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Conserved domains on  [gi|568968562|ref|XP_006514188|]
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ferroptosis suppressor protein 1 isoform X3 [Mus musculus]

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

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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];
2-266 2.76e-31

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: 119.85  E-value: 2.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGGGSAGV----------- 65
Cdd:COG1252   88 VTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFERAERRRlltivvvgggp 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  66 ---EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGVQLLLSERVSNLEELpr 127
Cdd:COG1252  160 tgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVHTGTRVTEVDAD-- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 128 neyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYSNIYAIGDCADTKE--- 202
Cdd:COG1252  233 -------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHPNVFAIGDCAAVPDpdg 300

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 203 ---PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 266
Cdd:COG1252  301 kpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
2-266 2.76e-31

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 119.85  E-value: 2.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGGGSAGV----------- 65
Cdd:COG1252   88 VTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFERAERRRlltivvvgggp 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  66 ---EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGVQLLLSERVSNLEELpr 127
Cdd:COG1252  160 tgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVHTGTRVTEVDAD-- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 128 neyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYSNIYAIGDCADTKE--- 202
Cdd:COG1252  233 -------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHPNVFAIGDCAAVPDpdg 300

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 203 ---PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 266
Cdd:COG1252  301 kpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 78-213 6.50e-15

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: 73.12  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   78 KEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyreyIKVETDKGTEVATNMVIVCNG 154
Cdd:pfam07992 176 KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG-----VEVILKDGTEIDADLVVVAIG 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568968562  155 IKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCADTKePKMAYHAGLHA 213
Cdd:pfam07992 247 RRPNTELLEAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDCRVGG-PELAQNAVAQG 301
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 66-198 6.67e-13

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 68.14  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  66 EMAAEIKTEypEKEVTLIH--SRV-PLA-DKELLPCVRQEVKEillrKGVQLLLSERVSNLEelprNEYREYiKVETDKG 141
Cdd:PRK09564 163 EAVEAAKHL--GKNVRIIQleDRIlPDSfDKEITDVMEEELRE----NGVELHLNEFVKSLI----GEDKVE-GVVTDKG 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 142 tEVATNMVIVCNGIKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCA 198
Cdd:PRK09564 232 -EYEADVVIVATGVKPNTEFLEDTGLK--TLKNGAIIVDEYGETS-IENIYAAGDCA 284
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 6-220 1.42e-08

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 55.34  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562    6 GGEALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQFIVVvgggsagvemAAEIKTEYPE--- 77
Cdd:TIGR01350 126 GEETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIG----------GGVIGIEFASifa 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   78 ---KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRneyreYIKVETDKGTEVAT--NMV 149
Cdd:TIGR01350 191 slgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEKNDD-----QVTYENKGGETETLtgEKV 261

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968562  150 IVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCADTkePKMAYHAGLHANVAVANI 220
Cdd:TIGR01350 262 LVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDVIGG--PMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
2-266 2.76e-31

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 119.85  E-value: 2.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGSTGPFPGKfnevscQQAAIQAYedMVKQIQ-----RSQFIVVVGGGSAGV----------- 65
Cdd:COG1252   88 VTLADGRTLSYDYLVIATGSVTNFFGI------PGLAEHAL--PLKTLEdalalRERLLAAFERAERRRlltivvvgggp 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  66 ---EMAAEI------KTEYPEK-----EVTLIHsrvplADKELLP----CVRQEVKEILLRKGVQLLLSERVSNLEELpr 127
Cdd:COG1252  160 tgvELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELEKRGVEVHTGTRVTEVDAD-- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 128 neyreyiKVETDKGTEVATNMVIVCNGIKINSsayrsAFAESRLASN--GALKVNEFLQVEGYSNIYAIGDCADTKE--- 202
Cdd:COG1252  233 -------GVTLEDGEEIPADTVIWAAGVKAPP-----LLADLGLPTDrrGRVLVDPTLQVPGHPNVFAIGDCAAVPDpdg 300

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 203 ---PKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAK 266
Cdd:COG1252  301 kpvPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLAWLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 2-221 1.52e-19

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: 86.40  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGST---GPFPGKFNEVSCQQAAIQAYEDMVKQIQRSQ----------FIvvvgggsaGVEMA 68
Cdd:COG0446   69 VTLRDGETLSYDKLVLATGARprpPPIPGLDLPGVFTLRTLDDADALREALKEFKgkravvigggPI--------GLELA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  69 AEIKTEypEKEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEElprneyREYIKVETDKGTEVA 145
Cdd:COG0446  141 EALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVELRLGETVVAIDG------DDKVAVTLTDGEEIP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 146 TNMVIVCNGIKINssayrSAFAES---RLASNGALKVNEFLQVeGYSNIYAIGDCADTKEP--------KMAYHAGLHAN 214
Cdd:COG0446  209 ADLVVVAPGVRPN-----TELAKDaglALGERGWIKVDETLQT-SDPDVYAAGDCAEVPHPvtgktvyiPLASAANKQGR 282


                 ....*..
gi 568968562 215 VAVANIV 221
Cdd:COG0446  283 VAAENIL 289
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 78-213 6.50e-15

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: 73.12  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   78 KEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNeyreyIKVETDKGTEVATNMVIVCNG 154
Cdd:pfam07992 176 KEVTLIEALdrlLRAFDEE----ISAALEKALEKNGVEVRLGTSVKEIIGDGDG-----VEVILKDGTEIDADLVVVAIG 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568968562  155 IKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCADTKePKMAYHAGLHA 213
Cdd:pfam07992 247 RRPNTELLEAAGLE--LDERGGIVVDEYLRTS-VPGIYAAGDCRVGG-PELAQNAVAQG 301
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 66-198 6.67e-13

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 68.14  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  66 EMAAEIKTEypEKEVTLIH--SRV-PLA-DKELLPCVRQEVKEillrKGVQLLLSERVSNLEelprNEYREYiKVETDKG 141
Cdd:PRK09564 163 EAVEAAKHL--GKNVRIIQleDRIlPDSfDKEITDVMEEELRE----NGVELHLNEFVKSLI----GEDKVE-GVVTDKG 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 142 tEVATNMVIVCNGIKINSSAYRSAFAEsrLASNGALKVNEFLQVEgYSNIYAIGDCA 198
Cdd:PRK09564 232 -EYEADVVIVATGVKPNTEFLEDTGLK--TLKNGAIIVDEYGETS-IENIYAAGDCA 284
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-198 2.79e-12

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 66.32  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGSTgPF----PGK-------FNEvscqqaaIQAYEDMVKQIQRSQ--------FIvvvgggs 62
Cdd:COG1251   89 VTLADGETLPYDKLVLATGSR-PRvppiPGAdlpgvftLRT-------LDDADALRAALAPGKrvvvigggLI------- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  63 aGVEMAAEIKTEypEKEVTLIH-SRVPLA---DKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRNEyreyiKVET 138
Cdd:COG1251  154 -GLEAAAALRKR--GLEVTVVErAPRLLPrqlDEE----AGALLQRLLEALGVEVRLGTGVTEIEGDDRVT-----GVRL 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968562 139 DKGTEVATNMVIVCNGIKINssayrSAFAE-SRLASNGALKVNEFLQVeGYSNIYAIGDCA 198
Cdd:COG1251  222 ADGEELPADLVVVAIGVRPN-----TELARaAGLAVDRGIVVDDYLRT-SDPDIYAAGDCA 276
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
2-207 8.30e-12

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 64.55  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   2 VLLQGGEALPFSHLILATGSTG---PFPGkfNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSAGVEMAAEIKTEypEK 78
Cdd:PRK04965  90 VVKSQGNQWQYDKLVLATGASAfvpPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRA--GK 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  79 EVTLI-HSRVPLADkeLLPC-VRQEVKEILLRKGVQLLLSERVSNLEELprneyREYIKVETDKGTEVATNMVIVCNGIK 156
Cdd:PRK04965 166 AVTLVdNAASLLAS--LMPPeVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLDSGRSIEVDAVIAAAGLR 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568968562 157 INSSAYRsafaESRLASNGALKVNEFLQVEGySNIYAIGDCADTKEPKMAY 207
Cdd:PRK04965 239 PNTALAR----RAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEINGQVLPF 284
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 64-222 1.71e-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: 57.79  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  64 GVEMA---AEIKTeypekEVTLIHSR---VPLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPrneyrEYIKVE 137
Cdd:COG1249  180 GLEFAqifARLGS-----EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVT 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 138 TDKGTEVATN---MVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCADtkEPKMAYHAGLHAN 214
Cdd:COG1249  246 LEDGGGEEAVeadKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGR 322


                 ....*...
gi 568968562 215 VAVANIVN 222
Cdd:COG1249  323 VAAENILG 330
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 6-220 1.42e-08

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 55.34  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562    6 GGEALPFSHLILATGS-----TGPFPGKFNEVSCQQAAIQayedmVKQIQRSQFIVVvgggsagvemAAEIKTEYPE--- 77
Cdd:TIGR01350 126 GEETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIG----------GGVIGIEFASifa 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   78 ---KEVTLIH--SRV-PLADKEllpcVRQEVKEILLRKGVQLLLSERVSNLEELPRneyreYIKVETDKGTEVAT--NMV 149
Cdd:TIGR01350 191 slgSKVTVIEmlDRIlPGEDAE----VSKVLQKALKKKGVKILTNTKVTAVEKNDD-----QVTYENKGGETETLtgEKV 261

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968562  150 IVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVeGYSNIYAIGDCADTkePKMAYHAGLHANVAVANI 220
Cdd:TIGR01350 262 LVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDVIGG--PMLAHVASHEGIVAAENI 329
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 10-283 4.70e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 47.45  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  10 LPFSHLILATGSTgpfPGKFNevscqqaaIQAYEDMV---KQIQRSQFIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSR 86
Cdd:PTZ00318 112 VPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHARGIRKRIVQCI---ERASLPTTSVEERKRLLHFV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562  87 V------------PLAD------KELLPCVRQEVKEILLRKGVQLLLSERVSNLEELPRNEYREYIKVETDKGT-EVATN 147
Cdd:PTZ00318 178 VvgggptgvefaaELADffrddvRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVkEVLDK 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562 148 MVIVCNGIKINSS--AYRSAFAESRLA--------SNGALKVNEFLQVEGYSNIYAIGDCADTKE---PKMAYHAGLHAN 214
Cdd:PTZ00318 258 EVVLKDGEVIPTGlvVWSTGVGPGPLTkqlkvdktSRGRISVDDHLRVKPIPNVFALGDCAANEErplPTLAQVASQQGV 337

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968562 215 VAVANIVNSMKQRPL-KAYKPGALTFLLSMGRNDGVGQISGF-YVGRLMVRLAKSRDLLISTSWKTMRQSP 283
Cdd:PTZ00318 338 YLAKEFNNELKGKPMsKPFVYRSLGSLAYLGNYSAIVQLGAFdLSGFKALLFWRSAYLTILGSWRSKLYVL 408
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 79-219 9.92e-05

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: 43.57  E-value: 9.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   79 EVTLIHSRVPLAdKELLPCVRQEVKEILLRKGVQLLLServSNLEELPRNEYREYIKVET-DKGTEVATNMVIVCNGIKI 157
Cdd:TIGR02053 191 EVTILQRSDRLL-PREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRGGGKIITVEKpGGQGEVEADELLVATGRRP 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568968562  158 NSSAYRSAFAESRLASNGALKVNEFLQVEGySNIYAIGDCadTKEPKMAYHAGLHANVAVAN 219
Cdd:TIGR02053 267 NTDGLGLEKAGVKLDERGGILVDETLRTSN-PGIYAAGDV--TGGLQLEYVAAKEGVVAAEN 325
PLN02507 PLN02507
glutathione reductase
 120-196 2.84e-04

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 42.11  E-value: 2.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968562 120 SNLEELPRNEyrEYIKVETDKGTEVATNMVIVCNGIKINSSAYRSAFAESRLASNGALKVNEFLQVEgYSNIYAIGD 196
Cdd:PLN02507 265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTN-IPSIWAIGD 338
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 2-198 5.15e-04

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 41.35  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562    2 VLLQGGEALPFSHLILATGSTG---PFPGK-------FNEVScqqaAIQAYEDMVKQIQRSQFIVVVGGGsagveMAAEI 71
Cdd:TIGR02374  87 VITDAGRTLSYDKLILATGSYPfilPIPGAdkkgvyvFRTIE----DLDAIMAMAQRFKKAAVIGGGLLG-----LEAAV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   72 KTEYPEKEVTLIHSRVPLADKELLPCVRQEVKEILLRKGVQLLLSErvsNLEELPRNEYREYIKVEtdKGTEVATNMVIV 151
Cdd:TIGR02374 158 GLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--DGSSLEADLIVM 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568968562  152 CNGIKINSSAYRSAfaesRLASNGALKVNEFLQVEGySNIYAIGDCA 198
Cdd:TIGR02374 233 AAGIRPNDELAVSA----GIKVNRGIIVNDSMQTSD-PDIYAVGECA 274
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 98-199 4.54e-03

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 38.42  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968562   98 VRQEVKEILLRKGVQLLLSERVSNLEELPRNEYReyikVETDKGTEVATNMVIVCNGIKINSSAYRSAFAESRLASNGAL 177
Cdd:TIGR01423 233 LRKELTKQLRANGINIMTNENPAKVTLNADGSKH----VTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAI 308

                          90       100
                  ....*....|....*....|..
gi 568968562  178 KVNEFLQVEgYSNIYAIGDCAD 199
Cdd:TIGR01423 309 QVDEFSRTN-VPNIYAIGDVTD 329
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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