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Conserved domains on  [gi|30017355|ref|NP_835159|]
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ferroptosis suppressor protein 1 isoform 2 [Mus musculus]

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];
67-355 3.24e-39

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 143.35  E-value: 3.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  67 ISYSATFKD---NFRQGKVIGIDLKNRMVLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ--- 140
Cdd:COG1252  60 IPLRELLRRagvRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdal 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 141 --RSQFIVVVGGGSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVR 189
Cdd:COG1252 132 alRERLLAAFERAERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLS 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 190 QEVKEILLRKGVQLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVN 269
Cdd:COG1252 207 EAAEKELEKRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVD 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 270 EFLQVEGYSNIYAIGDCADTKE------PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISG 343
Cdd:COG1252 276 PTLQVPGHPNVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG 355

                       330
                ....*....|..
gi 30017355 344 FYVGRLMVRLAK 355
Cdd:COG1252 356 LKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
67-355 3.24e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 143.35  E-value: 3.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  67 ISYSATFKD---NFRQGKVIGIDLKNRMVLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ--- 140
Cdd:COG1252  60 IPLRELLRRagvRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdal 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 141 --RSQFIVVVGGGSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVR 189
Cdd:COG1252 132 alRERLLAAFERAERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLS 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 190 QEVKEILLRKGVQLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVN 269
Cdd:COG1252 207 EAAEKELEKRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVD 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 270 EFLQVEGYSNIYAIGDCADTKE------PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISG 343
Cdd:COG1252 276 PTLQVPGHPNVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG 355

                       330
                ....*....|..
gi 30017355 344 FYVGRLMVRLAK 355
Cdd:COG1252 356 LKLSGFLAWLLK 367
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-296 5.19e-14

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 72.64  E-value: 5.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   77 FRQGKVIGIDLKNRMVLLQGgEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 153
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  154 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 231
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30017355  232 TEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCADTKEPKMAY 296
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.43e-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: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSATFKDNFRQGK----------VIG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKLNngievllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    85 IDLKNRMVLLQ-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 153
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   154 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 221
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   222 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSA-FEsrLASNGALKVNEFLQVEgYSNIYAIGDCADTKePKMAYHAGL 300
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDCRVGG-PELAQNAVA 299


                  ..
gi 30017355   301 HA 302
Cdd:pfam07992 300 QG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 77-309 5.04e-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: 54.57  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    77 FRQGKVI-----GIDLKNRMVLLQGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 143
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   144 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 214
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   215 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAY-RSAFESRLASNGALKVNEFLQVeGYSNIYAIGDCADTke 291
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDVIGG-- 311

                         250
                  ....*....|....*...
gi 30017355   292 PKMAYHAGLHANVAVANI 309
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
67-355 3.24e-39

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 143.35  E-value: 3.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  67 ISYSATFKD---NFRQGKVIGIDLKNRMVLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ--- 140
Cdd:COG1252  60 IPLRELLRRagvRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdal 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 141 --RSQFIVVVGGGSAGV--------------EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVR 189
Cdd:COG1252 132 alRERLLAAFERAERRRlltivvvgggptgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLS 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 190 QEVKEILLRKGVQLLLSERVSNLEELprneyreyiKVETDKGTEVATNMVIVCNGIKINSSAYRSAFEsrLASNGALKVN 269
Cdd:COG1252 207 EAAEKELEKRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVD 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 270 EFLQVEGYSNIYAIGDCADTKE------PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISG 343
Cdd:COG1252 276 PTLQVPGHPNVFAIGDCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGG 355

                       330
                ....*....|..
gi 30017355 344 FYVGRLMVRLAK 355
Cdd:COG1252 356 LKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-310 5.25e-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: 97.96  E-value: 5.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  64 KTFISYSATFKdnfRQGKVIGIDLKNRMVLLQGGEALPFSHLILATGST---GPFPGKFNEVSCQQAAIQAYEDMVKQIQ 140
Cdd:COG0446  44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGLDLPGVFTLRTLDDADALREALK 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 141 RSQ----------FIvvvgggsaGVEMAAEIKTEypEKEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSE 207
Cdd:COG0446 121 EFKgkravvigggPI--------GLELAEALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVELRLGE 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 208 RVSNLEElprneyREYIKVETDKGTEVATNMVIVCNGIKINSSAyrsAFESRLA--SNGALKVNEFLQVeGYSNIYAIGD 285
Cdd:COG0446 187 TVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTEL---AKDAGLAlgERGWIKVDETLQT-SDPDVYAAGD 256

                       250       260       270
                ....*....|....*....|....*....|...
gi 30017355 286 CADTKEP--------KMAYHAGLHANVAVANIV 310
Cdd:COG0446 257 CAEVPHPvtgktvyiPLASAANKQGRVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
81-287 7.78e-15

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 75.18  E-value: 7.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  81 KVIGIDLKNRMVLLQGGEALPFSHLILATGSTgPF----PGK-------FNEvscqqaaIQAYEDMVKQIQRSQ------ 143
Cdd:COG1251  78 RVTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPGAdlpgvftLRT-------LDDADALRAALAPGKrvvvig 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 144 --FIvvvgggsaGVEMAAEIKTEypEKEVTLIH-SRVPLA---DKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPR 217
Cdd:COG1251 150 ggLI--------GLEAAAALRKR--GLEVTVVErAPRLLPrqlDEE----AGALLQRLLEALGVEVRLGTGVTEIEGDDR 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 218 NEyreyiKVETDKGTEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVeGYSNIYAIGDCA 287
Cdd:COG1251 216 VT-----GVRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCA 276
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-296 5.19e-14

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 72.64  E-value: 5.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   77 FRQGKVIGIDLKNRMVLLQGgEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSA 153
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  154 GVEMAAEIKTEypEKEVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKG 231
Cdd:PRK04965 153 GTELAMDLCRA--GKAVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSG 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30017355  232 TEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCADTKEPKMAY 296
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 81-287 1.96e-12

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 68.14  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   81 KVIGIDLKNRMVL---LQGGEAL--PFSHLILATGSTGPFPgKFNEVSCQ-----------QAAIQAYEDmvKQIQR--- 141
Cdd:PRK09564  78 EVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARPIIP-PIKNINLEnvytlksmedgLALKELLKD--EEIKNivi 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  142 --SQFIVVvgggsagvEMAAEIKTEypEKEVTLIH--SRV-PLA-DKELLPCVRQEVKEillrKGVQLLLSERVSNLEel 215
Cdd:PRK09564 155 igAGFIGL--------EAVEAAKHL--GKNVRIIQleDRIlPDSfDKEITDVMEEELRE----NGVELHLNEFVKSLI-- 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017355  216 prNEYREYiKVETDKGtEVATNMVIVCNGIKINSSAYRSAFESRLAsNGALKVNEFLQVEgYSNIYAIGDCA 287
Cdd:PRK09564 219 --GEDKVE-GVVTDKG-EYEADVVIVATGVKPNTEFLEDTGLKTLK-NGAIIVDEYGETS-IENIYAAGDCA 284
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 39-311 4.12e-10

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: 60.87  E-value: 4.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  39 LVDMKDSFhhnVAALRASVESGFAKK--TFISYSATFKDNfrqgkvigidlknRMVLLQGGEALPFSHLILATGSTG--- 113
Cdd:COG1249  82 LMARKDKV---VDRLRGGVEELLKKNgvDVIRGRARFVDP-------------HTVEVTGGETLTADHIVIATGSRPrvp 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 114 PFPGkFNEVScqqaAI---QAYEdmVKQIQRS------QFIvvvgggsaGVEMA---AEIKTeypekEVTLIHSR---VP 178
Cdd:COG1249 146 PIPG-LDEVR----VLtsdEALE--LEELPKSlvviggGYI--------GLEFAqifARLGS-----EVTLVERGdrlLP 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355 179 LADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPrneyrEYIKVETDKGTEVATN---MVIVCNGIKINSSAYrsA 255
Cdd:COG1249 206 GEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVTLEDGGGEEAVeadKVLVATGRRPNTDGL--G 274

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30017355 256 FES---RLASNGALKVNEFLQVeGYSNIYAIGDCADtkEPKMAYHAGLHANVAVANIVN 311
Cdd:COG1249 275 LEAagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGRVAAENILG 330
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.43e-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: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSATFKDNFRQGK----------VIG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVVKKLNngievllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    85 IDLKNRMVLLQ-----GGEALPFSHLILATGSTG---PFPGkfnevscqqaAIQAYEDMVKQIQRSQFIVVVGGGSA--- 153
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPG----------VELNVGFLVRTLDSAEALRLKLLPKRvvv 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   154 ---------GVEMAAEIKteypeKEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyr 221
Cdd:pfam07992 158 vgggyigveLAAALAKLG-----KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   222 eyIKVETDKGTEVATNMVIVCNGIKINSSAYRSA-FEsrLASNGALKVNEFLQVEgYSNIYAIGDCADTKePKMAYHAGL 300
Cdd:pfam07992 226 --VEVILKDGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDCRVGG-PELAQNAVA 299


                  ..
gi 30017355   301 HA 302
Cdd:pfam07992 300 QG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 77-309 5.04e-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: 54.57  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    77 FRQGKVI-----GIDLKNRMVLLQGG---EALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQ 143
Cdd:TIGR01350  99 LKKNKVTvikgeAKFLDPGTVSVTGEngeETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   144 FIVVvgggsagvemAAEIKTEYPE------KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEE 214
Cdd:TIGR01350 174 VIIG----------GGVIGIEFASifaslgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   215 LPRneyreYIKVETDKGTEVAT--NMVIVCNGIKINSSAY-RSAFESRLASNGALKVNEFLQVeGYSNIYAIGDCADTke 291
Cdd:TIGR01350 240 NDD-----QVTYENKGGETETLtgEKVLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDVIGG-- 311

                         250
                  ....*....|....*...
gi 30017355   292 PKMAYHAGLHANVAVANI 309
Cdd:TIGR01350 312 PMLAHVASHEGIVAAENI 329
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-372 1.63e-07

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 52.85  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   77 FRQGKVIGIDLKNRMVL----------LQGGEALPFSHLILATGSTgpfPGKFNevscqqaaIQAYEDMV---KQIQRSQ 143
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHAR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  144 FIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSRV------------PLAD------KELLPCVRQEVKEILLRKGVQLLL 205
Cdd:PTZ00318 148 GIRKRIVQCI---ERASLPTTSVEERKRLLHFVVvgggptgvefaaELADffrddvRNLNPELVEECKVTVLEAGSEVLG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  206 S--ERVSN--LEELPRNEYREYIK----------VETDKGTEVATNMVIVCNGIKINSSAYRSAFESRlaSNGALKVNEF 271
Cdd:PTZ00318 225 SfdQALRKygQRRLRRLGVDIRTKtavkevldkeVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKT--SRGRISVDDH 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355  272 LQVEGYSNIYAIGDCADTKE---PKMAYHAGLHANVAVANIVNSMKQRPL-KAYKPGALTFLLSMGRNDGVGQISGF-YV 346
Cdd:PTZ00318 303 LRVKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAFdLS 382

                        330       340
                 ....*....|....*....|....*.
gi 30017355  347 GRLMVRLAKSRDLLISTSWKTMRQSP 372
Cdd:PTZ00318 383 GFKALLFWRSAYLTILGSWRSKLYVL 408
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 81-287 1.31e-06

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 50.21  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355    81 KVIGIDLKNRMVLLQGGEALPFSHLILATGSTG---PFPGK-------FNEVScqqaAIQAYEDMVKQIQRSQFIVVVGG 150
Cdd:TIGR02374  76 TVIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPGAdkkgvyvFRTIE----DLDAIMAMAQRFKKAAVIGGGLL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   151 GsagveMAAEIKTEYPEKEVTLIHSRVPLADKELLPCVRQEVKEILLRKGVQLLLSErvsNLEELPRNEYREYIKVEtdK 230
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30017355   231 GTEVATNMVIVCNGIKINSSAyrsAFESRLASNGALKVNEFLQVEGySNIYAIGDCA 287
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTSD-PDIYAVGECA 274
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 169-308 9.15e-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: 41.25  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017355   169 EVTLIHSRVPLAdKELLPCVRQEVKEILLRKGVQLLLServSNLEELPRNEYREYIKVET-DKGTEVATNMVIVCNGIKI 247
Cdd:TIGR02053 191 EVTILQRSDRLL-PREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRGGGKIITVEKpGGQGEVEADELLVATGRRP 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017355   248 NSSAYR-SAFESRLASNGALKVNEFLQVEGySNIYAIGDCadTKEPKMAYHAGLHANVAVAN 308
Cdd:TIGR02053 267 NTDGLGlEKAGVKLDERGGILVDETLRTSN-PGIYAAGDV--TGGLQLEYVAAKEGVVAAEN 325
PLN02507 PLN02507
glutathione reductase
 210-285 1.32e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 40.57  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30017355  210 SNLEELPRNEyrEYIKVETDKGTEVATNMVIVCNGIKINSSayRSAFES---RLASNGALKVNEFLQVEgYSNIYAIGD 285
Cdd:PLN02507 265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTK--RLNLEAvgvELDKAGAVKVDEYSRTN-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.
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