGDQVLVVTEDETYR-----FDALLYATGR--KPNTEPLgLENTDiELTERGAIKVDDYCQ-TSVPGVFAVGD 291
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 173-410 4.53e-06

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: 49.20  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   173 DKKVIHIKKTTTDGVDLEQEIKYDYLVCSHGAETQTFNIPGIAeygcflkeiwdaqkirarilHCLEQAQFKDLPAETRR 252
Cdd:TIGR01423 130 DKNVVLVRESADPKSAVKERLQAEHILLATGSWPQMLGIPGIE--------------------HCISSNEAFYLDEPPRR 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   253 ryvhTVVVGGGPTGMEFAGemadfIEDDLKswypelADDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTAL 332
Cdd:TIGR01423 190 ----VLTVGGGFISVEFAG-----IFNAYK------PRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENP 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   333 KKVTaenihvevKNPDGSKQ-----EEVIPYGLLVWAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKlKGYKDIFALG 407
Cdd:TIGR01423 255 AKVT--------LNADGSKHvtfesGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSR-TNVPNIYAIG 325


                  ...
gi 19115108   408 DCT 410
Cdd:TIGR01423 326 DVT 328
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 188-410 7.87e-06

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 48.47  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  188 DLEQEIKYDYLVCSHGAETQTFNIPGIAEygcfLKEIWDAQKIrarilhcleqAQFKDLPAetrrryvHTVVVGGGPTGM 267
Cdd:PRK08010 113 EGNLEIHGEKIFINTGAQTVVPPIPGITT----TPGVYDSTGL----------LNLKELPG-------HLGILGGGYIGV 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  268 EFAGEMADFieddlkswypeladDFAVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTAENIHVEVKNP 347
Cdd:PRK08010 172 EFASMFANF--------------GSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSE 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115108  348 DGSKQEEvipyGLLVwAGGNRARPLTKKLMEGSEEQNNRRGLVVDEYLKLKGyKDIFALGDCT 410
Cdd:PRK08010 238 HAQLAVD----ALLI-ASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTA-DNIWAMGDVT 294
PRK06116 PRK06116
glutathione reductase; Validated
 236-411 4.32e-05

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 45.92  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  236 HCLEQAQFKDLPAETRRryvhTVVVGGGPTGMEFAG-------EMADFIEDD--LKSWYPELADdfavTLVEALpsvlpm 306
Cdd:PRK06116 153 YGITSDGFFALEELPKR----VAVVGAGYIAVEFAGvlnglgsETHLFVRGDapLRGFDPDIRE----TLVEEM------ 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  307 fsaklrdytqslfDSSHIKIRTNTALKKVtaenihveVKNPDGS-----KQEEVIPYGLLVWAGGnRaRPLTKKLmeGSE 381
Cdd:PRK06116 219 -------------EKKGIRLHTNAVPKAV--------EKNADGSltltlEDGETLTVDCLIWAIG-R-EPNTDGL--GLE 273

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19115108  382 ----EQNNRRGLVVDEYLK--LKGykdIFALGDCTH 411
Cdd:PRK06116 274 nagvKLNEKGYIIVDEYQNtnVPG---IYAVGDVTG 306
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 258-425 5.11e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 46.07  E-value: 5.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  258 VVVGGGPTGMEFAgemadfieddlkSWYPELADDfaVTLVEALPSVLPMFSAKLRDYTQSLFDSSHIKIRTNTALKKVTA 337
Cdd:PRK06327 187 AVIGAGVIGLELG------------SVWRRLGAE--VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKT 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108  338 --ENIHVEVKNPDGSKQEEVIPYgLLVWAGgnRaRPLTKKL-MEGSEEQNNRRGLV-VDEYLK--LKGykdIFALGDCTH 411
Cdd:PRK06327 253 ggKGVSVAYTDADGEAQTLEVDK-LIVSIG--R-VPNTDGLgLEAVGLKLDERGFIpVDDHCRtnVPN---VYAIGDVVR 325

                        170
                 ....*....|....
gi 19115108  412 TAYapTAQVASQQG 425
Cdd:PRK06327 326 GPM--LAHKAEEEG 337
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 160-409 1.84e-04

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 44.43  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   160 VKFYEAE-CTDVDADKKVIHikktttdgVDLEQEIKYDYLVCSHGAETQTFNIPGIAEYGCF-LKEIWDAQKIRArilhc 237
Cdd:TIGR02374  69 ITLYTGEtVIQIDTDQKQVI--------TDAGRTLSYDKLILATGSYPFILPIPGADKKGVYvFRTIEDLDAIMA----- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   238 leqaqfkdlpaeTRRRYVHTVVVGGGPTGMEFAGEMADFIEDdlkswypeladdfaVTLVEALPSVLP-----MFSAKLR 312
Cdd:TIGR02374 136 ------------MAQRFKKAAVIGGGLLGLEAAVGLQNLGMD--------------VSVIHHAPGLMAkqldqTAGRLLQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115108   313 DYTQSLFDSSHIKIRTNTALKKVTAENIHVEvknpDGSkqeeVIPYGLLVWAGGnrARPLTKKLMEGSEEQNnrRGLVVD 392
Cdd:TIGR02374 190 RELEQKGLTFLLEKDTVEIVGATKADRIRFK----DGS----SLEADLIVMAAG--IRPNDELAVSAGIKVN--RGIIVN 257

                         250
                  ....*....|....*..
gi 19115108   393 EYLKLKGyKDIFALGDC 409
Cdd:TIGR02374 258 DSMQTSD-PDIYAVGEC 273
 
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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