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Conserved domains on  [gi|545495127|ref|XP_005619028|]
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ferroptosis suppressor protein 1 isoform X3 [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 1.13e-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: 117.93  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSWELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252  147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252  222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 545495127 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 1.13e-29

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 117.93  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSWELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252  147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252  222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 545495127 285 DCADVKE------PKMAYHAGLHASVAVANIVNSRKQRPLKAYKP 323
Cdd:COG1252  291 DCAAVPDpdgkpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRY 335
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 153-289 4.77e-10

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 60.82  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564 160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545495127 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 1.80e-06

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: 49.24  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127   19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127   85 IDVQNQMVLLE-----DGEALPFSHLILATGSTGLFPGkfnqvsswelaIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPP-----------IPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  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 6.29e-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: 48.02  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 545495127  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 1.13e-29

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 117.93  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  76 NFRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPG-----------KfnqvsSWELAIQAYEDMVKQVQRSQS 144
Cdd:COG1252   72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGipglaehalplK-----TLEDALALRERLLAAFERAER 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 145 VVVVGGG-----SAGVEMAAEVKTEFPEK-----------EVTLIHsqvalADKELLP----CVRQEAKEILLQKGVQLL 204
Cdd:COG1252  147 RRLLTIVvvgggPTGVELAGELAELLRKLlrypgidpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVH 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 205 LSERVSNLEDlplneyrERiqVHTDKGTEVATNLVIVCNGIKVNSSAYHSAFDghLASNGALRVNEYLQVEGYSHIYAIG 284
Cdd:COG1252  222 TGTRVTEVDA-------DG--VTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGHPNVFAIG 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 545495127 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 5.79e-21

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: 92.57  E-value: 5.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  64 KTFISYSVTFKenfRQGLVVEIDVQNQMVLLEDGEALPFSHLILATGST---GLFPGkfnqvssWELA----IQAYEDMV 136
Cdd:COG0446   44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPG-------LDLPgvftLRTLDDAD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 137 KqvqrsqsvvvvgggsagveMAAEVKTEFPE----------------------KEVTLIH--SQV-ALADKEllpcVRQE 191
Cdd:COG0446  114 A-------------------LREALKEFKGKravvigggpiglelaealrkrgLKVTLVEraPRLlGVLDPE----MAAL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 192 AKEILLQKGVQLLLSERVSNLEDlplneyRERIQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdgHLA--SNGALRVN 269
Cdd:COG0446  171 LEEELREHGVELRLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDA---GLAlgERGWIKVD 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 545495127 270 EYLQVeGYSHIYAIGDCADVKEP--------KMAYHAGLHASVAVANIV 310
Cdd:COG0446  242 ETLQT-SDPDVYAAGDCAEVPHPvtgktvyiPLASAANKQGRVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
82-310 2.21e-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: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLFPGkfnqVSSWELA-------IQAYEDMvkqvqrsqsvvvvgggsag 154
Cdd:COG1251   79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPP----IPGADLPgvftlrtLDDADAL------------------- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 155 VEMAAEVKT-----------EFPE------KEVTLIHsqvaLADKeLLPcvRQ---EA----KEILLQKGVQLLLSERVS 210
Cdd:COG1251  136 RAALAPGKRvvvigggliglEAAAalrkrgLEVTVVE----RAPR-LLP--RQldeEAgallQRLLEALGVEVRLGTGVT 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 211 NLEDlplNEYRERiqVHTDKGTEVATNLVIVCNGIKVNSSAyhsAFDGHLASNGALRVNEYLQVeGYSHIYAIGDCADVK 290
Cdd:COG1251  209 EIEG---DDRVTG--VRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHP 279

                        250       260
                 ....*....|....*....|
gi 545495127 291 EPkmayHAGLHASVAVANIV 310
Cdd:COG1251  280 GP----VYGRRVLELVAPAY 295
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 153-289 4.77e-10

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 60.82  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 153 AGVEMAAEVKTEfpEKEVTLI-HSQVALA---DKELLPCVRQEAKEillqKGVQLLLSERVSNLedlpLNEYRERIqVHT 228
Cdd:PRK09564 160 IGLEAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSL----IGEDKVEG-VVT 228

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545495127 229 DKGtEVATNLVIVCNGIKVNSSAYHSAfDGHLASNGALRVNEYLQVEgYSHIYAIGDCADV 289
Cdd:PRK09564 229 DKG-EYEADVVIVATGVKPNTEFLEDT-GLKTLKNGAIIVDEYGETS-IENIYAAGDCATI 286
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 154-311 6.04e-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: 57.40  E-value: 6.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 154 GVEMA-------AevktefpekEVTLIHSQ---VALADKEllpcVRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:COG1249  180 GLEFAqifarlgS---------EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DG 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 224 IQVHTDKGTEVATN---LVIVCNGIKVNSsayhsafDG--------HLASNGALRVNEYLQVeGYSHIYAIGDCADvkEP 292
Cdd:COG1249  242 VTVTLEDGGGEEAVeadKVLVATGRRPNT-------DGlgleaagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GP 311

                        170
                 ....*....|....*....
gi 545495127 293 KMAYHAGLHASVAVANIVN 311
Cdd:COG1249  312 QLAHVASAEGRVAAENILG 330
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-296 9.66e-09

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 56.46  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  77 FRQGLVVEIDVQNQMVLLeDGEALPFSHLILATGSTGLFPgkfnQVSSWELAI-----QAYEDMVKQVQRSQSVVVVGGG 151
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKS-QGNQWQYDKLVLATGASAFVP----PIPGRELMLtlnsqQEYRAAETQLRDAQRVLVVGGG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 152 SAGVEMAAEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSERVSNledlpLNEYRERIQVHTDKG 231
Cdd:PRK04965 151 LIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQG-----LEKTDSGIRATLDSG 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545495127 232 TEVATNLVIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCADVKEPKMAY 296
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTALARRA---GLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.80e-06

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: 49.24  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127   19 GGFGGIAAASQLQTLNIPFMLVDMKDSFHHN----VAALRASVESGFAKKTFISYSVTFKEN---FRQGL-------VVE 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEEVvkkLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127   85 IDVQNQMVLLE-----DGEALPFSHLILATGSTGLFPGkfnqvsswelaIQAYEDMVKQVQRSQSVVVVGGGSAGVE--- 156
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPP-----------IPGVELNVGFLVRTLDSAEALRLKLLPKrvv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  157 ---------MAAEVKTEFPeKEVTLIHsqvalADKELLPC----VRQEAKEILLQKGVQLLLSERVSNLEDLPlneyrER 223
Cdd:pfam07992 157 vvgggyigvELAAALAKLG-KEVTLIE-----ALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDG-----DG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  224 IQVHTDKGTEVATNLVIVCNGIKVNSSAYHSAfdG-HLASNGALRVNEYLQVEgYSHIYAIGDCaDVKEPKMAYHAGLHA 302
Cdd:pfam07992 226 VEVILKDGTEIDADLVVVAIGRRPNTELLEAA--GlELDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-291 2.68e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 48.99  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  77 FRQGLVVEIDVQNQMVL----------LEDGEALPFSHLILATGSTglfPGKFNqvsswelaIQAYEDMVKQVQRSQSVV 146
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAFFLKEVNHAR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 147 VVGGGSAGVEMAAEVKTEFPEKEVTLIHSQVA------------LAD------KELLPCVRQEAKEILLQKGVQLLLS-- 206
Cdd:PTZ00318 148 GIRKRIVQCIERASLPTTSVEERKRLLHFVVVgggptgvefaaeLADffrddvRNLNPELVEECKVTVLEAGSEVLGSfd 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 207 ERVSNLEDLPLNEYRERIQVH------------TDKGTEVATNLVIVCNGIKVNSSAYHSAFDGhlASNGALRVNEYLQV 274
Cdd:PTZ00318 228 QALRKYGQRRLRRLGVDIRTKtavkevldkevvLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDK--TSRGRISVDDHLRV 305

                        250
                 ....*....|....*..
gi 545495127 275 EGYSHIYAIGDCADVKE 291
Cdd:PTZ00318 306 KPIPNVFALGDCAANEE 322
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 188-309 6.29e-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: 48.02  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  188 VRQEAKEILLQKGVQLLLSERVSNLEDlplNEYRERIQVhtdKGTEVAT---NLVIVCNGIKVNSSAYHSAFDG-HLASN 263
Cdd:TIGR01350 213 VSKVLQKALKKKGVKILTNTKVTAVEK---NDDQVTYEN---KGGETETltgEKVLVAVGRKPNTEGLGLEKLGvELDER 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 545495127  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 6.39e-05

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 45.20  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127   82 VVEIDVQNQMVLLEDGEALPFSHLILATGSTGLF---PGKFNQVSSWELAIQAYEDMVKQVQRSQSVVVVGGGSAGVEMA 158
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPFIlpiPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127  159 AEVKTEfpEKEVTLIHSQVALADKELLPCVRQEAKEILLQKGVQLLLSErvsNLEDLPLNEYRERIqvHTDKGTEVATNL 238
Cdd:TIGR02374 157 VGLQNL--GMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRI--RFKDGSSLEADL 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 545495127  239 VIVCNGIKVNSSAYHSAfdgHLASNGALRVNEYLQVEGySHIYAIGDCA 287
Cdd:TIGR02374 230 IVMAAGIRPNDELAVSA---GIKVNRGIIVNDSMQTSD-PDIYAVGECA 274
PRK07251 PRK07251
FAD-containing oxidoreductase;
169-285 1.51e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 40.50  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545495127 169 EVTLIHSQVALADKELlPCVRQEAKEILLQKGVQLLLSERVSNLEdlplNEyRERIQVHTDKGTEvATNLVIVCNGIKVN 248
Cdd:PRK07251 182 KVTVLDAASTILPREE-PSVAALAKQYMEEDGITFLLNAHTTEVK----ND-GDQVLVVTEDETY-RFDALLYATGRKPN 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 545495127 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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