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Conserved domains on  [gi|1953381193|ref|XP_038518740|]
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ferroptosis suppressor protein 1 isoform X1 [Canis lupus familiaris]

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];
76-355 1.52e-35

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 133.72  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953381193 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKPGALTFLLAMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 1.52e-35

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 133.72  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953381193 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKPGALTFLLAMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 153-289 7.24e-10

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 60.05  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564  160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953381193 229 DKGtEVATNLVIVCNGIKVNSSAYHSAfDGHLASNGALRVNEYLQVEgYSHIYAIGDCADV 289
Cdd:PRK09564  229 DKG-EYEADVVIVATGVKPNTEFLEDT-GLKTLKNGAIIVDEYGETS-IENIYAAGDCATI 286
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 8.62e-07

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: 50.01  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  85 IDVQNQMVLLE-----DGEALPFSHLILATGStglfpgkfnqvSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGA-----------RPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 224 IQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdG-HLASNGALRVNEYLQVEgYSHIYAIGDCaDVKEPKMAYHAGLHA 302
Cdd:pfam07992 226 VEVILKDGTEIDADLVVVAIGRRPNTELLEAA--GlELDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 188-309 7.16e-06

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: 47.64  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953381193 264 GALRVNEYLQVeGYSHIYAIGDCADvkEPKMAYHAGLHASVAVANI 309
Cdd:TIGR01350 287 GRIVVDEYMRT-NVPGIYAIGDVIG--GPMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 1.52e-35

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 133.72  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953381193 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKPGALTFLLAMGRNDGVGQISGFYVGRLMVRLAK 355
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-310 1.26e-20

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: 91.41  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  64 KTFISYSVTFKenfRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGST---GLFPG-KFNQVSSrelaIQAYEDMVKqv 139
Cdd:COG0446    44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGlDLPGVFT----LRTLDDADA-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 140 qrsqsvvvvgggsagveMAAEVKTEFPE----------------------KEVTLIH--SQV-ALADKEllpcVRQEAKE 194
Cdd:COG0446   115 -----------------LREALKEFKGKravvigggpiglelaealrkrgLKVTLVEraPRLlGVLDPE----MAALLEE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 195 ILLQKGVQLLLSERVSNLEDlplneyRERIQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdgHLA--SNGALRVNEYL 272
Cdd:COG0446   174 ELREHGVELRLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDA---GLAlgERGWIKVDETL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1953381193 273 QVeGYSHIYAIGDCADVKEP--------KMAYHAGLHASVAVANIV 310
Cdd:COG0446   245 QT-SDPDVYAAGDCAEVPHPvtgktvyiPLASAANKQGRVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
82-310 2.22e-12

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 67.86  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPGkfnqVSSRELA-------IQAYEDMvkqvqrsqsvvvvgggsag 154
Cdd:COG1251    79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPP----IPGADLPgvftlrtLDDADAL------------------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 155 VEMAAEVKT-----------EFPE------KEVTLIHsqvaLADKeLLPcvRQ---EA----KEILLQKGVQLLLSERVS 210
Cdd:COG1251   136 RAALAPGKRvvvigggliglEAAAalrkrgLEVTVVE----RAPR-LLP--RQldeEAgallQRLLEALGVEVRLGTGVT 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 211 NLEDlplNEYRERiqVHTDKGTEVATNLVIVCNGIKVNSSAyhsAFDGHLASNGALRVNEYLQVeGYSHIYAIGDCADVK 290
Cdd:COG1251   209 EIEG---DDRVTG--VRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHP 279

                         250       260
                  ....*....|....*....|
gi 1953381193 291 EPkmayHAGLHASVAVANIV 310
Cdd:COG1251   280 GP----VYGRRVLELVAPAY 295
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 153-289 7.24e-10

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 60.05  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564  160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953381193 229 DKGtEVATNLVIVCNGIKVNSSAYHSAfDGHLASNGALRVNEYLQVEgYSHIYAIGDCADV 289
Cdd:PRK09564  229 DKG-EYEADVVIVATGVKPNTEFLEDT-GLKTLKNGAIIVDEYGETS-IENIYAAGDCATI 286
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-296 7.51e-10

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 59.93  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  77 FRQGLVVEIDVQNQMVLLeDGEALPFSHLILATGSTGLFPgkfnQVSSRELAI-----QAYEDMVKQVQRSQSVVVVGGG 151
Cdd:PRK04965   76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAFVP----PIPGRELMLtlnsqQEYRAAETQLRDAQRVLVVGGG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 152 SAGVEMAAEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSERVSNledlpLNEYRERIQVHTDKG 231
Cdd:PRK04965  151 LIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQG-----LEKTDSGIRATLDSG 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953381193 232 TEVATNLVIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCADVKEPKMAY 296
Cdd:PRK04965  224 RSIEVDAVIAAAGLRPNTALARRA---GLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 154-311 7.43e-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: 57.02  E-value: 7.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 154 GVEMA-------AevktefpekEVTLIHSQ---VALADKEllpcVRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:COG1249   180 GLEFAqifarlgS---------EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DG 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 224 IQVHTDKGTEVATN---LVIVCNGIKVNSsayhsafDG--------HLASNGALRVNEYLQVeGYSHIYAIGDCADvkEP 292
Cdd:COG1249   242 VTVTLEDGGGEEAVeadKVLVATGRRPNT-------DGlgleaagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GP 311

                         170
                  ....*....|....*....
gi 1953381193 293 KMAYHAGLHASVAVANIVN 311
Cdd:COG1249   312 QLAHVASAEGRVAAENILG 330
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 8.62e-07

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: 50.01  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  85 IDVQNQMVLLE-----DGEALPFSHLILATGStglfpgkfnqvSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGA-----------RPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 224 IQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdG-HLASNGALRVNEYLQVEgYSHIYAIGDCaDVKEPKMAYHAGLHA 302
Cdd:pfam07992 226 VEVILKDGTEIDADLVVVAIGRRPNTELLEAA--GlELDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-344 1.79e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 49.38  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  77 FRQGLVVEIDVQNQMVL----------LEDGEALPFSHLILATGSTglfPGKFNqvssrelaIQAYEDMVKQVQRSQSVV 146
Cdd:PTZ00318   79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAFFLKEVNHAR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 147 VVGGGSAGVEMAAEVKTEFPEKEVTLIHSQVA------------LAD------KELLPCVRQEAKEILLQKGVQLLLS-- 206
Cdd:PTZ00318  148 GIRKRIVQCIERASLPTTSVEERKRLLHFVVVgggptgvefaaeLADffrddvRNLNPELVEECKVTVLEAGSEVLGSfd 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 207 ERVSNLEDLPLNEYRERIQVH------------TDKGTEVATNLVIVCNGIKVNSSAYHSAFDGhlASNGALRVNEYLQV 274
Cdd:PTZ00318  228 QALRKYGQRRLRRLGVDIRTKtavkevldkevvLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDK--TSRGRISVDDHLRV 305

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953381193 275 EGYSHIYAIGDCADVKE---PKMAYHAGLHASVAVANIVNSRKQRPL-KAYKPGALTFLLAMGRNDGVGQISGF 344
Cdd:PTZ00318  306 KPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAF 379
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 188-309 7.16e-06

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: 47.64  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953381193 264 GALRVNEYLQVeGYSHIYAIGDCADvkEPKMAYHAGLHASVAVANI 309
Cdd:TIGR01350 287 GRIVVDEYMRT-NVPGIYAIGDVIG--GPMLAHVASHEGIVAAENI 329
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-287 4.24e-05

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 45.59  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193  82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLF---PGKFNQVSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVEMA 158
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPFIlpiPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 159 AEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSErvsNLEDLPLNEYRERIqvHTDKGTEVATNL 238
Cdd:TIGR02374 157 VGLQNL--GMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRI--RFKDGSSLEADL 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953381193 239 VIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCA 287
Cdd:TIGR02374 230 IVMAAGIRPNDELAVSA---GIKVNRGIIVNDSMQTSD-PDIYAVGECA 274
PRK07251 PRK07251
FAD-containing oxidoreductase;
169-285 2.10e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 39.73  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953381193 169 EVTLIHSQVALADKELlPCVRQEAKEILLQKGVQLLLSERVSNLEdlplNEyRERIQVHTDKGTEvATNLVIVCNGIKVN 248
Cdd:PRK07251  182 KVTVLDAASTILPREE-PSVAALAKQYMEEDGITFLLNAHTTEVK----ND-GDQVLVVTEDETY-RFDALLYATGRKPN 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953381193 249 SSAYH-SAFDGHLASNGALRVNEYLQ--VEGyshIYAIGD 285
Cdd:PRK07251  255 TEPLGlENTDIELTERGAIKVDDYCQtsVPG---VFAVGD 291
 
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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