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Conserved domains on  [gi|556426019|ref|WP_023310946|]
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MULTISPECIES: helix-turn-helix domain-containing protein [Enterobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11832 super family cl32729
hydrogen peroxide resistance inhibitor IprA;
37-207 1.15e-16

hydrogen peroxide resistance inhibitor IprA;


The actual alignment was detected with superfamily member PRK11832:

Pssm-ID: 183332 [Multi-domain]  Cd Length: 207  Bit Score: 74.92  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  37 STENNENIHFIVSGEVEFRRESDELCMFTlQNKCIFGLSSIYYNSTHMYGLVRASTVV-RTLKKEDFFRLMSEKNLWEAL 115
Cdd:PRK11832  37 SDVNNEDTFVILEGVISLRREENVLIGIT-QAPYIMGLADGLMKNDIPYKLISEGNCTgYHLPAKQTITLIEQNQLWRDA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019 116 SKVLSWYVCLLSKRDEVLVARSAYSIVREFLLEINELMVHHQRDINIYDYIQEYTSLARSTIIKILADLKKGNYIQVDKG 195
Cdd:PRK11832 116 FYWLAWQNRILELRDVQLIGHNSYEQIRATLLSMIDWNEELRSRIGVMNYIHQRTRISRSVVAEVLAALRKGGYIEMNKG 195

                        170
                 ....*....|..
gi 556426019 196 RLMYLSALPEKY 207
Cdd:PRK11832 196 KLVAINRLPSEY 207
 
Name Accession Description Interval E-value
PRK11832 PRK11832
hydrogen peroxide resistance inhibitor IprA;
37-207 1.15e-16

hydrogen peroxide resistance inhibitor IprA;


Pssm-ID: 183332 [Multi-domain]  Cd Length: 207  Bit Score: 74.92  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  37 STENNENIHFIVSGEVEFRRESDELCMFTlQNKCIFGLSSIYYNSTHMYGLVRASTVV-RTLKKEDFFRLMSEKNLWEAL 115
Cdd:PRK11832  37 SDVNNEDTFVILEGVISLRREENVLIGIT-QAPYIMGLADGLMKNDIPYKLISEGNCTgYHLPAKQTITLIEQNQLWRDA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019 116 SKVLSWYVCLLSKRDEVLVARSAYSIVREFLLEINELMVHHQRDINIYDYIQEYTSLARSTIIKILADLKKGNYIQVDKG 195
Cdd:PRK11832 116 FYWLAWQNRILELRDVQLIGHNSYEQIRATLLSMIDWNEELRSRIGVMNYIHQRTRISRSVVAEVLAALRKGGYIEMNKG 195

                        170
                 ....*....|..
gi 556426019 196 RLMYLSALPEKY 207
Cdd:PRK11832 196 KLVAINRLPSEY 207
HTH_46 pfam15977
Winged helix-turn-helix DNA binding;
138-205 7.51e-16

Winged helix-turn-helix DNA binding;


Pssm-ID: 435049 [Multi-domain]  Cd Length: 68  Bit Score: 68.84  E-value: 7.51e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426019  138 AYSIVREFLLEINELMVHHQRDINIYDYIQEYTSLARSTIIKILADLKKGNYIQVDKGRLMYLSALPE 205
Cdd:pfam15977   1 SYDIIRALLLELMDLPEEFRENISVLNYIQQRTHLSRSSIMKILSELKKGGYIEIDRGRLVAINNLPS 68
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 11-197 6.85e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 56.53  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  11 PQAELDAIIAAtegFEERTLRKWQRISTEN--NENIHFIVSGEVEFRRES---DELCMFTLQNKCIFGLSSIYYNSTHMY 85
Cdd:COG0664    5 SDEELEALLAH---LELRTLKKGEVLFREGdpADHLYFVLSGLVKLYRISedgREQILGFLGPGDFFGELSLLGGEPSPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  86 GlVRA--STVVRTLKKEDFFRLMSE-KNLWEALSKVLSWYVCLLSKRDEVLVARSAYSIVREFLLEineLMVHHQRDINI 162
Cdd:COG0664   82 T-AEAleDSELLRIPREDLEELLERnPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLE---LADRLDGRIDL 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 556426019 163 Y---DYIQEYTSLARSTIIKILADLKKGNYIQVDKGRL 197
Cdd:COG0664  158 PltqEEIASYLGLTRETVSRILKKLEKEGLIELERGRI 195
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 11-108 1.43e-04

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 40.00  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  11 PQAELDAIIAAtegFEERTLRKWQRISTEN--NENIHFIVSGEVEFRRESD---ELCMFTLQNKCIFGLSSIYYNSTHMY 85
Cdd:cd00038    6 DDEELEELADA---LEERRFPAGEVIIRQGdpADSLYIVLSGSVEVYKLDEdgrEQIVGFLGPGDLFGELALLGNGPRSA 82

                         90       100
                 ....*....|....*....|....*
gi 556426019  86 GlVRAST--VVRTLKKEDFFRLMSE 108
Cdd:cd00038   83 T-VRALTdsELLVLPRSDFRRLLQE 106
 
Name Accession Description Interval E-value
PRK11832 PRK11832
hydrogen peroxide resistance inhibitor IprA;
37-207 1.15e-16

hydrogen peroxide resistance inhibitor IprA;


Pssm-ID: 183332 [Multi-domain]  Cd Length: 207  Bit Score: 74.92  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  37 STENNENIHFIVSGEVEFRRESDELCMFTlQNKCIFGLSSIYYNSTHMYGLVRASTVV-RTLKKEDFFRLMSEKNLWEAL 115
Cdd:PRK11832  37 SDVNNEDTFVILEGVISLRREENVLIGIT-QAPYIMGLADGLMKNDIPYKLISEGNCTgYHLPAKQTITLIEQNQLWRDA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019 116 SKVLSWYVCLLSKRDEVLVARSAYSIVREFLLEINELMVHHQRDINIYDYIQEYTSLARSTIIKILADLKKGNYIQVDKG 195
Cdd:PRK11832 116 FYWLAWQNRILELRDVQLIGHNSYEQIRATLLSMIDWNEELRSRIGVMNYIHQRTRISRSVVAEVLAALRKGGYIEMNKG 195

                        170
                 ....*....|..
gi 556426019 196 RLMYLSALPEKY 207
Cdd:PRK11832 196 KLVAINRLPSEY 207
HTH_46 pfam15977
Winged helix-turn-helix DNA binding;
138-205 7.51e-16

Winged helix-turn-helix DNA binding;


Pssm-ID: 435049 [Multi-domain]  Cd Length: 68  Bit Score: 68.84  E-value: 7.51e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426019  138 AYSIVREFLLEINELMVHHQRDINIYDYIQEYTSLARSTIIKILADLKKGNYIQVDKGRLMYLSALPE 205
Cdd:pfam15977   1 SYDIIRALLLELMDLPEEFRENISVLNYIQQRTHLSRSSIMKILSELKKGGYIEIDRGRLVAINNLPS 68
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 11-197 6.85e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 56.53  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  11 PQAELDAIIAAtegFEERTLRKWQRISTEN--NENIHFIVSGEVEFRRES---DELCMFTLQNKCIFGLSSIYYNSTHMY 85
Cdd:COG0664    5 SDEELEALLAH---LELRTLKKGEVLFREGdpADHLYFVLSGLVKLYRISedgREQILGFLGPGDFFGELSLLGGEPSPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  86 GlVRA--STVVRTLKKEDFFRLMSE-KNLWEALSKVLSWYVCLLSKRDEVLVARSAYSIVREFLLEineLMVHHQRDINI 162
Cdd:COG0664   82 T-AEAleDSELLRIPREDLEELLERnPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLE---LADRLDGRIDL 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 556426019 163 Y---DYIQEYTSLARSTIIKILADLKKGNYIQVDKGRL 197
Cdd:COG0664  158 PltqEEIASYLGLTRETVSRILKKLEKEGLIELERGRI 195
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 11-108 1.43e-04

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 40.00  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426019  11 PQAELDAIIAAtegFEERTLRKWQRISTEN--NENIHFIVSGEVEFRRESD---ELCMFTLQNKCIFGLSSIYYNSTHMY 85
Cdd:cd00038    6 DDEELEELADA---LEERRFPAGEVIIRQGdpADSLYIVLSGSVEVYKLDEdgrEQIVGFLGPGDLFGELALLGNGPRSA 82

                         90       100
                 ....*....|....*....|....*
gi 556426019  86 GlVRAST--VVRTLKKEDFFRLMSE 108
Cdd:cd00038   83 T-VRALTdsELLVLPRSDFRRLLQE 106
 
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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