NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622952967|ref|XP_028706712|]
View 

sulfide:quinone oxidoreductase, mitochondrial isoform X2 [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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
71-324 1.40e-37

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: 138.02  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 147 IQLHY----------------------------EKTGKR---------------------SKANIIFNTSlgAIFGV--K 175
Cdd:COG0446    88 ARPRPppipgldlpgvftlrtlddadalrealkEFKGKRavvigggpiglelaealrkrgLKVTLVERAP--RLLGVldP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 176 KYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-DVLKTSPVA-DAAGWVD 252
Cdd:COG0446   166 EMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtELAKDAGLAlGERGWIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 253 VDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQTPTKKYDgytSCPLVT 318
Cdd:COG0446   240 VD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGTFISKVFD---LCIAST 313

                  ....*.
gi 1622952967 319 GYNRVI 324
Cdd:COG0446   314 GTGRLL 319
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
71-324 1.40e-37

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: 138.02  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 147 IQLHY----------------------------EKTGKR---------------------SKANIIFNTSlgAIFGV--K 175
Cdd:COG0446    88 ARPRPppipgldlpgvftlrtlddadalrealkEFKGKRavvigggpiglelaealrkrgLKVTLVERAP--RLLGVldP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 176 KYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-DVLKTSPVA-DAAGWVD 252
Cdd:COG0446   166 EMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtELAKDAGLAlGERGWIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 253 VDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQTPTKKYDgytSCPLVT 318
Cdd:COG0446   240 VD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGTFISKVFD---LCIAST 313

                  ....*.
gi 1622952967 319 GYNRVI 324
Cdd:COG0446   314 GTGRLL 319
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
193-308 1.58e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 49.77  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 193 NYKQNLIEVRAdkQEAVFENLDKPGETQ---VISYEMLHVTPPMGPPDVLKTSPV-ADAAGWVDVDkETLQHKRYPNVFG 268
Cdd:PTZ00318  237 RLRRLGVDIRT--KTAVKEVLDKEVVLKdgeVIPTGLVVWSTGVGPGPLTKQLKVdKTSRGRISVD-DHLRVKPIPNVFA 313
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622952967 269 IGDCTNLPTSK--TAAAVAAQSGI-LDRTISLIMKNQTPTKKY 308
Cdd:PTZ00318  314 LGDCAANEERPlpTLAQVASQQGVyLAKEFNNELKGKPMSKPF 356
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
71-324 1.40e-37

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: 138.02  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967  71 VAVVEPSERHFYQP--IWTLVGAGAKQLSS-SGRPMASVIPSGVEWI-KARVTELNPDKNCIHTDNDEQISYRYLIIALG 146
Cdd:COG0446     8 ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 147 IQLHY----------------------------EKTGKR---------------------SKANIIFNTSlgAIFGV--K 175
Cdd:COG0446    88 ARPRPppipgldlpgvftlrtlddadalrealkEFKGKRavvigggpiglelaealrkrgLKVTLVERAP--RLLGVldP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 176 KYADALQEIIRERNLTVNYKQNLIEVRAD-KQEAVFENldkpGETqvISYEMLHVTPPMGPP-DVLKTSPVA-DAAGWVD 252
Cdd:COG0446   166 EMAALLEEELREHGVELRLGETVVAIDGDdKVAVTLTD----GEE--IPADLVVVAPGVRPNtELAKDAGLAlGERGWIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 253 VDkETLQHkRYPNVFGIGDCTNLP---TSKTA-----------AAVAAQSgILDRTISLIMKNQTPTKKYDgytSCPLVT 318
Cdd:COG0446   240 VD-ETLQT-SDPDVYAAGDCAEVPhpvTGKTVyiplasaankqGRVAAEN-ILGGPAPFPGLGTFISKVFD---LCIAST 313

                  ....*.
gi 1622952967 319 GYNRVI 324
Cdd:COG0446   314 GTGRLL 319
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
56-324 2.59e-29

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 116.77  E-value: 2.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967  56 ITMAARMKRKVGAE-NVAVVEPSERHFYQPIWTLVGAGAKQLSSSGRPMASVI-PSGVEWIKARVTELNPDKNCIHTDND 133
Cdd:COG1252    14 LEAARRLRKKLGGDaEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLrRAGVRFIQGEVTGIDPEARTVTLADG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 134 EQISYRYLIIALGIQLHYEK----------------------------------------------TG------------ 155
Cdd:COG1252    94 RTLSYDYLVIATGSVTNFFGipglaehalplktledalalrerllaaferaerrrlltivvvgggpTGvelagelaellr 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 156 --------KRSKANIIFNTSLGAIFGV--KKYADALQEIIRERNLTVNYKQNLIEVRADKqeAVFENldkpGETqvISYE 225
Cdd:COG1252   174 kllrypgiDPDKVRITLVEAGPRILPGlgEKLSEAAEKELEKRGVEVHTGTRVTEVDADG--VTLED----GEE--IPAD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 226 MLHVTPPMGPPDVLKTSPVA-DAAGWVDVDkETLQHKRYPNVFGIGDCTNLPTSKT-----AAAVAAQSG-ILDRTISLI 298
Cdd:COG1252   246 TVIWAAGVKAPPLLADLGLPtDRRGRVLVD-PTLQVPGHPNVFAIGDCAAVPDPDGkpvpkTAQAAVQQAkVLAKNIAAL 324
                         330       340
                  ....*....|....*....|....*..
gi 1622952967 299 MKNQtPTKKYDG-YTSCPLVTGYNRVI 324
Cdd:COG1252   325 LRGK-PLKPFRYrDKGCLASLGRGAAV 350
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
193-308 1.58e-06

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 49.77  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622952967 193 NYKQNLIEVRAdkQEAVFENLDKPGETQ---VISYEMLHVTPPMGPPDVLKTSPV-ADAAGWVDVDkETLQHKRYPNVFG 268
Cdd:PTZ00318  237 RLRRLGVDIRT--KTAVKEVLDKEVVLKdgeVIPTGLVVWSTGVGPGPLTKQLKVdKTSRGRISVD-DHLRVKPIPNVFA 313
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622952967 269 IGDCTNLPTSK--TAAAVAAQSGI-LDRTISLIMKNQTPTKKY 308
Cdd:PTZ00318  314 LGDCAANEERPlpTLAQVASQQGVyLAKEFNNELKGKPMSKPF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH