NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2270895521|ref|WP_254247649|]
View 

Crp/Fnr family transcriptional regulator [Loktanella salsilacus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 47-251 2.80e-31

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: 115.08  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLeGQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIGLNRP-PH 124
Cdd:COG0664     4 LSDEELEALLAH-LELRTLKKGEVLFREGDPADHLYFVLSGLVkLYRISEDGREQILG-FLGPGDFFGELSLLGGEPsPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 125 ETTMQTDGSVHLLSRKALCDFGAQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLtikakseQISEHASDR 204
Cdd:COG0664    82 TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLL-------ELADRLDGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2270895521 205 FPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSLTRPNVKINERS 251
Cdd:COG0664   155 IDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDRE 201
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 47-251 2.80e-31

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: 115.08  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLeGQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIGLNRP-PH 124
Cdd:COG0664     4 LSDEELEALLAH-LELRTLKKGEVLFREGDPADHLYFVLSGLVkLYRISEDGREQILG-FLGPGDFFGELSLLGGEPsPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 125 ETTMQTDGSVHLLSRKALCDFGAQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLtikakseQISEHASDR 204
Cdd:COG0664    82 TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLL-------ELADRLDGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2270895521 205 FPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSLTRPNVKINERS 251
Cdd:COG0664   155 IDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDRE 201
fixK PRK09391
transcriptional regulator FixK; Provisional
 71-240 3.19e-09

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 55.82  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  71 VFSDSKPNDRIAIVRSGwAVS--RVRSDGNQTtISQIFMAGDIIGLSdiglNRPPHETTMQ--TDGSVHLLSRKALCDFG 146
Cdd:PRK09391   49 IYGEGEPADYVYQVESG-AVRtyRLLSDGRRQ-IGAFHLPGDVFGLE----SGSTHRFTAEaiVDTTVRLIKRRSLEQAA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 147 AQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLTIkakSEQISehASDRFPLPLSQKEIGDALGLTDIYVN 226
Cdd:PRK09391  123 ATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEM---DERLG--GAGMMALPMSRRDIADYLGLTIETVS 197

                         170
                  ....*....|....
gi 2270895521 227 RLLRGLQKSGQLSL 240
Cdd:PRK09391  198 RALSQLQDRGLIGL 211
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 47-152 2.43e-07

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: 48.48  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLeGQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIgLNRPPHE 125
Cdd:cd00038     5 LDDEELEELADA-LEERRFPAGEVIIRQGDPADSLYIVLSGSVeVYKLDEDGREQIVG-FLGPGDLFGELAL-LGNGPRS 81

                          90       100
                  ....*....|....*....|....*....
gi 2270895521 126 TTMQ--TDGSVHLLSRKALCDFGAQHPRL 152
Cdd:cd00038    82 ATVRalTDSELLVLPRSDFRRLLQEYPEL 110
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 182-236 2.14e-05

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: 41.67  E-value: 2.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2270895521 182 RLMHFLLTIKAKSEQIsehasdRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSG 236
Cdd:pfam13545   2 RLARFLLELAARDGGG------RIDLPLTQEDLADLLGTTRETVSRVLSELRREG 50
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
202-242 1.46e-03

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 35.88  E-value: 1.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2270895521  202 SDRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSLTR 242
Cdd:smart00419   2 GIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREG 42
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 47-251 2.80e-31

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: 115.08  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLeGQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIGLNRP-PH 124
Cdd:COG0664     4 LSDEELEALLAH-LELRTLKKGEVLFREGDPADHLYFVLSGLVkLYRISEDGREQILG-FLGPGDFFGELSLLGGEPsPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 125 ETTMQTDGSVHLLSRKALCDFGAQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLtikakseQISEHASDR 204
Cdd:COG0664    82 TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLL-------ELADRLDGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2270895521 205 FPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSLTRPNVKINERS 251
Cdd:COG0664   155 IDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDRE 201
fixK PRK09391
transcriptional regulator FixK; Provisional
 71-240 3.19e-09

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 55.82  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  71 VFSDSKPNDRIAIVRSGwAVS--RVRSDGNQTtISQIFMAGDIIGLSdiglNRPPHETTMQ--TDGSVHLLSRKALCDFG 146
Cdd:PRK09391   49 IYGEGEPADYVYQVESG-AVRtyRLLSDGRRQ-IGAFHLPGDVFGLE----SGSTHRFTAEaiVDTTVRLIKRRSLEQAA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 147 AQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLTIkakSEQISehASDRFPLPLSQKEIGDALGLTDIYVN 226
Cdd:PRK09391  123 ATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEM---DERLG--GAGMMALPMSRRDIADYLGLTIETVS 197

                         170
                  ....*....|....
gi 2270895521 227 RLLRGLQKSGQLSL 240
Cdd:PRK09391  198 RALSQLQDRGLIGL 211
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 47-152 2.43e-07

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: 48.48  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLeGQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIgLNRPPHE 125
Cdd:cd00038     5 LDDEELEELADA-LEERRFPAGEVIIRQGDPADSLYIVLSGSVeVYKLDEDGREQIVG-FLGPGDLFGELAL-LGNGPRS 81

                          90       100
                  ....*....|....*....|....*....
gi 2270895521 126 TTMQ--TDGSVHLLSRKALCDFGAQHPRL 152
Cdd:cd00038    82 ATVRalTDSELLVLPRSDFRRLLQEYPEL 110
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
47-239 8.54e-07

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 48.94  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521  47 LTDTERDALSRLEGQAVALGKRDHVFSDSKPNDRIAIVRSGWAVSRVRSDGNQTTISQIFMAGDIIGLSDIGLNRPPH-- 124
Cdd:PRK11161   24 LNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGQHPSfa 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521 125 ---ETTMqtdgsVHLLSRKALCDFGAQHPRLFALILSLASLDATALNDRLHAITRYSAEDRLMHFLLTIkakSEQISEH- 200
Cdd:PRK11161  104 qalETSM-----VCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNL---SRRFAQRg 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2270895521 201 -ASDRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLS 239
Cdd:PRK11161  176 fSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLA 215
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 182-236 2.14e-05

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: 41.67  E-value: 2.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2270895521 182 RLMHFLLTIKAKSEQIsehasdRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSG 236
Cdd:pfam13545   2 RLARFLLELAARDGGG------RIDLPLTQEDLADLLGTTRETVSRVLSELRREG 50
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 63-138 7.90e-05

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: 40.67  E-value: 7.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270895521  63 VALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIgLNRPPHETTMQTDGSVHLLS 138
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVkVYRTLEDGREQILA-VLGPGDFFGELAL-LGGEPRSATVVALTDSELLV 76
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 179-240 6.28e-04

helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.


Pssm-ID: 238044 [Multi-domain]  Cd Length: 67  Bit Score: 37.26  E-value: 6.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2270895521 179 AEDRLMHFLLTIKAkseqiSEHASDRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSL 240
Cdd:cd00092     1 AKERLASFLLNLSL-----RYGAGDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISR 57
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
202-242 1.46e-03

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 35.88  E-value: 1.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2270895521  202 SDRFPLPLSQKEIGDALGLTDIYVNRLLRGLQKSGQLSLTR 242
Cdd:smart00419   2 GIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREG 42
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 47-157 9.32e-03

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 35.45  E-value: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270895521   47 LTDTERDALSRLEgQAVALGKRDHVFSDSKPNDRIAIVRSGWA-VSRVRSDGNQTTISqIFMAGDIIGLSDIGLNRPPHE 125
Cdd:smart00100   5 LDAEELRELADAL-EPVRYPAGEVIIRQGDVGDSFYIIVSGEVeVYKVLEDGEEQIVG-TLGPGDFFGELALLTNSRRAA 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2270895521  126 TTMQ---TDGSVHLLSRKALCDFGAQHPRLFALIL 157
Cdd:smart00100  83 SAAAvalELATLLRIDFRDFLQLLPELPQLLLELL 117
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH