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Conserved domains on  [gi|20129725|ref|NP_610221|]
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uncharacterized protein Dmel_CG9410, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 50-191 9.28e-56

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


:

Pssm-ID: 176855  Cd Length: 138  Bit Score: 173.43  E-value: 9.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725  50 YTKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrL 129
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129725 130 FNYLLNEWSFKPGLkdiPNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQEVRRR 191
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 50-191 9.28e-56

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176855  Cd Length: 138  Bit Score: 173.43  E-value: 9.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725  50 YTKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrL 129
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129725 130 FNYLLNEWSFKPGLkdiPNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQEVRRR 191
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 50-187 5.14e-29

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 105.33  E-value: 5.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725  50 YTKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrL 129
Cdd:COG2867   4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDG-P 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20129725 130 FNYLLNEWSFKPgLKDipNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQE 187
Cdd:COG2867  83 FKHLEGRWRFEP-LGE--GGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 56-184 4.23e-27

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 99.88  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725    56 VGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRgsEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrLFNYLLN 135
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLER--DGSLADWRVAFGGLRRSFTARVTLQPPERIEMVLVDG-DFKRLEG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20129725   136 EWSFKPGLKDipNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAF 184
Cdd:pfam03364  78 SWRFEPGGPG--TRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAF 124
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
51-189 5.16e-09

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 53.01  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725   51 TKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGRlF 130
Cdd:PRK10724  18 SRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGP-F 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129725  131 NYLLNEWSFKPgLKdiPNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQEVR 189
Cdd:PRK10724  97 KKLIGGWKFTP-LS--QEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAK 152
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 50-191 9.28e-56

Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and similar proteins. COQ10p is a hydrophobic protein located in the inner membrane of mitochondria that binds coenzyme Q (CoQ), also called ubiquinone, which is an essential electron carrier of the respiratory chain. Deletion of the gene encoding COQ10p (COQ10 or YOL008W) in Saccharomyces cerevisiae results in respiratory defect because of the inability to oxidize NADH and succinate. COQ10p may function in the delivery of CoQ (Q6 in budding yeast) to its proper location for electron transport. The human homolog, called Q-binding protein COQ10 homolog A (COQ10A), is able to fully complement for the absence of COQ10p in fission yeast. Human COQ10A also has a splice variant COQ10B. COQ10p belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176855  Cd Length: 138  Bit Score: 173.43  E-value: 9.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725  50 YTKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrL 129
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129725 130 FNYLLNEWSFKPGLkdiPNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQEVRRR 191
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 50-187 5.14e-29

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 105.33  E-value: 5.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725  50 YTKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrL 129
Cdd:COG2867   4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDG-P 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20129725 130 FNYLLNEWSFKPgLKDipNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQE 187
Cdd:COG2867  83 FKHLEGRWRFEP-LGE--GGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 56-184 4.23e-27

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 99.88  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725    56 VGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRgsEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGrLFNYLLN 135
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLER--DGSLADWRVAFGGLRRSFTARVTLQPPERIEMVLVDG-DFKRLEG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20129725   136 EWSFKPGLKDipNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAF 184
Cdd:pfam03364  78 SWRFEPGGPG--TRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAF 124
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
51-189 5.16e-09

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 53.01  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129725   51 TKKELVGYSMQDMYSVVSDVSNYHKFVPYVKRSDVHSRGSEGFKADLIVGFPPLNEAYTSQVTLVPPSLVKSECHDGRlF 130
Cdd:PRK10724  18 SRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGP-F 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129725  131 NYLLNEWSFKPgLKdiPNSCVLDFKVSFEFKSLLHSNVANIFFDLICDQMENAFIQEVR 189
Cdd:PRK10724  97 KKLIGGWKFTP-LS--QEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAK 152
 
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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