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Conserved domains on  [gi|672086244|ref|XP_008771110|]
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ferroptosis suppressor protein 1 isoform X1 [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];
106-386 1.21e-39

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 106 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 180
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 181 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 231
Cdd:COG1252  144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 232 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYS 309
Cdd:COG1252  219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHP 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 310 NIYAIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVR 383
Cdd:COG1252  285 NVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAW 364


                 ...
gi 672086244 384 LAK 386
Cdd:COG1252  365 LLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
106-386 1.21e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 106 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 180
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 181 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 231
Cdd:COG1252  144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 232 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYS 309
Cdd:COG1252  219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHP 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 310 NIYAIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVR 383
Cdd:COG1252  285 NVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAW 364


                 ...
gi 672086244 384 LAK 386
Cdd:COG1252  365 LLK 367
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
107-327 5.06e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 75.72  E-value: 5.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 107 FRQGKVIGIDLKNRMVLLeGGEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 183
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 184 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 261
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672086244 262 TEVATNMVIVCNGIKINSSAYRsafaESRLASNGALKVNEFLQVEGySNIYAIGDCADIKEPKMAY 327
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTALAR----RAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 49-333 4.05e-09

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: 57.33  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244   49 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQ----------GKVIG 114
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKlnngievllgTEVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  115 IDLKNRMVLLE-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 183
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  184 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 251
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  252 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCaDIKEPKMAYHAGL 331
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVA 299


                  ..
gi 672086244  332 HA 333
Cdd:pfam07992 300 QG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 107-340 1.42e-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: 56.50  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  107 FRQGKVI-----GIDLKNRMVLLEGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 173
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  174 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 244
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  245 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCadIKE 322
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGG 311

                         250
                  ....*....|....*...
gi 672086244  323 PKMAYHAGLHANIAVANI 340
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
106-386 1.21e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 145.66  E-value: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 106 NFRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGG 180
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFER 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 181 GSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGV 231
Cdd:COG1252  144 AERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 232 QLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYS 309
Cdd:COG1252  219 EVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHP 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 310 NIYAIGDCADIKE------PKMAYHAGLHANIAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVR 383
Cdd:COG1252  285 NVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAW 364


                 ...
gi 672086244 384 LAK 386
Cdd:COG1252  365 LLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 94-341 5.94e-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: 101.04  E-value: 5.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  94 KTFISYSVTFKdnfRQGKVIGIDLKNRMVLLEGGEALPFSHLILATGST---GPFPGKFNEVSCQQAAIQAYEDMVKQIQ 170
Cdd:COG0446   44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGLDLPGVFTLRTLDDADALREALK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 171 RSQ----------FIvvvgggsaGVEMAAEIKTEypEKEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSE 237
Cdd:COG0446  121 EFKgkravvigggPI--------GLELAEALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVELRLGE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 238 RVSNLEElprneyREYIKVETDKGTEVATNMVIVCNGIKINssayrSAFAES---RLASNGALKVNEFLQVeGYSNIYAI 314
Cdd:COG0446  187 TVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPN-----TELAKDaglALGERGWIKVDETLQT-SDPDVYAA 254

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 672086244 315 GDCADIKEP--------KMAYHAGLHANIAVANIV 341
Cdd:COG0446  255 GDCAEVPHPvtgktvyiPLASAANKQGRVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
111-341 4.00e-16

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 79.42  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 111 KVIGIDLKNRMVLLEGGEALPFSHLILATGSTgPF----PGK-------FNEvscqqaaIQAYEDMVKQIQRSQ------ 173
Cdd:COG1251   78 RVTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPGAdlpgvftLRT-------LDDADALRAALAPGKrvvvig 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 174 --FIvvvgggsaGVEMAAEIKTEypEKEVTLIH-SRVPLA---DKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPR 247
Cdd:COG1251  150 ggLI--------GLEAAAALRKR--GLEVTVVErAPRLLPrqlDEE----AGALLQRLLEALGVEVRLGTGVTEIEGDDR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 248 NEyreyiKVETDKGTEVATNMVIVCNGIKINssayrSAFAE-SRLASNGALKVNEFLQVeGYSNIYAIGDCADIKEPkma 326
Cdd:COG1251  216 VT-----GVRLADGEELPADLVVVAIGVRPN-----TELARaAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHPGP--- 281

                        250
                 ....*....|....*
gi 672086244 327 yHAGLHANIAVANIV 341
Cdd:COG1251  282 -VYGRRVLELVAPAY 295
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
107-327 5.06e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 75.72  E-value: 5.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 107 FRQGKVIGIDLKNRMVLLeGGEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 183
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 184 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 261
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672086244 262 TEVATNMVIVCNGIKINSSAYRsafaESRLASNGALKVNEFLQVEGySNIYAIGDCADIKEPKMAY 327
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTALAR----RAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 111-342 3.10e-13

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 70.84  E-value: 3.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 111 KVIGIDLKNRMVL---LEGGEAL--PFSHLILATGSTGPFPgKFNEVSCQ-----------QAAIQAYEDmvKQIQR--- 171
Cdd:PRK09564  78 EVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARPIIP-PIKNINLEnvytlksmedgLALKELLKD--EEIKNivi 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 172 --SQFIVVvgggsagvEMAAEIKTEypEKEVTLIH--SRV-PLA-DKELLPCVRQEVKEillrKGVQLLLSERVSNLEel 245
Cdd:PRK09564 155 igAGFIGL--------EAVEAAKHL--GKNVRIIQleDRIlPDSfDKEITDVMEEELRE----NGVELHLNEFVKSLI-- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 246 prNEYREYiKVETDKGtEVATNMVIVCNGIKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCADIkepkm 325
Cdd:PRK09564 219 --GEDKVE-GVVTDKG-EYEADVVIVATGVKPNTEFLEDTGLK--TLKNGAIIVDEYGETS-IENIYAAGDCATI----- 286

                        250
                 ....*....|....*....
gi 672086244 326 aYHAGLHAN--IAVANIVN 342
Cdd:PRK09564 287 -YNIVSNKNvyVPLATTAN 304
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 184-342 2.70e-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: 58.56  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 184 GVEMA---AEIKTeypekEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPrneyrEYIKVE 257
Cdd:COG1249  180 GLEFAqifARLGS-----EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVT 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 258 TDKGTEVATN---MVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCADikEPKMAYHAGLHAN 334
Cdd:COG1249  246 LEDGGGEEAVeadKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGR 322


                 ....*...
gi 672086244 335 IAVANIVN 342
Cdd:COG1249  323 VAAENILG 330
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 49-333 4.05e-09

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: 57.33  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244   49 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKDNFRQ----------GKVIG 114
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKlnngievllgTEVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  115 IDLKNRMVLLE-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 183
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  184 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 251
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  252 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCaDIKEPKMAYHAGL 331
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVA 299


                  ..
gi 672086244  332 HA 333
Cdd:pfam07992 300 QG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 107-340 1.42e-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: 56.50  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  107 FRQGKVI-----GIDLKNRMVLLEGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 173
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  174 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 244
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  245 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCadIKE 322
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGG 311

                         250
                  ....*....|....*...
gi 672086244  323 PKMAYHAGLHANIAVANI 340
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 107-403 3.37e-07

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 52.08  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 107 FRQGKVIGIDLKNRMVL----------LEGGEALPFSHLILATGSTgpfPGKFNevscqqaaIQAYEDMV---KQIQRSQ 173
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHAR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 174 FIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSRV------------PLAD------KELLPCVRQEVKEILLRKGVQLLL 235
Cdd:PTZ00318 148 GIRKRIVQCI---ERASLPTTSVEERKRLLHFVVvgggptgvefaaELADffrddvRNLNPELVEECKVTVLEAGSEVLG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 236 SERVSNLEELPRNEYREYIKVETDKGT-EVATNMVIVCNGIKINSS--AYRSAFAESRLA--------SNGALKVNEFLQ 304
Cdd:PTZ00318 225 SFDQALRKYGQRRLRRLGVDIRTKTAVkEVLDKEVVLKDGEVIPTGlvVWSTGVGPGPLTkqlkvdktSRGRISVDDHLR 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244 305 VEGYSNIYAIGDCADIKE---PKMAYHAGLHANIAVANIVNSMKQRPL-KAYKPGALTFLLSMGRNDGVGQISGF-YVGR 379
Cdd:PTZ00318 305 VKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAFdLSGF 384

                        330       340
                 ....*....|....*....|....
gi 672086244 380 LMVRLAKSRDLLISTSWKTMRQSP 403
Cdd:PTZ00318 385 KALLFWRSAYLTILGSWRSKLYVL 408
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 111-320 1.09e-06

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 50.98  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  111 KVIGIDLKNRMVLLEGGEALPFSHLILATGSTG---PFPGK-------FNEVScqqaAIQAYEDMVKQIQRSQFIVVVGG 180
Cdd:TIGR02374  76 TVIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPGAdkkgvyvFRTIE----DLDAIMAMAQRFKKAAVIGGGLL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  181 GsagveMAAEIKTEYPEKEVTLIHSRVPLADKELLPCVRQEVKEILLRKGVQLLLSErvsNLEELPRNEYREYIKVEtdK 260
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  261 GTEVATNMVIVCNGIKINSSAYRSAfaesRLASNGALKVNEFLQVEGySNIYAIGDCADI 320
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDELAVSA----GIKVNRGIIVNDSMQTSD-PDIYAVGECAEH 276
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 199-339 3.42e-04

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: 42.79  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  199 EVTLIHSRVPLAdKELLPCVRQEVKEILLRKGVQLLLServSNLEELPRNEYREYIKVET-DKGTEVATNMVIVCNGIKI 277
Cdd:TIGR02053 191 EVTILQRSDRLL-PREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRGGGKIITVEKpGGQGEVEADELLVATGRRP 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672086244  278 NSSAYRSAFAESRLASNGALKVNEFLQVEGySNIYAIGDCadIKEPKMAYHAGLHANIAVAN 339
Cdd:TIGR02053 267 NTDGLGLEKAGVKLDERGGILVDETLRTSN-PGIYAAGDV--TGGLQLEYVAAKEGVVAAEN 325
PLN02507 PLN02507
glutathione reductase
 240-316 5.39e-04

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 42.11  E-value: 5.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672086244 240 SNLEELPRNEyrEYIKVETDKGTEVATNMVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVEgYSNIYAIGD 316
Cdd:PLN02507 265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTN-IPSIWAIGD 338
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 218-319 8.15e-03

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: 38.42  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672086244  218 VRQEVKEILLRKGVQLLLSERVSNLEELPRNEYReyikVETDKGTEVATNMVIVCNGIKINSSAYRSAFAESRLASNGAL 297
Cdd:TIGR01423 233 LRKELTKQLRANGINIMTNENPAKVTLNADGSKH----VTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAI 308

                          90       100
                  ....*....|....*....|..
gi 672086244  298 KVNEFLQVEgYSNIYAIGDCAD 319
Cdd:TIGR01423 309 QVDEFSRTN-VPNIYAIGDVTD 329
 
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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