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Conserved domains on  [gi|505210790|ref|WP_015397892|]
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type II toxin-antitoxin system RatA family toxin [Bartonella australis]

Protein Classification

type II toxin-antitoxin system RatA family toxin( domain architecture ID 10167417)

type II toxin-antitoxin (TA) system RatA family toxin similar to Escherichia coli ribosome association toxin RatA, which binds to 50S ribosomal subunits, preventing them from associating with 30S subunits to form 70S ribosomes, and is the toxin component of the RatA (PasT)-RatB (PasI) TA module

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 ...
 4-147 7.87e-55

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: 168.80  E-value: 7.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   4 FTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlLLADMTVGYKMFREIFTTQVFLQPrENLIEVKY 83
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDE----LEAELTVGFGGIRESFTSRVTLVP-PESIEAEL 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505210790  84 INGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKRAHQI 147
Cdd:cd07813   76 VDGPFKHLEGEWRFKPLGE-NACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-147 7.87e-55

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: 168.80  E-value: 7.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   4 FTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlLLADMTVGYKMFREIFTTQVFLQPrENLIEVKY 83
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDE----LEAELTVGFGGIRESFTSRVTLVP-PESIEAEL 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505210790  84 INGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKRAHQI 147
Cdd:cd07813   76 VDGPFKHLEGEWRFKPLGE-NACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-143 5.19e-53

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 164.26  E-value: 5.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   1 MPAFTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEfeekTLLLADMTVGYKMFREIFTTQVFLQPrENLIE 80
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDG----DEVVAELTVSFKGLRESFTTRNTLDP-PERID 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505210790  81 VKYINGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKR 143
Cdd:COG2867   76 FELVDGPFKHLEGRWRFEPLGE-GGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-141 1.04e-28

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: 102.19  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   10 IAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlllADMTVGYKMFREIFTTQVFLQPRENLIEVkYINGPFK 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL------ADWRVAFGGLRRSFTARVTLQPPERIEMV-LVDGDFK 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 505210790   90 YLENRWIFHPTQDINTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFE 141
Cdd:pfam03364  74 RLEGSWRFEPGGPGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-148 1.25e-18

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 77.27  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   1 MPAFTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlLLADMTVGYKMFREIFTTQVFLQPRENlIE 80
Cdd:PRK10724  14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQ----MTAAVDVSKAGISKTFTTRNQLTSNQS-IL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505210790  81 VKYINGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKRAHQIY 148
Cdd:PRK10724  89 MQLVDGPFKKLIGGWKFTPLSQ-EACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEVY 155
 
Name Accession Description Interval E-value
COQ10p_like cd07813
Coenzyme Q-binding protein COQ10p and similar proteins; Coenzyme Q-binding protein COQ10p and ...
 4-147 7.87e-55

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: 168.80  E-value: 7.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   4 FTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlLLADMTVGYKMFREIFTTQVFLQPrENLIEVKY 83
Cdd:cd07813    1 YSKSRLVPYSAEQMFDLVADVERYPEFLPWCTASRVLERDEDE----LEAELTVGFGGIRESFTSRVTLVP-PESIEAEL 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505210790  84 INGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKRAHQI 147
Cdd:cd07813   76 VDGPFKHLEGEWRFKPLGE-NACKVEFDLEFEFKSRLLEALAGLVFDEVAKKMVDAFEKRAKQL 138
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-143 5.19e-53

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


Pssm-ID: 442114  Cd Length: 137  Bit Score: 164.26  E-value: 5.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   1 MPAFTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEfeekTLLLADMTVGYKMFREIFTTQVFLQPrENLIE 80
Cdd:COG2867    1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDG----DEVVAELTVSFKGLRESFTTRNTLDP-PERID 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505210790  81 VKYINGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKR 143
Cdd:COG2867   76 FELVDGPFKHLEGRWRFEPLGE-GGTKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-141 1.04e-28

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: 102.19  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   10 IAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlllADMTVGYKMFREIFTTQVFLQPRENLIEVkYINGPFK 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSL------ADWRVAFGGLRRSFTARVTLQPPERIEMV-LVDGDFK 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 505210790   90 YLENRWIFHPTQDINTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFE 141
Cdd:pfam03364  74 RLEGSWRFEPGGPGTRVKVTLELDFEFASPLPGALLGFVFRRVLRTLLEAFR 125
PRK10724 PRK10724
type II toxin-antitoxin system RatA family toxin;
1-148 1.25e-18

type II toxin-antitoxin system RatA family toxin;


Pssm-ID: 182678  Cd Length: 158  Bit Score: 77.27  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   1 MPAFTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEektlLLADMTVGYKMFREIFTTQVFLQPRENlIE 80
Cdd:PRK10724  14 MPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRVLESTPGQ----MTAAVDVSKAGISKTFTTRNQLTSNQS-IL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505210790  81 VKYINGPFKYLENRWIFHPTQDiNTCNIEFSIDYEFKSKMLGLVMGSVFDIAFRKFTDAFEKRAHQIY 148
Cdd:PRK10724  89 MQLVDGPFKKLIGGWKFTPLSQ-EACRIEFHLDFEFTNKLIELAFGRVFKELASNMVQAFTVRAKEVY 155
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-144 1.84e-10

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: 55.41  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790   4 FTTHRHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEEKTLLLADMTVGYKMFREIfTTQVFLQPRENLIEVKY 83
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTLTS-EVTEVDPPRPGRFRVTG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505210790  84 iNGPFKYLENRWIFHPTQDINTCnIEFSIDYEFKS---KMLGLVMGSVFDIAFRKFTDAFEKRA 144
Cdd:cd07812   80 -GGGGVDGTGEWRLEPEGDGGTR-VTYTVEYDPPGpllKVFALLLAGALKRELAALLRALKARL 141
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 8-144 4.30e-03

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 35.54  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505210790    8 RHIAHNAREMFDLVSDVERYPEFVPMCESLVVRSREEFEEKTLLLADMTVGYKMFREIFTTqvfLQPRENLIEVKYI-NG 86
Cdd:pfam10604   3 IEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVE---YDPAPRLLAYRIVePL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505210790   87 PFKYLENRWIFHPTQDinTCNIEFSIDYEF---KSKMLGLVMGSVFDIAFRKFTDAFEKRA 144
Cdd:pfam10604  80 GVANYVGTWTVTPAGG--GTRVTWTGEFDGpplGGPFRDPAAARAVKGDYRAGLDRLKAVL 138
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 16-42 7.80e-03

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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: 176861  Cd Length: 140  Bit Score: 34.52  E-value: 7.80e-03
                         10        20
                 ....*....|....*....|....*..
gi 505210790  16 EMFDLVSDVERYPEFVPMCESLVVRSR 42
Cdd:cd07819   16 AVMDVLADVEAYPEWSPKVKSVEVLLR 42
 
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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