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Conserved domains on  [gi|1622952963|ref|XP_028706711|]
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sulfide:quinone oxidoreductase, mitochondrial isoform X1 [Macaca mulatta]

Protein Classification

FAD/NAD(P)-binding oxidoreductase( domain architecture ID 11418561)

FAD/NAD(P)-binding 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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
71-389 6.35e-55

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: 185.40  E-value: 6.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 147 IQLHYEKIKGLpegfAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTfpntpvkcAGAPqkIMYLSEAYFRKTGKrsKAN 226
Cdd:COG0446    88 ARPRPPPIPGL----DLPGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALRKRGL--KVT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 227 IIFNTSlgAIFGV--KKYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-D 302
Cdd:COG0446   152 LVERAP--RLLGVldPEMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 303 VLKTSPVA-DAAGWVDVDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQ 367
Cdd:COG0446   224 LAKDAGLAlGERGWIKVD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGT 300
                         330       340
                  ....*....|....*....|..
gi 1622952963 368 TPTKKYDgytSCPLVTGYNRVI 389
Cdd:COG0446   301 FISKVFD---LCIASTGTGRLL 319
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
71-389 6.35e-55

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: 185.40  E-value: 6.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 147 IQLHYEKIKGLpegfAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTfpntpvkcAGAPqkIMYLSEAYFRKTGKrsKAN 226
Cdd:COG0446    88 ARPRPPPIPGL----DLPGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALRKRGL--KVT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 227 IIFNTSlgAIFGV--KKYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-D 302
Cdd:COG0446   152 LVERAP--RLLGVldPEMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 303 VLKTSPVA-DAAGWVDVDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQ 367
Cdd:COG0446   224 LAKDAGLAlGERGWIKVD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGT 300
                         330       340
                  ....*....|....*....|..
gi 1622952963 368 TPTKKYDgytSCPLVTGYNRVI 389
Cdd:COG0446   301 FISKVFD---LCIASTGTGRLL 319
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
70-373 2.46e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 62.09  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  70 NVAVVEPSERHFYQPIWTLVGAGAKQLSSSGRPM-ASVIPSGVEWIKARVTELNPDKNCI----------HTDNDEQISY 138
Cdd:PTZ00318   35 NITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVrPALAKLPNRYLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 139 RYLIIALGIQLHYEKIKGLPEgFAHPKIGSNYSvKTVEKtwKALQDFKEGNaiftFPNTPVKCA----------GAPQKI 208
Cdd:PTZ00318  115 DKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHA-RGIRK--RIVQCIERAS----LPTTSVEERkrllhfvvvgGGPTGV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 209 MYLSEA--YFRKTGKRskaniiFNTSL------------GAIFGvkkyadALQEIIRERNLtVNYKQNLIEVRAdkQEAV 274
Cdd:PTZ00318  187 EFAAELadFFRDDVRN------LNPELveeckvtvleagSEVLG------SFDQALRKYGQ-RRLRRLGVDIRT--KTAV 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 275 FENLDKPGETQ---VISYEMLHVTPPMGPPDVLKTSPV-ADAAGWVDVDkETLQHKRYPNVFGIGDCTNLPTSK--TAAA 348
Cdd:PTZ00318  252 KEVLDKEVVLKdgeVIPTGLVVWSTGVGPGPLTKQLKVdKTSRGRISVD-DHLRVKPIPNVFALGDCAANEERPlpTLAQ 330
                         330       340
                  ....*....|....*....|....*.
gi 1622952963 349 VAAQSGI-LDRTISLIMKNQTPTKKY 373
Cdd:PTZ00318  331 VASQQGVyLAKEFNNELKGKPMSKPF 356
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
71-389 6.35e-55

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: 185.40  E-value: 6.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 147 IQLHYEKIKGLpegfAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTfpntpvkcAGAPqkIMYLSEAYFRKTGKrsKAN 226
Cdd:COG0446    88 ARPRPPPIPGL----DLPGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALRKRGL--KVT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 227 IIFNTSlgAIFGV--KKYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-D 302
Cdd:COG0446   152 LVERAP--RLLGVldPEMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 303 VLKTSPVA-DAAGWVDVDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQ 367
Cdd:COG0446   224 LAKDAGLAlGERGWIKVD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGT 300
                         330       340
                  ....*....|....*....|..
gi 1622952963 368 TPTKKYDgytSCPLVTGYNRVI 389
Cdd:COG0446   301 FISKVFD---LCIASTGTGRLL 319
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
56-389 1.14e-41

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 152.21  E-value: 1.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  56 ITMAARMKRKVGAE-NVAVVEPSERHFYQPIWTLVGAGAKQLSSSGRPMASVI-PSGVEWIKARVTELNPDKNCIHTDND 133
Cdd:COG1252    14 LEAARRLRKKLGGDaEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLrRAGVRFIQGEVTGIDPEARTVTLADG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 134 EQISYRYLIIALGIQLHYEKIKGLPEgFAHPkigsnysVKTVE---KTWKALQDFKEGN--------AIFTFPNTPVKCA 202
Cdd:COG1252    94 RTLSYDYLVIATGSVTNFFGIPGLAE-HALP-------LKTLEdalALRERLLAAFERAerrrlltiVVVGGGPTGVELA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 203 GApqkIMYLSEAYFRKTGKR-SKANIIFNTSLGAIFGV--KKYADALQEIIRERNLTVNYKQNLIEVRADKqeAVFENld 279
Cdd:COG1252   166 GE---LAELLRKLLRYPGIDpDKVRITLVEAGPRILPGlgEKLSEAAEKELEKRGVEVHTGTRVTEVDADG--VTLED-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 280 kpGETqvISYEMLHVTPPMGPPDVLKTSPVA-DAAGWVDVDkETLQHKRYPNVFGIGDCTNLPTSKT-----AAAVAAQS 353
Cdd:COG1252   239 --GEE--IPADTVIWAAGVKAPPLLADLGLPtDRRGRVLVD-PTLQVPGHPNVFAIGDCAAVPDPDGkpvpkTAQAAVQQ 313
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1622952963 354 G-ILDRTISLIMKNQtPTKKYDG-YTSCPLVTGYNRVI 389
Cdd:COG1252   314 AkVLAKNIAALLRGK-PLKPFRYrDKGCLASLGRGAAV 350
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
70-373 2.46e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 62.09  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963  70 NVAVVEPSERHFYQPIWTLVGAGAKQLSSSGRPM-ASVIPSGVEWIKARVTELNPDKNCI----------HTDNDEQISY 138
Cdd:PTZ00318   35 NITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVrPALAKLPNRYLRAVVYDVDFEEKRVkcgvvsksnnANVNTFSVPY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 139 RYLIIALGIQLHYEKIKGLPEgFAHPKIGSNYSvKTVEKtwKALQDFKEGNaiftFPNTPVKCA----------GAPQKI 208
Cdd:PTZ00318  115 DKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHA-RGIRK--RIVQCIERAS----LPTTSVEERkrllhfvvvgGGPTGV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 209 MYLSEA--YFRKTGKRskaniiFNTSL------------GAIFGvkkyadALQEIIRERNLtVNYKQNLIEVRAdkQEAV 274
Cdd:PTZ00318  187 EFAAELadFFRDDVRN------LNPELveeckvtvleagSEVLG------SFDQALRKYGQ-RRLRRLGVDIRT--KTAV 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952963 275 FENLDKPGETQ---VISYEMLHVTPPMGPPDVLKTSPV-ADAAGWVDVDkETLQHKRYPNVFGIGDCTNLPTSK--TAAA 348
Cdd:PTZ00318  252 KEVLDKEVVLKdgeVIPTGLVVWSTGVGPGPLTKQLKVdKTSRGRISVD-DHLRVKPIPNVFALGDCAANEERPlpTLAQ 330
                         330       340
                  ....*....|....*....|....*.
gi 1622952963 349 VAAQSGI-LDRTISLIMKNQTPTKKY 373
Cdd:PTZ00318  331 VASQQGVyLAKEFNNELKGKPMSKPF 356
 
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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