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Conserved domains on  [gi|1958757588|ref|XP_038954799|]
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ferroptosis suppressor protein 1 isoform X4 [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
100-379 1.21e-39

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.28  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 100 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 174
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 175 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 225
Cdd:COG1252   144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 226 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVNEFLQVEGYSNIY 305
Cdd:COG1252   219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 306 AIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 379
Cdd:COG1252   288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
100-379 1.21e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.28  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 100 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 174
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 175 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 225
Cdd:COG1252   144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 226 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVNEFLQVEGYSNIY 305
Cdd:COG1252   219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 306 AIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 379
Cdd:COG1252   288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
101-320 2.48e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 76.88  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 101 FRQGKVIGIDLKNRMVLLeGGEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 177
Cdd:PRK04965   76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 178 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 255
Cdd:PRK04965  153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958757588 256 TEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCADIKEPKMAY 320
Cdd:PRK04965  224 RSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 43-326 1.68e-08

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: 55.40  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588  43 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQGK----------VIG 108
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKLNngievllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 109 IDLKNRMVLLE-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 177
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 178 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 245
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 246 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSA-FEsrLASNGALKVNEFLQVEgYSNIYAIGDCaDIKEPKMAYHAGL 324
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVA 299


                  ..
gi 1958757588 325 HA 326
Cdd:pfam07992 300 QG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 101-333 1.54e-07

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: 53.03  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 101 FRQGKVI-----GIDLKNRMVLLEGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 167
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 168 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 238
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 239 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAY-RSAFESRLASNGALKVNEFLQVeGYSNIYAIGDCadIKE 315
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGG 311

                         250
                  ....*....|....*...
gi 1958757588 316 PKMAYHAGLHANIAVANI 333
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
100-379 1.21e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.28  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 100 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 174
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 175 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 225
Cdd:COG1252   144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 226 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVNEFLQVEGYSNIY 305
Cdd:COG1252   219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 306 AIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 379
Cdd:COG1252   288 AIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 88-334 1.13e-23

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: 100.27  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588  88 KTFISYSVTFKdnfRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGST---GPFPGKFNEVSCQQAAIQAYEDMVKQIQ 164
Cdd:COG0446    44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGLDLPGVFTLRTLDDADALREALK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 165 RSQ----------FIvvvgggsaGVEMAAEIKTEypEKEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSE 231
Cdd:COG0446   121 EFKgkravvigggPI--------GLELAEALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVELRLGE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 232 RVSNLEElprneyREYIKVETDKGTEVATNMVIVCNGIKINSSAyrsAFESRLA--SNGALKVNEFLQVeGYSNIYAIGD 309
Cdd:COG0446   187 TVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTEL---AKDAGLAlgERGWIKVDETLQT-SDPDVYAAGD 256

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958757588 310 CADIKEP--------KMAYHAGLHANIAVANIV 334
Cdd:COG0446   257 CAEVPHPvtgktvyiPLASAANKQGRVAAENIL 289
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
101-320 2.48e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 76.88  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 101 FRQGKVIGIDLKNRMVLLeGGEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 177
Cdd:PRK04965   76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 178 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 255
Cdd:PRK04965  153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958757588 256 TEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCADIKEPKMAY 320
Cdd:PRK04965  224 RSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
105-334 3.02e-15

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 76.72  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 105 KVIGIDLKNRMVLLEGGEALPFSHLILATGSTgPF----PGK-------FNEvscqqaaIQAYEDMVKQIQRSQ------ 167
Cdd:COG1251    78 RVTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPGAdlpgvftLRT-------LDDADALRAALAPGKrvvvig 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 168 --FIvvvgggsaGVEMAAEIKTEypEKEVTLIH-SRVPLA---DKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPR 241
Cdd:COG1251   150 ggLI--------GLEAAAALRKR--GLEVTVVErAPRLLPrqlDEE----AGALLQRLLEALGVEVRLGTGVTEIEGDDR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 242 NEyreyiKVETDKGTEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVeGYSNIYAIGDCADIKEPkmayH 321
Cdd:COG1251   216 VT-----GVRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHPGP----V 282

                         250
                  ....*....|...
gi 1958757588 322 AGLHANIAVANIV 334
Cdd:COG1251   283 YGRRVLELVAPAY 295
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 105-335 8.69e-13

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 69.30  E-value: 8.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 105 KVIGIDLKNRMVL---LEGGEAL--PFSHLILATGSTGPFPgKFNEVSCQ-----------QAAIQAYEDmvKQIQR--- 165
Cdd:PRK09564   78 EVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARPIIP-PIKNINLEnvytlksmedgLALKELLKD--EEIKNivi 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 166 --SQFIVVvgggsagvEMAAEIKTEypEKEVTLIH--SRV-PLA-DKELLPCVRQEVKEillrKGVQLLLSERVSNLEel 239
Cdd:PRK09564  155 igAGFIGL--------EAVEAAKHL--GKNVRIIQleDRIlPDSfDKEITDVMEEELRE----NGVELHLNEFVKSLI-- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 240 prNEYREYiKVETDKGtEVATNMVIVCNGIKINSSAYRSAFESRLAsNGALKVNEFLQVEgYSNIYAIGDCADIkepkma 319
Cdd:PRK09564  219 --GEDKVE-GVVTDKG-EYEADVVIVATGVKPNTEFLEDTGLKTLK-NGAIIVDEYGETS-IENIYAAGDCATI------ 286

                         250
                  ....*....|....*...
gi 1958757588 320 YHAGLHAN--IAVANIVN 335
Cdd:PRK09564  287 YNIVSNKNvyVPLATTAN 304
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 178-335 3.16e-09

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: 58.17  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 178 GVEMA---AEIKTeypekEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPrneyrEYIKVE 251
Cdd:COG1249   180 GLEFAqifARLGS-----EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVT 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 252 TDKGTEVATN---MVIVCNGIKINSSAYrsAFES---RLASNGALKVNEFLQVeGYSNIYAIGDCADikEPKMAYHAGLH 325
Cdd:COG1249   246 LEDGGGEEAVeadKVLVATGRRPNTDGL--GLEAagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAE 320

                         170
                  ....*....|
gi 1958757588 326 ANIAVANIVN 335
Cdd:COG1249   321 GRVAAENILG 330
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 43-326 1.68e-08

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: 55.40  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588  43 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQGK----------VIG 108
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKLNngievllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 109 IDLKNRMVLLE-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 177
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 178 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 245
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 246 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSA-FEsrLASNGALKVNEFLQVEgYSNIYAIGDCaDIKEPKMAYHAGL 324
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVA 299


                  ..
gi 1958757588 325 HA 326
Cdd:pfam07992 300 QG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 101-396 1.00e-07

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 53.62  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 101 FRQGKVIGIDLKNRMVL----------LEGGEALPFSHLILATGSTgpfPGKFNevscqqaaIQAYEDMV---KQIQRSQ 167
Cdd:PTZ00318   79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHAR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 168 FIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSRV------------PLAD------KELLPCVRQEVKEILLRKGVQLLL 229
Cdd:PTZ00318  148 GIRKRIVQCI---ERASLPTTSVEERKRLLHFVVvgggptgvefaaELADffrddvRNLNPELVEECKVTVLEAGSEVLG 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 230 S--ERVSN--LEELPRNEYREYIK----------VETDKGTEVATNMVIVCNGIKINSSAYRSAFESRlaSNGALKVNEF 295
Cdd:PTZ00318  225 SfdQALRKygQRRLRRLGVDIRTKtavkevldkeVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKT--SRGRISVDDH 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 296 LQVEGYSNIYAIGDCADIKE---PKMAYHAGLHANIAVANIVNSMKQRPL-KAYKPGALTFLLSMGRNDGVGQISGF-YV 370
Cdd:PTZ00318  303 LRVKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAFdLS 382

                         330       340
                  ....*....|....*....|....*.
gi 1958757588 371 GRLMVRLAKSRDLLISTSWKTMRQSP 396
Cdd:PTZ00318  383 GFKALLFWRSAYLTILGSWRSKLYVL 408
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 101-333 1.54e-07

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: 53.03  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 101 FRQGKVI-----GIDLKNRMVLLEGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 167
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 168 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 238
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 239 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAY-RSAFESRLASNGALKVNEFLQVeGYSNIYAIGDCadIKE 315
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGG 311

                         250
                  ....*....|....*...
gi 1958757588 316 PKMAYHAGLHANIAVANI 333
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 105-313 6.14e-07

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 51.75  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 105 KVIGIDLKNRMVLLEGGEALPFSHLILATGSTG---PFPGK-------FNEVScqqaAIQAYEDMVKQIQRSQFIVVVGG 174
Cdd:TIGR02374  76 TVIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPGAdkkgvyvFRTIE----DLDAIMAMAQRFKKAAVIGGGLL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 175 GsagveMAAEIKTEYPEKEVTLIHSRVPLADKELLPCVRQEVKEILLRKGVQLLLSErvsNLEELPRNEYREYIKVEtdK 254
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958757588 255 GTEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCADI 313
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTSD-PDIYAVGECAEH 276
PLN02507 PLN02507
glutathione reductase
 234-309 1.46e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 40.57  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958757588 234 SNLEELPRNEyrEYIKVETDKGTEVATNMVIVCNGIKINSSayRSAFES---RLASNGALKVNEFLQVEgYSNIYAIGD 309
Cdd:PLN02507  265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTK--RLNLEAvgvELDKAGAVKVDEYSRTN-IPSIWAIGD 338
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 193-332 2.67e-03

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 39.71  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757588 193 EVTLIHSRVPLAdKELLPCVRQEVKEILLRKGVQLLLServSNLEELPRNEYREYIKVET-DKGTEVATNMVIVCNGIKI 271
Cdd:TIGR02053 191 EVTILQRSDRLL-PREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRGGGKIITVEKpGGQGEVEADELLVATGRRP 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958757588 272 NSSAYR-SAFESRLASNGALKVNEFLQVEGySNIYAIGDCadIKEPKMAYHAGLHANIAVAN 332
Cdd:TIGR02053 267 NTDGLGlEKAGVKLDERGGILVDETLRTSN-PGIYAAGDV--TGGLQLEYVAAKEGVVAAEN 325
 
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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