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Conserved domains on  [gi|488193114|ref|WP_002264322|]
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DUF1836 domain-containing protein [Streptococcus mutans]

Protein Classification

DUF1836 domain-containing protein( domain architecture ID 10556141)

DUF1836 domain-containing protein belongs to the helix-turn-helix (HTH) transcription regulator MerR superfamily and may bind DNA

CATH:  1.10.10.10
Gene Ontology:  GO:0003677
PubMed:  15808743|12829265|17302809|35130613
SCOP:  3000158

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1836 pfam08876
Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.
 7-105 1.80e-37

Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.


:

Pssm-ID: 430279  Cd Length: 102  Bit Score: 123.91  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193114    7 PKWDDLPELDLYLDQVLLYVNQTtdAAASKDKGLTASMINNYVKHGHIEKPIKKKYNRKQVARLIVITALKNVFSIQEIS 86
Cdd:pfam08876   1 PKWEELPNIDLYMDQVITLINDK--LEPLDDKILTKTMINNYVKNKLIPPPKKKKYSKEQIALLIIIYYLKSVLSIDEIK 78

                          90       100
                  ....*....|....*....|....
gi 488193114   87 QTLTVLTAN-----NSSKNLYNDF 105
Cdd:pfam08876  79 KGLSLATNTindreISLEEAYDYF 102
 
Name Accession Description Interval E-value
DUF1836 pfam08876
Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.
 7-105 1.80e-37

Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.


Pssm-ID: 430279  Cd Length: 102  Bit Score: 123.91  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193114    7 PKWDDLPELDLYLDQVLLYVNQTtdAAASKDKGLTASMINNYVKHGHIEKPIKKKYNRKQVARLIVITALKNVFSIQEIS 86
Cdd:pfam08876   1 PKWEELPNIDLYMDQVITLINDK--LEPLDDKILTKTMINNYVKNKLIPPPKKKKYSKEQIALLIIIYYLKSVLSIDEIK 78

                          90       100
                  ....*....|....*....|....
gi 488193114   87 QTLTVLTAN-----NSSKNLYNDF 105
Cdd:pfam08876  79 KGLSLATNTindreISLEEAYDYF 102
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 34-104 3.47e-03

Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.


Pssm-ID: 133383 [Multi-domain]  Cd Length: 127  Bit Score: 35.62  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488193114  34 ASKDKGLTASMINNYVKHGHIEKPIK-----KKYNRKQVARLIVITALKNV-FSIQEISQTLtvltannsskNLYND 104
Cdd:cd01108    6 AAKLTGLSAKMIRYYEEIGLIPPPSRsdngyRVYNQRDIEELRFIRRARDLgFSLEEIRELL----------ALWRD 72
 
Name Accession Description Interval E-value
DUF1836 pfam08876
Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.
 7-105 1.80e-37

Domain of unknown function (DUF1836); This family of proteins are functionally uncharacterized.


Pssm-ID: 430279  Cd Length: 102  Bit Score: 123.91  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488193114    7 PKWDDLPELDLYLDQVLLYVNQTtdAAASKDKGLTASMINNYVKHGHIEKPIKKKYNRKQVARLIVITALKNVFSIQEIS 86
Cdd:pfam08876   1 PKWEELPNIDLYMDQVITLINDK--LEPLDDKILTKTMINNYVKNKLIPPPKKKKYSKEQIALLIIIYYLKSVLSIDEIK 78

                          90       100
                  ....*....|....*....|....
gi 488193114   87 QTLTVLTAN-----NSSKNLYNDF 105
Cdd:pfam08876  79 KGLSLATNTindreISLEEAYDYF 102
HTH_CueR cd01108
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ...
 34-104 3.47e-03

Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.


Pssm-ID: 133383 [Multi-domain]  Cd Length: 127  Bit Score: 35.62  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488193114  34 ASKDKGLTASMINNYVKHGHIEKPIK-----KKYNRKQVARLIVITALKNV-FSIQEISQTLtvltannsskNLYND 104
Cdd:cd01108    6 AAKLTGLSAKMIRYYEEIGLIPPPSRsdngyRVYNQRDIEELRFIRRARDLgFSLEEIRELL----------ALWRD 72
 
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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