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Conserved domains on  [gi|1953064408|ref|XP_038390119|]
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ferroptosis suppressor protein 1 isoform X2 [Canis lupus familiaris]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 1903257)

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 Homo sapiens ferroptosis suppressor protein and Saccharomyces cerevisiae apoptosis-inducing factor

CATH:  3.50.50.100
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  31810296

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Ndh super family cl43367
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-323 1.05e-29

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


The actual alignment was detected with superfamily member COG1252:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 117.16  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1953064408 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKP 323
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRY 335
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-323 1.05e-29

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 117.16  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1953064408 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKP 323
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRY 335
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: 59.67  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564  160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953064408 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 9.82e-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: 49.62  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  85 IDVQNQMVLLE-----DGEALPFSHLILATGStglfpgkfnqvSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGA-----------RPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 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 8.24e-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: 47.25  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953064408 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];
76-323 1.05e-29

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 117.16  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSRELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252    72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252   147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252   222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1953064408 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKP 323
Cdd:COG1252   291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRY 335
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-310 1.25e-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: 90.64  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  64 KTFISYSVTFKenfRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGST---GLFPG-KFNQVSSrelaIQAYEDMVKqv 139
Cdd:COG0446    44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGlDLPGVFT----LRTLDDADA-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 140 qrsqsvvvvgggsagveMAAEVKTEFPE----------------------KEVTLIH--SQV-ALADKEllpcVRQEAKE 194
Cdd:COG0446   115 -----------------LREALKEFKGKravvigggpiglelaealrkrgLKVTLVEraPRLlGVLDPE----MAALLEE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 195 ILLQKGVQLLLSERVSNLEDlplneyRERIQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdgHLA--SNGALRVNEYL 272
Cdd:COG0446   174 ELREHGVELRLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDA---GLAlgERGWIKVDETL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1953064408 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 2.02e-12

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 67.47  E-value: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPGkfnqVSSRELA-------IQAYEDMvkqvqrsqsvvvvgggsag 154
Cdd:COG1251    79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPP----IPGADLPgvftlrtLDDADAL------------------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 155 VEMAAEVKT-----------EFPE------KEVTLIHsqvaLADKeLLPcvRQ---EA----KEILLQKGVQLLLSERVS 210
Cdd:COG1251   136 RAALAPGKRvvvigggliglEAAAalrkrgLEVTVVE----RAPR-LLP--RQldeEAgallQRLLEALGVEVRLGTGVT 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 211 NLEDlplNEYRERiqVHTDKGTEVATNLVIVCNGIKVNSSAyhsAFDGHLASNGALRVNEYLQVeGYSHIYAIGDCADVK 290
Cdd:COG1251   209 EIEG---DDRVTG--VRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHP 279

                         250       260
                  ....*....|....*....|
gi 1953064408 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: 59.67  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564  160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953064408 229 DKGtEVATNLVIVCNGIKVNSSAYHSAfDGHLASNGALRVNEYLQVEgYSHIYAIGDCADV 289
Cdd:PRK09564  229 DKG-EYEADVVIVATGVKPNTEFLEDT-GLKTLKNGAIIVDEYGETS-IENIYAAGDCATI 286
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-296 7.42e-10

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 59.55  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  77 FRQGLVVEIDVQNQMVLLeDGEALPFSHLILATGSTGLFPgkfnQVSSRELAI-----QAYEDMVKQVQRSQSVVVVGGG 151
Cdd:PRK04965   76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAFVP----PIPGRELMLtlnsqQEYRAAETQLRDAQRVLVVGGG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 152 SAGVEMAAEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSERVSNledlpLNEYRERIQVHTDKG 231
Cdd:PRK04965  151 LIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQG-----LEKTDSGIRATLDSG 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953064408 232 TEVATNLVIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCADVKEPKMAY 296
Cdd:PRK04965  224 RSIEVDAVIAAAGLRPNTALARRA---GLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 154-311 9.40e-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: 56.25  E-value: 9.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 154 GVEMA-------AevktefpekEVTLIHSQ---VALADKEllpcVRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:COG1249   180 GLEFAqifarlgS---------EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DG 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 224 IQVHTDKGTEVATN---LVIVCNGIKVNSsayhsafDG--------HLASNGALRVNEYLQVeGYSHIYAIGDCADvkEP 292
Cdd:COG1249   242 VTVTLEDGGGEEAVeadKVLVATGRRPNT-------DGlgleaagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GP 311

                         170
                  ....*....|....*....
gi 1953064408 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 9.82e-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: 49.62  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  85 IDVQNQMVLLE-----DGEALPFSHLILATGStglfpgkfnqvSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGA-----------RPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 224 IQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdG-HLASNGALRVNEYLQVEgYSHIYAIGDCaDVKEPKMAYHAGLHA 302
Cdd:pfam07992 226 VEVILKDGTEIDADLVVVAIGRRPNTELLEAA--GlELDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-291 1.62e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 49.38  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  77 FRQGLVVEIDVQNQMVL----------LEDGEALPFSHLILATGSTglfPGKFNqvssrelaIQAYEDMVKQVQRSQSVV 146
Cdd:PTZ00318   79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAFFLKEVNHAR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 147 VVGGGSAGVEMAAEVKTEFPEKEVTLIHSQVA------------LAD------KELLPCVRQEAKEILLQKGVQLLLS-- 206
Cdd:PTZ00318  148 GIRKRIVQCIERASLPTTSVEERKRLLHFVVVgggptgvefaaeLADffrddvRNLNPELVEECKVTVLEAGSEVLGSfd 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 207 ERVSNLEDLPLNEYRERIQVH------------TDKGTEVATNLVIVCNGIKVNSSAYHSAFDGhlASNGALRVNEYLQV 274
Cdd:PTZ00318  228 QALRKYGQRRLRRLGVDIRTKtavkevldkevvLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDK--TSRGRISVDDHLRV 305

                         250
                  ....*....|....*..
gi 1953064408 275 EGYSHIYAIGDCADVKE 291
Cdd:PTZ00318  306 KPIPNVFALGDCAANEE 322
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 188-309 8.24e-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: 47.25  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953064408 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 3.91e-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: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408  82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLF---PGKFNQVSSRELAIQAYEDMVKQVQRSQSVVVVGGGSAGVEMA 158
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPFIlpiPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 159 AEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSErvsNLEDLPLNEYRERIqvHTDKGTEVATNL 238
Cdd:TIGR02374 157 VGLQNL--GMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRI--RFKDGSSLEADL 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953064408 239 VIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCA 287
Cdd:TIGR02374 230 IVMAAGIRPNDELAVSA---GIKVNRGIIVNDSMQTSD-PDIYAVGECA 274
PRK07251 PRK07251
FAD-containing oxidoreductase;
169-285 2.08e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 39.73  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953064408 169 EVTLIHSQVALADKELlPCVRQEAKEILLQKGVQLLLSERVSNLEdlplNEyRERIQVHTDKGTEvATNLVIVCNGIKVN 248
Cdd:PRK07251  182 KVTVLDAASTILPREE-PSVAALAKQYMEEDGITFLLNAHTTEVK----ND-GDQVLVVTEDETY-RFDALLYATGRKPN 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953064408 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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