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Conserved domains on  [gi|1965217578|ref|XP_039014453|]
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alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial-like isoform X1 [Hibiscus syriacus]

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];
1-336 1.88e-63

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 206.14  E-value: 1.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 230 lesQILEADLVLWTVGSKA--LLPELEpcdkpheLPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQV 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADLG-------LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309

                         330       340
                  ....*....|....*....|....*....
gi 1965217578 308 AFQQADFAGWNLWAAINNRPLLPFRFQNL 336
Cdd:COG1252   310 AVQQAKVLAKNIAALLRGKPLKPFRYRDK 338
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-336 1.88e-63

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 206.14  E-value: 1.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 230 lesQILEADLVLWTVGSKA--LLPELEpcdkpheLPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQV 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADLG-------LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309

                         330       340
                  ....*....|....*....|....*....
gi 1965217578 308 AFQQADFAGWNLWAAINNRPLLPFRFQNL 336
Cdd:COG1252   310 AVQQAKVLAKNIAALLRGKPLKPFRYRDK 338
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-312 4.43e-20

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: 88.91  E-value: 4.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLA---------NTGVQFLQD--KVKILHpsdhwgmnGHKQSSCGGTVLlESGLLIEYD 69
Cdd:pfam07992  41 VLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGteVVSIDP--------GAKKVVLEELVD-GDGETITYD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  70 WLVLALGVEAKLDVVQGALEFA-LPFSTLDDACKVNKKLrTLERmkfgkdslicVAVVGCGYSGVELAATISERLQDRGI 148
Cdd:pfam07992 112 RLVIATGARPRLPPIPGVELNVgFLVRTLDSAEALRLKL-LPKR----------VVVVGGGYIGVELAAALAKLGKEVTL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 149 VQAinvETTICPTAPAGNREAALKVLSSRKVQLLLGYFVRcvrrvtdmetsgdaTVKREGKDIAESNSEKyvldlqpaek 228
Cdd:pfam07992 181 IEA---LDRLLRAFDEEISAALEKALEKNGVEVRLGTSVK--------------EIIGDGDGVEVILKDG---------- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 229 glesQILEADLVLWTVGSKALLPELEPCDkpheLPLNARGQAETDETLRVKgHPRIFAIGDssslrdsAGRLLPATAQVA 308
Cdd:pfam07992 234 ----TEIDADLVVVAIGRRPNTELLEAAG----LELDERGGIVVDEYLRTS-VPGIYAAGD-------CRVGGPELAQNA 297


                  ....
gi 1965217578 309 FQQA 312
Cdd:pfam07992 298 VAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 23-336 3.87e-19

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 87.51  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  23 LANTGVQFLQDKVKILHPSDhwgmnghKQSSCGGTVLLESGLL----IEYDWLVLALGVEAKLDVVQGALEFALPFSTLD 98
Cdd:PTZ00318   72 LAKLPNRYLRAVVYDVDFEE-------KRVKCGVVSKSNNANVntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVN 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  99 DACKVNKKL-RTLERMKFG------KDSLICVAVVGCGYSGVELAATISERLQDrgivQAINVETTICPTAPAGNREAAL 171
Cdd:PTZ00318  145 HARGIRKRIvQCIERASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFFRD----DVRNLNPELVEECKVTVLEAGS 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 172 KVLSSrkvqlllgyFVRCVRRVTDMEtsgdatVKREGKDIAESNSEKYVLDLQPAEKglESQILEADLVLWT--VGSKAL 249
Cdd:PTZ00318  221 EVLGS---------FDQALRKYGQRR------LRRLGVDIRTKTAVKEVLDKEVVLK--DGEVIPTGLVVWStgVGPGPL 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 250 LPELePCDKphelplNARGQAETDETLRVKGHPRIFAIGDSSSLRDsagRLLPATAQVAFQQADFAGWNLWAAINNRPLL 329
Cdd:PTZ00318  284 TKQL-KVDK------TSRGRISVDDHLRVKPIPNVFALGDCAANEE---RPLPTLAQVASQQGVYLAKEFNNELKGKPMS 353


                  ....*...
gi 1965217578 330 -PFRFQNL 336
Cdd:PTZ00318  354 kPFVYRSL 361
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-336 1.88e-63

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 206.14  E-value: 1.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 230 lesQILEADLVLWTVGSKA--LLPELEpcdkpheLPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQV 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADLG-------LPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309

                         330       340
                  ....*....|....*....|....*....
gi 1965217578 308 AFQQADFAGWNLWAAINNRPLLPFRFQNL 336
Cdd:COG1252   310 AVQQAKVLAKNIAALLRGKPLKPFRYRDK 338
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-312 4.43e-20

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: 88.91  E-value: 4.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLA---------NTGVQFLQD--KVKILHpsdhwgmnGHKQSSCGGTVLlESGLLIEYD 69
Cdd:pfam07992  41 VLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGteVVSIDP--------GAKKVVLEELVD-GDGETITYD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  70 WLVLALGVEAKLDVVQGALEFA-LPFSTLDDACKVNKKLrTLERmkfgkdslicVAVVGCGYSGVELAATISERLQDRGI 148
Cdd:pfam07992 112 RLVIATGARPRLPPIPGVELNVgFLVRTLDSAEALRLKL-LPKR----------VVVVGGGYIGVELAAALAKLGKEVTL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 149 VQAinvETTICPTAPAGNREAALKVLSSRKVQLLLGYFVRcvrrvtdmetsgdaTVKREGKDIAESNSEKyvldlqpaek 228
Cdd:pfam07992 181 IEA---LDRLLRAFDEEISAALEKALEKNGVEVRLGTSVK--------------EIIGDGDGVEVILKDG---------- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 229 glesQILEADLVLWTVGSKALLPELEPCDkpheLPLNARGQAETDETLRVKgHPRIFAIGDssslrdsAGRLLPATAQVA 308
Cdd:pfam07992 234 ----TEIDADLVVVAIGRRPNTELLEAAG----LELDERGGIVVDEYLRTS-VPGIYAAGD-------CRVGGPELAQNA 297


                  ....
gi 1965217578 309 FQQA 312
Cdd:pfam07992 298 VAQG 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 23-336 3.87e-19

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 87.51  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  23 LANTGVQFLQDKVKILHPSDhwgmnghKQSSCGGTVLLESGLL----IEYDWLVLALGVEAKLDVVQGALEFALPFSTLD 98
Cdd:PTZ00318   72 LAKLPNRYLRAVVYDVDFEE-------KRVKCGVVSKSNNANVntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVN 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  99 DACKVNKKL-RTLERMKFG------KDSLICVAVVGCGYSGVELAATISERLQDrgivQAINVETTICPTAPAGNREAAL 171
Cdd:PTZ00318  145 HARGIRKRIvQCIERASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFFRD----DVRNLNPELVEECKVTVLEAGS 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 172 KVLSSrkvqlllgyFVRCVRRVTDMEtsgdatVKREGKDIAESNSEKYVLDLQPAEKglESQILEADLVLWT--VGSKAL 249
Cdd:PTZ00318  221 EVLGS---------FDQALRKYGQRR------LRRLGVDIRTKTAVKEVLDKEVVLK--DGEVIPTGLVVWStgVGPGPL 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 250 LPELePCDKphelplNARGQAETDETLRVKGHPRIFAIGDSSSLRDsagRLLPATAQVAFQQADFAGWNLWAAINNRPLL 329
Cdd:PTZ00318  284 TKQL-KVDK------TSRGRISVDDHLRVKPIPNVFALGDCAANEE---RPLPTLAQVASQQGVYLAKEFNNELKGKPMS 353


                  ....*...
gi 1965217578 330 -PFRFQNL 336
Cdd:PTZ00318  354 kPFVYRSL 361
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 57-319 2.31e-15

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: 75.62  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  57 TVLLESGLLIEYDWLVLALGVEAKLDVVQGA-LEFALPFSTLDDACKVNKKLRTLErmkfGKDslicVAVVGCGYSGVEL 135
Cdd:COG0446    68 TVTLRDGETLSYDKLVLATGARPRPPPIPGLdLPGVFTLRTLDDADALREALKEFK----GKR----AVVIGGGPIGLEL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 136 AATiserLQDRGI-VQAINVETTICPTAPAGNREAALKVLSSRKVQLLLGYfvrcvrRVTDMETSGDATVKREGKdiaes 214
Cdd:COG0446   140 AEA----LRKRGLkVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGE------TVVAIDGDDKVAVTLTDG----- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 215 nsekyvldlqpaekglesQILEADLVLWTVGskaLLPELEPCDKPHeLPLNARGQAETDETLRVkGHPRIFAIGDSSSLR 294
Cdd:COG0446   205 ------------------EEIPADLVVVAPG---VRPNTELAKDAG-LALGERGWIKVDETLQT-SDPDVYAAGDCAEVP 261

                         250       260
                  ....*....|....*....|....*..
gi 1965217578 295 D--SAGRLLPATAQVAFQQADFAGWNL 319
Cdd:COG0446   262 HpvTGKTVYIPLASAANKQGRVAAENI 288
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
1-319 3.19e-10

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 60.54  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578   1 MLYELLSGEVDDWEIAPRFSELLANTGVQF-LQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEA 79
Cdd:COG1251    44 PLSKVLAGETDEEDLLLRPADFYEENGIDLrLGTRVTAIDRAAR-------------TVTLADGETLPYDKLVLATGSRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  80 -KLDVVQGALEFALPFSTLDDAckvnKKLRtlERMKFGKDslicVAVVGCGYSGVELAATiserLQDRGivqainVETTI 158
Cdd:COG1251   111 rVPPIPGADLPGVFTLRTLDDA----DALR--AALAPGKR----VVVIGGGLIGLEAAAA----LRKRG------LEVTV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 159 CPTAP------AGNREAAL--KVLSSRKVQLLLGYFVRCVR---RVTDMETSgDATVkregkdiaesnsekyvldlqpae 227
Cdd:COG1251   171 VERAPrllprqLDEEAGALlqRLLEALGVEVRLGTGVTEIEgddRVTGVRLA-DGEE----------------------- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 228 kglesqiLEADLVLWTVGSKallPELE-------PCDkphelplnaRGqAETDETLRVkGHPRIFAIGDSSSLRD-SAGR 299
Cdd:COG1251   227 -------LPADLVVVAIGVR---PNTElaraaglAVD---------RG-IVVDDYLRT-SDPDIYAAGDCAEHPGpVYGR 285

                         330       340
                  ....*....|....*....|
gi 1965217578 300 LLPATAQVAFQQADFAGWNL 319
Cdd:COG1251   286 RVLELVAPAYEQARVAAANL 305
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 123-331 1.49e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 55.57  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 123 VAVVGCGYSGVELAATISeRLqdrGI-VQAINVETTICPTAPAGNREAALKVLsSRKVQLLLGYfvrcvrRVTDMETSGD 201
Cdd:PRK06292  172 LAVIGGGVIGLELGQALS-RL---GVkVTVFERGDRILPLEDPEVSKQAQKIL-SKEFKIKLGA------KVTSVEKSGD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 202 ATVKREgkdiaesnsekyvldlqpaEKGLESQILEADLVLWTVGSKALLPELepcdKPHEL--PLNARGQAETDETLRvK 279
Cdd:PRK06292  241 EKVEEL-------------------EKGGKTETIEADYVLVATGRRPNTDGL----GLENTgiELDERGRPVVDEHTQ-T 296

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1965217578 280 GHPRIFAIGDSsslrdSAGRLLpatAQVAFQQADFAGWNLWAAIN---NRPLLPF 331
Cdd:PRK06292  297 SVPGIYAAGDV-----NGKPPL---LHEAADEGRIAAENAAGDVAggvRYHPIPS 343
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 123-319 1.37e-07

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: 52.78  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 123 VAVVGCGYSGVELAA---------TISERLqDRgivqainvettICPTAPAGNREAALKVLSSRKVQLLLGYfvrcvrRV 193
Cdd:COG1249   171 LVVIGGGYIGLEFAQifarlgsevTLVERG-DR-----------LLPGEDPEISEALEKALEKEGIDILTGA------KV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 194 TDMETSGDatvkregkdiaesnseKYVLDLqpaEKGLESQILEADLVLWTVGSKALLPELEPcdkphE---LPLNARGQA 270
Cdd:COG1249   233 TSVEKTGD----------------GVTVTL---EDGGGEEAVEADKVLVATGRRPNTDGLGL-----EaagVELDERGGI 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1965217578 271 ETDETLRVkGHPRIFAIGdssslrDSAGRllPATAQVAFQQADFAGWNL 319
Cdd:COG1249   289 KVDEYLRT-SVPGIYAIG------DVTGG--PQLAHVASAEGRVAAENI 328
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 123-315 1.45e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 46.29  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 123 VAVVGCGYSGVELAatiserlqdrGIVQAINVETTIC-------PTAPAGNREAALKVLSSRKVQLLLGYFVRCVrrvtd 195
Cdd:PRK06416  175 LVVIGGGYIGVEFA----------SAYASLGAEVTIVealprilPGEDKEISKLAERALKKRGIKIKTGAKAKKV----- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 196 METSGDATVKregkdiaesnsekyvldlqpAEKGLESQILEADLVLWTVGSKallPELEpcdkphELPLNA------RGQ 269
Cdd:PRK06416  240 EQTDDGVTVT--------------------LEDGGKEETLEADYVLVAVGRR---PNTE------NLGLEElgvktdRGF 290

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1965217578 270 AETDETLRvKGHPRIFAIGDSsslrdSAGrllPATAQVAFQQADFA 315
Cdd:PRK06416  291 IEVDEQLR-TNVPNIYAIGDI-----VGG---PMLAHKASAEGIIA 327
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 58-300 3.14e-04

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 42.22  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578  58 VLLESGLLIEYDWLVLALGVEAK-LDVVQGALEFALPFSTLDDACKVNKKLRTLERmkfgkdslicVAVVGCGYSGVELA 136
Cdd:PRK09754   91 LVLTNGESWHWDQLFIATGAAARpLPLLDALGERCFTLRHAGDAARLREVLQPERS----------VVIVGAGTIGLELA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 137 ATISERlqdRGIVQAINVETTIC-PTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvTDMETSGDAtvkregkdiaesn 215
Cdd:PRK09754  161 ASATQR---RCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---------NAIEHVVDG------------- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217578 216 sEKYVLDLQPAEKglesqiLEADLVLWTVGSKALlpelepcDK-PHELPLNARGQAETDETLRVkGHPRIFAIGDSSSLR 294
Cdd:PRK09754  216 -EKVELTLQSGET------LQADVVIYGIGISAN-------DQlAREANLDTANGIVIDEACRT-CDPAIFAGGDVAITR 280


                  ....*.
gi 1965217578 295 DSAGRL 300
Cdd:PRK09754  281 LDNGAL 286
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 231-289 1.60e-03

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 40.12  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1965217578 231 ESQILEADLVLWTVGSKallPELEPCDKPHELPLNARGQAETDETLRVKGHPRIFAIGD 289
Cdd:COG0493   354 SEFTLPADLVILAIGQT---PDPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGD 409
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 224-289 6.82e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.32  E-value: 6.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965217578 224 QPAEKglESQILEADLVLWTVGSKAllpELEPCDKPHELPlNARGQAETDETLRVKGHPRIFAIGD 289
Cdd:PRK12771  358 SPVTG--EEETLEADLVVLAIGQDI---DSAGLESVPGVE-VGRGVVQVDPNFMMTGRPGVFAGGD 417
 
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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