NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|874507329|ref|NP_001297154|]
View 

ferroptosis suppressor protein 1 [Heterocephalus glaber]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441299)

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; similar to sulfide:quinone oxidoreductase which catalyzes the oxidation of hydrogen sulfide using quinone as the electron acceptor

EC:  1.6.-.-
Gene Ontology:  GO:0003954|GO:0006116
PubMed:  15590775|28181562

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 4.43e-40

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 4.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  76 NFRQGQVVGIDLKNQTVLLQGGEALPFSHLILATGSTGPFPGkfNK--------VCSQQAAIQAYEDMVTQVQRSE---- 143
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAErrrl 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 144 ------------FivvvgggsagvEMAAEI----KTDYPEKGVTLIHSQVSL--ADKELLP----CVRQEVKEILLRKGV 201
Cdd:COG1252  150 ltivvvgggptgV-----------ELAGELaellRKLLRYPGIDPDKVRITLveAGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 202 QLVLSERVNNLEElplseyrDyiKVQTDKGTEVATNLVIPCIGIKINSSAYGSAFEsrLASSGALRVNEFLQVEGYSNIY 281
Cdd:COG1252  219 EVHTGTRVTEVDA-------D--GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 282 AIGDCADVNE------PKMAYLAGLHANVAVANIVNSMKQRPLKTYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252  288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 4.43e-40

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 4.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  76 NFRQGQVVGIDLKNQTVLLQGGEALPFSHLILATGSTGPFPGkfNK--------VCSQQAAIQAYEDMVTQVQRSE---- 143
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAErrrl 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 144 ------------FivvvgggsagvEMAAEI----KTDYPEKGVTLIHSQVSL--ADKELLP----CVRQEVKEILLRKGV 201
Cdd:COG1252  150 ltivvvgggptgV-----------ELAGELaellRKLLRYPGIDPDKVRITLveAGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 202 QLVLSERVNNLEElplseyrDyiKVQTDKGTEVATNLVIPCIGIKINSSAYGSAFEsrLASSGALRVNEFLQVEGYSNIY 281
Cdd:COG1252  219 EVHTGTRVTEVDA-------D--GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 282 AIGDCADVNE------PKMAYLAGLHANVAVANIVNSMKQRPLKTYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252  288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-310 6.46e-16

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 78.42  E-value: 6.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  77 FRQGQVVGIDLKNQTVLLQGgEALPFSHLILATGSTG---PFPGkfNKVCSQQAAIQAYEDMVTQVQRSEFIVVVGGGSA 153
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 154 GVEMAAEIKTDypEKGVTLIHSQVSLADKELLPCVRQEVKEILLRKGVQLVLSERVNNLEELplseyRDYIKVQTDKGTE 233
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSGRS 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 234 VATNLVIPCIGIKINSSaygsafesrLASSGALRVNEFLQVEGY-----SNIYAIGDCADVNEPKMAYL--AGLHANVAV 306
Cdd:PRK04965 226 IEVDAVIAAAGLRPNTA---------LARRAGLAVNRGIVVDSYlqtsaPDIYALGDCAEINGQVLPFLqpIQLSAMALA 296


                 ....
gi 874507329 307 ANIV 310
Cdd:PRK04965 297 KNLL 300
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 91-309 9.14e-08

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: 53.80  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   91 TVLLQGG---EALPFSHLILATGS-----TGPFPGKFNKVCSQQAAIQayedmVTQVQRSEFIVVVGGgsagveMAAEIK 162
Cdd:TIGR01350 118 TVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIGGGV------IGIEFA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  163 TDYPEKG--VTLIHSQvsladKELLPC----VRQEVKEILLRKGVQLVLSERVNNLEELplseyRDYIKVQTDKGTEVAT 236
Cdd:TIGR01350 187 SIFASLGskVTVIEML-----DRILPGedaeVSKVLQKALKKKGVKILTNTKVTAVEKN-----DDQVTYENKGGETETL 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 874507329  237 --NLVIPCIGIKINSSAYG-SAFESRLASSGALRVNEFLQVeGYSNIYAIGdcaDVNEPKM-AYLAGLHANVAVANI 309
Cdd:TIGR01350 257 tgEKVLVAVGRKPNTEGLGlEKLGVELDERGRIVVDEYMRT-NVPGIYAIG---DVIGGPMlAHVASHEGIVAAENI 329
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.23e-06

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 49.62  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   19 GGFGGIAAASQLQALNCPFTLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQ----------GQVVG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKlnngievllgTEVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   85 IDLKNQTVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNKVCSQQAAIQAYEDMVTQVQRS------------EF 144
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKrvvvvgggyigvEL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  145 ivvvgggsagVEMAAEIKTDypekgVTLIHsqvslADKELLPC----VRQEVKEILLRKGVQLVLSERVNNLEELPlsey 220
Cdd:pfam07992 168 ----------AAALAKLGKE-----VTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG---- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  221 rDYIKVQTDKGTEVATNLVIPCIGIKINSSAYGSA-FEsrLASSGALRVNEFLQVEgYSNIYAIGDCaDVNEPKMAYLAG 299
Cdd:pfam07992 224 -DGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAV 298


                  ...
gi 874507329  300 LHA 302
Cdd:pfam07992 299 AQG 301
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 4.43e-40

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 4.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  76 NFRQGQVVGIDLKNQTVLLQGGEALPFSHLILATGSTGPFPGkfNK--------VCSQQAAIQAYEDMVTQVQRSE---- 143
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAErrrl 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 144 ------------FivvvgggsagvEMAAEI----KTDYPEKGVTLIHSQVSL--ADKELLP----CVRQEVKEILLRKGV 201
Cdd:COG1252  150 ltivvvgggptgV-----------ELAGELaellRKLLRYPGIDPDKVRITLveAGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 202 QLVLSERVNNLEElplseyrDyiKVQTDKGTEVATNLVIPCIGIKINSSAYGSAFEsrLASSGALRVNEFLQVEGYSNIY 281
Cdd:COG1252  219 EVHTGTRVTEVDA-------D--GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 282 AIGDCADVNE------PKMAYLAGLHANVAVANIVNSMKQRPLKTYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252  288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-310 3.26e-24

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: 101.43  E-value: 3.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  64 KTFISYSVTFKdnfRQGQVVGIDLKNQTVLLQGGEALPFSHLILATGST---GPFPG-KFNKVCSqqaaIQAYEDMV--- 136
Cdd:COG0446   44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGlDLPGVFT----LRTLDDADalr 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 137 TQVQRSE----------FIvvvgggsaGVEMAAEIKtdypEKG--VTLIH--SQV-SLADKEllpcVRQEVKEILLRKGV 201
Cdd:COG0446  117 EALKEFKgkravvigggPI--------GLELAEALR----KRGlkVTLVEraPRLlGVLDPE----MAALLEEELREHGV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 202 QLVLSERVNNLEElplseyRDYIKVQTDKGTEVATNLVIPCIGIKINSSAygsAFESRLA--SSGALRVNEFLQVeGYSN 279
Cdd:COG0446  181 ELRLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTEL---AKDAGLAlgERGWIKVDETLQT-SDPD 250

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 874507329 280 IYAIGDCADVNEP---KMAYLA-GLHAN----VAVANIV 310
Cdd:COG0446  251 VYAAGDCAEVPHPvtgKTVYIPlASAANkqgrVAAENIL 289
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-310 6.46e-16

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 78.42  E-value: 6.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  77 FRQGQVVGIDLKNQTVLLQGgEALPFSHLILATGSTG---PFPGkfNKVCSQQAAIQAYEDMVTQVQRSEFIVVVGGGSA 153
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 154 GVEMAAEIKTDypEKGVTLIHSQVSLADKELLPCVRQEVKEILLRKGVQLVLSERVNNLEELplseyRDYIKVQTDKGTE 233
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSGRS 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 234 VATNLVIPCIGIKINSSaygsafesrLASSGALRVNEFLQVEGY-----SNIYAIGDCADVNEPKMAYL--AGLHANVAV 306
Cdd:PRK04965 226 IEVDAVIAAAGLRPNTA---------LARRAGLAVNRGIVVDSYlqtsaPDIYALGDCAEINGQVLPFLqpIQLSAMALA 296


                 ....
gi 874507329 307 ANIV 310
Cdd:PRK04965 297 KNLL 300
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
82-310 3.29e-13

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 70.17  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  82 VVGIDLKNQTVLLQGGEALPFSHLILATGSTgPF----PGK-------FNKvcsqqaaIQAYEDMVTQVQRSE------- 143
Cdd:COG1251   79 VTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPGAdlpgvftLRT-------LDDADALRAALAPGKrvvvigg 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 144 -FIvvvgggsaGVEMAAEIKtdypEKG--VTLIHsqvsLADKeLLPcvRQ-------EVKEILLRKGVQLVLSERVNNLE 213
Cdd:COG1251  151 gLI--------GLEAAAALR----KRGleVTVVE----RAPR-LLP--RQldeeagaLLQRLLEALGVEVRLGTGVTEIE 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 214 ElplseyRDYIK-VQTDKGTEVATNLVIPCIGIKINSSAygsAFESRLASSGALRVNEFLQVeGYSNIYAIGDCADVNEP 292
Cdd:COG1251  212 G------DDRVTgVRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHPGP 281

                        250
                 ....*....|....*...
gi 874507329 293 kmayLAGLHANVAVANIV 310
Cdd:COG1251  282 ----VYGRRVLELVAPAY 295
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 156-290 1.85e-09

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 58.90  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 156 EMAAEIKTDypEKGVTLI-HSQVSLA---DKELLPCVRQEVKEillrKGVQLVLSERVNNLEelplSEYRDYiKVQTDKG 231
Cdd:PRK09564 163 EAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSLI----GEDKVE-GVVTDKG 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 874507329 232 tEVATNLVIPCIGIKINSSAYGSAFESRLASsGALRVNEFLQVEgYSNIYAIGDCADVN 290
Cdd:PRK09564 232 -EYEADVVIVATGVKPNTEFLEDTGLKTLKN-GAIIVDEYGETS-IENIYAAGDCATIY 287
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 39-311 2.75e-08

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: 55.09  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  39 LVDMKDSFhhnVAALRASVESGFAKK--TFISYSVTFKDNfrqgqvvgidlknQTVLLQGGEALPFSHLILATGSTG--- 113
Cdd:COG1249   82 LMARKDKV---VDRLRGGVEELLKKNgvDVIRGRARFVDP-------------HTVEVTGGETLTADHIVIATGSRPrvp 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 114 PFPGKFNK--VCSQQA----------------AIqayedmvtqvqrsefivvvgggsaGVEMA-------AEiktdypek 168
Cdd:COG1249  146 PIPGLDEVrvLTSDEAleleelpkslvvigggYI------------------------GLEFAqifarlgSE-------- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 169 gVTLIHSQ---VSLADKEllpcVRQEVKEILLRKGVQLVLSERVNNLEELPlseyrDYIKVQTDKGTEVATN---LVIPC 242
Cdd:COG1249  194 -VTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVTLEDGGGEEAVeadKVLVA 263

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 874507329 243 IGIKINSSAYGsaFES---RLASSGALRVNEFLQVeGYSNIYAIGDCADvnEPKMAYLAGLHANVAVANIVN 311
Cdd:COG1249  264 TGRRPNTDGLG--LEAagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGRVAAENILG 330
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 91-309 9.14e-08

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: 53.80  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   91 TVLLQGG---EALPFSHLILATGS-----TGPFPGKFNKVCSQQAAIQayedmVTQVQRSEFIVVVGGgsagveMAAEIK 162
Cdd:TIGR01350 118 TVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIGGGV------IGIEFA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  163 TDYPEKG--VTLIHSQvsladKELLPC----VRQEVKEILLRKGVQLVLSERVNNLEELplseyRDYIKVQTDKGTEVAT 236
Cdd:TIGR01350 187 SIFASLGskVTVIEML-----DRILPGedaeVSKVLQKALKKKGVKILTNTKVTAVEKN-----DDQVTYENKGGETETL 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 874507329  237 --NLVIPCIGIKINSSAYG-SAFESRLASSGALRVNEFLQVeGYSNIYAIGdcaDVNEPKM-AYLAGLHANVAVANI 309
Cdd:TIGR01350 257 tgEKVLVAVGRKPNTEGLGlEKLGVELDERGRIVVDEYMRT-NVPGIYAIG---DVIGGPMlAHVASHEGIVAAENI 329
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-290 1.38e-07

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 53.29  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   82 VVGIDLKNQTVLLQGGEALPFSHLILATGSTG---PFPGKFNKVCSQQAAIQAYEDMVTQVQRSEFIVVVGGGSAGVEMA 158
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  159 AEIKTDYPEkgVTLIHSQVSLADKELLPCVRQEVKEILLRKGVQLVLSErvnNLEELPLSEYRDYIKVQtdKGTEVATNL 238
Cdd:TIGR02374 157 VGLQNLGMD--VSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--DGSSLEADL 229

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 874507329  239 VIPCIGIKINSSAygsAFESRLASSGALRVNEFLQVEGySNIYAIGDCADVN 290
Cdd:TIGR02374 230 IVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTSD-PDIYAVGECAEHN 277
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-344 3.83e-07

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 51.69  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  77 FRQGQVVGIDLKNQTVL----------LQGGEALPFSHLILATGSTgpfPGKFNkvcsqqaaIQAYEDMVTQVQRSEFIV 146
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAFFLKEVNHAR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 147 VVGGGSAGVEMAAEIKTDYPEKGVTLIHSQV------------SLAD------KELLPCVRQEVKEILLRKGVQlVLSER 208
Cdd:PTZ00318 148 GIRKRIVQCIERASLPTTSVEERKRLLHFVVvgggptgvefaaELADffrddvRNLNPELVEECKVTVLEAGSE-VLGSF 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 209 vnnleELPLSEY------RDYIKVQ--------------TDKGTEVATNLVIPCIGIKINSSAYGSAFESRlaSSGALRV 268
Cdd:PTZ00318 227 -----DQALRKYgqrrlrRLGVDIRtktavkevldkevvLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKT--SRGRISV 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329 269 NEFLQVEGYSNIYAIGDCADVNE---PKMAYLAGLHANVAVANIVNSMKQRPL-KTYKPGALTFLLSMGRNDGVGQISGF 344
Cdd:PTZ00318 300 DDHLRVKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAF 379
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.23e-06

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 49.62  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   19 GGFGGIAAASQLQALNCPFTLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQ----------GQVVG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKlnngievllgTEVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329   85 IDLKNQTVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNKVCSQQAAIQAYEDMVTQVQRS------------EF 144
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKrvvvvgggyigvEL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  145 ivvvgggsagVEMAAEIKTDypekgVTLIHsqvslADKELLPC----VRQEVKEILLRKGVQLVLSERVNNLEELPlsey 220
Cdd:pfam07992 168 ----------AAALAKLGKE-----VTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG---- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 874507329  221 rDYIKVQTDKGTEVATNLVIPCIGIKINSSAYGSA-FEsrLASSGALRVNEFLQVEgYSNIYAIGDCaDVNEPKMAYLAG 299
Cdd:pfam07992 224 -DGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAV 298


                  ...
gi 874507329  300 LHA 302
Cdd:pfam07992 299 AQG 301
PLN02507 PLN02507
glutathione reductase
 211-285 3.30e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 39.41  E-value: 3.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 874507329 211 NLEELPLSEyrDYIKVQTDKGTEVATNLVIPCIGIKINSSAYG-SAFESRLASSGALRVNEFLQVEgYSNIYAIGD 285
Cdd:PLN02507 266 NLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTKRLNlEAVGVELDKAGAVKVDEYSRTN-IPSIWAIGD 338
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH