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Conserved domains on  [gi|38014288|gb|AAH02435|]
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COQ10A protein, partial [Homo sapiens]

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 ...
 33-171 1.16e-60

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: 185.37  E-value: 1.16e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  33 YSERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGkL 112
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38014288 113 FNHLETIWRFSPGIpayPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERRA 171
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRA 135
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 33-171 1.16e-60

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: 185.37  E-value: 1.16e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  33 YSERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGkL 112
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38014288 113 FNHLETIWRFSPGIpayPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERRA 171
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRA 135
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 33-170 3.50e-31

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 110.34  E-value: 3.50e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  33 YSERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGKl 112
Cdd:COG2867   4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDGP- 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38014288 113 FNHLETIWRFspgIPAYPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERR 170
Cdd:COG2867  83 FKHLEGRWRF---EPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 39-168 1.05e-25

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: 96.03  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288    39 MGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHlkAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGkLFNHLET 118
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDG-DFKRLEG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 38014288   119 IWRFSPGIPAypRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFE 168
Cdd:pfam03364  78 SWRFEPGGPG--TRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
34-171 3.53e-12

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 61.48  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288   34 SERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGKlF 113
Cdd:PRK10724  18 SRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGP-F 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38014288  114 NHLETIWRFspgIPAYPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERRA 171
Cdd:PRK10724  97 KKLIGGWKF---TPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRA 151
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 33-171 1.16e-60

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: 185.37  E-value: 1.16e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  33 YSERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGkL 112
Cdd:cd07813   1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDELEAELTVGFGGIRESFTSRVTLVPPESIEAELVDG-P 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38014288 113 FNHLETIWRFSPGIpayPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERRA 171
Cdd:cd07813  80 FKHLEGEWRFKPLG---ENACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRA 135
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 33-170 3.50e-31

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 110.34  E-value: 3.50e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  33 YSERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGKl 112
Cdd:COG2867   4 ISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEVVAELTVSFKGLRESFTTRNTLDPPERIDFELVDGP- 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38014288 113 FNHLETIWRFspgIPAYPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERR 170
Cdd:COG2867  83 FKHLEGRWRF---EPLGEGGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 39-168 1.05e-25

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: 96.03  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288    39 MGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHlkAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGkLFNHLET 118
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL--ADWRVAFGGLRRSFTARVTLQPPERIEMVLVDG-DFKRLEG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 38014288   119 IWRFSPGIPAypRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFE 168
Cdd:pfam03364  78 SWRFEPGGPG--TRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
34-171 3.53e-12

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 61.48  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288   34 SERRIMGYSMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSAVSMVKPHMVKAVCTDGKlF 113
Cdd:PRK10724  18 SRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMQLVDGP-F 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 38014288  114 NHLETIWRFspgIPAYPRTCTVDFSISFEFRSLLHSQLATMFFDEVVKQNVAAFERRA 171
Cdd:PRK10724  97 KKLIGGWKF---TPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRA 151
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 42-175 3.39e-04

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 39.23  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014288  42 SMQEMYEVVSNVQEYREFVPWCKKSLVVSSRKGHLKAQLEVGFPPVMERYTSA--VSMVKPHMVKAVCTDGKLFNHLETI 119
Cdd:cd07812  10 PPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTLTSevTEVDPPRPGRFRVTGGGGGVDGTGE 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 38014288 120 WRFSPgIPayPRTCTVDFSISFEFRSLLhSQLATMFFDEVVKQNVAAFERRAATKF 175
Cdd:cd07812  90 WRLEP-EG--DGGTRVTYTVEYDPPGPL-LKVFALLLAGALKRELAALLRALKARL 141
 
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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