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Conserved domains on  [gi|1525557239|gb|RQV51207|]
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Crp/Fnr family transcriptional regulator [Burkholderia cenocepacia]

Protein Classification

Crp/Fnr family transcriptional regulator( domain architecture ID 11429533)

Crp/Fnr family transcriptional regulator containing a DNA-binding Crp-like helix-turn-helix (HTH) domain, may bind cyclic nucleotides

CATH:  2.60.120.10|1.10.10.10
Gene Ontology:  GO:0003677|GO:0030552
PubMed:  11407111|14638413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 55-263 2.96e-40

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: 138.20  E-value: 2.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  55 FRTLAPEHQALVLAQSHVEQCEAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELRK 134
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 135 YEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQALAQLFNPAlypDTGPSL 214
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRL---DGRIDL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1525557239 215 SISQEELGMLVGVSRQRINQALQQLEKLGALRLAYNQIDVVDLDALARF 263
Cdd:COG0664   158 PLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 55-263 2.96e-40

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: 138.20  E-value: 2.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  55 FRTLAPEHQALVLAQSHVEQCEAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELRK 134
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 135 YEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQALAQLFNPAlypDTGPSL 214
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRL---DGRIDL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1525557239 215 SISQEELGMLVGVSRQRINQALQQLEKLGALRLAYNQIDVVDLDALARF 263
Cdd:COG0664   158 PLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 76-160 5.13e-11

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 57.62  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  76 EAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELRKYEVVAIQRSTVLFVPVDTFHA 155
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLE 84


                  ....*
gi 1525557239 156 LLDTS 160
Cdd:pfam00027  85 LLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 54-168 1.61e-10

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: 56.95  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  54 WFRTLAPEHQALVLAQSHVEQCEAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELR 133
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1525557239 134 KYEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVI 168
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 77-267 3.20e-05

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 43.66  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  77 AGDVIAH--RLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRElRKYEVVAIQRSTvlfvpVDTFH 154
Cdd:PRK13918   13 PGAVILYpgVPGPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAE-RAYFAEAVTDSR-----IDVLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 155 -ALLDTSLpfTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQALAQLFNPAL--YPDTGPS-LSISQEELGMLVGVSRQ 230
Cdd:PRK13918   87 pALMSAED--NLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLatQEDSGETmIYATHDELAAAVGSVRE 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1525557239 231 RINQALQQLEKLGALRLAYNQIDVVDLDALARFGMEQ 267
Cdd:PRK13918  165 TVTKVIGELSREGYIRSGYGKIQLLDLKGLEELAESA 201
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 55-263 2.96e-40

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: 138.20  E-value: 2.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  55 FRTLAPEHQALVLAQSHVEQCEAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELRK 134
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 135 YEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQALAQLFNPAlypDTGPSL 214
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRL---DGRIDL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1525557239 215 SISQEELGMLVGVSRQRINQALQQLEKLGALRLAYNQIDVVDLDALARF 263
Cdd:COG0664   158 PLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 76-160 5.13e-11

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 57.62  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  76 EAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELRKYEVVAIQRSTVLFVPVDTFHA 155
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDFLE 84


                  ....*
gi 1525557239 156 LLDTS 160
Cdd:pfam00027  85 LLERD 89
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 54-168 1.61e-10

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: 56.95  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  54 WFRTLAPEHQALVLAQSHVEQCEAGDVIAHRLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRELR 133
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1525557239 134 KYEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVI 168
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 192-263 4.40e-09

Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.


Pssm-ID: 463917 [Multi-domain]  Cd Length: 68  Bit Score: 51.69  E-value: 4.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1525557239 192 ARVAQALAQLFNPAlyPDTGPSLSISQEELGMLVGVSRQRINQALQQLEKLGALRlaYNQIDVVDLDALARF 263
Cdd:pfam13545   1 QRLARFLLELAARD--GGGRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIE--RGRITILDPEALEAL 68
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 77-267 3.20e-05

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 43.66  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239  77 AGDVIAH--RLAPSAYWIGVHQGLLKLAIFNVSGRGCTFSGVPSGGWFGEGSVIKRElRKYEVVAIQRSTvlfvpVDTFH 154
Cdd:PRK13918   13 PGAVILYpgVPGPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAE-RAYFAEAVTDSR-----IDVLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 155 -ALLDTSLpfTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQALAQLFNPAL--YPDTGPS-LSISQEELGMLVGVSRQ 230
Cdd:PRK13918   87 pALMSAED--NLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLatQEDSGETmIYATHDELAAAVGSVRE 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1525557239 231 RINQALQQLEKLGALRLAYNQIDVVDLDALARFGMEQ 267
Cdd:PRK13918  165 TVTKVIGELSREGYIRSGYGKIQLLDLKGLEELAESA 201
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
118-243 4.99e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 40.35  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525557239 118 SGGWFGE-GSVIKRELRKYEVVAIQRSTVLFVPVDTFHALLDTSLPFTRFVIHQLNNRMGEFIASIQNSRLLDVDARVAQ 196
Cdd:PRK11753   68 QGDFIGElGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQ 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1525557239 197 AL---AQLFNPALYPDtGPSLSISQEELGMLVGVSRQRINQALQQLEKLG 243
Cdd:PRK11753  148 TLldlAKQPDAMTHPD-GMQIKITRQEIGRIVGCSREMVGRVLKMLEDQG 196
BirA COG1654
Biotin operon repressor [Transcription];
216-243 8.75e-03

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 36.89  E-value: 8.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 1525557239 216 ISQEELGMLVGVSRQRINQALQQLEKLG 243
Cdd:COG1654    19 HSGEELAEELGVSRAAVWKHIKALRELG 46
 
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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