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Conserved domains on  [gi|1840401234|ref|WP_170214757|]
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Crp/Fnr family transcriptional regulator [Kurthia gibsonii]

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 ...
 2-215 1.13e-38

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: 132.80  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   2 FDAVPQIVQQIFKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPlITY 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGG-EPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  82 PLSAKVLDCCTIFSISKEQLEHELSENlAALRECLTWIQIQRMRE-QTKLRDLLLYGKKGALSSILIRLANSYGEkktdk 160
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELLERN-PELARALLRLLARRLRQlQERLVSLAFLSAEERLARFLLELADRLDG----- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840401234 161 siQISEKFTHSELASLCATSREVVNRLLQEFKKEKVISEENGYLTIHRLDYLQQF 215
Cdd:COG0664   154 --RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 2-215 1.13e-38

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: 132.80  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   2 FDAVPQIVQQIFKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPlITY 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGG-EPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  82 PLSAKVLDCCTIFSISKEQLEHELSENlAALRECLTWIQIQRMRE-QTKLRDLLLYGKKGALSSILIRLANSYGEkktdk 160
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELLERN-PELARALLRLLARRLRQlQERLVSLAFLSAEERLARFLLELADRLDG----- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840401234 161 siQISEKFTHSELASLCATSREVVNRLLQEFKKEKVISEENGYLTIHRLDYLQQF 215
Cdd:COG0664   154 --RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-114 3.60e-16

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: 71.59  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   1 MFDAVPQIVQQIFKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTpLIT 80
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLG-NGP 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1840401234  81 YPLSAKVLDCCTIFSISKEQLEHELSENLAALRE 114
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARR 113
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 19-108 5.17e-15

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: 68.02  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  19 KHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPlITYPLSAKVLDCCTIFSISK 98
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGG-EPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1840401234  99 EQLEHELSEN 108
Cdd:pfam00027  80 EDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 15-114 1.18e-12

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: 62.42  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   15 AHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPL-ITYPLSAKVLDCCTI 93
Cdd:smart00100  15 DALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSrRAASAAAVALELATL 94

                           90       100
                   ....*....|....*....|.
gi 1840401234   94 FSISKEQLEHELSENLAALRE 114
Cdd:smart00100  95 LRIDFRDFLQLLPELPQLLLE 115
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
13-198 6.27e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 51.14  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  13 FKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPLITYPLSAKVLDCCT 92
Cdd:PRK11753   16 FLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  93 IFSISKEQLeHELSENLAALRECLTWIQIQRMREQT-KLRDLLLYGKKGALSSILIRLAnsygeKKTD-----KSIQIse 166
Cdd:PRK11753   96 VAEISYKKF-RQLIQVNPDILMALSAQMARRLQNTSrKVGDLAFLDVTGRIAQTLLDLA-----KQPDamthpDGMQI-- 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840401234 167 KFTHSELASLCATSREVVNRLLQEFKKEKVIS 198
Cdd:PRK11753  168 KITRQEIGRIVGCSREMVGRVLKMLEDQGLIS 199
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 2-215 1.13e-38

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: 132.80  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   2 FDAVPQIVQQIFKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPlITY 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGG-EPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  82 PLSAKVLDCCTIFSISKEQLEHELSENlAALRECLTWIQIQRMRE-QTKLRDLLLYGKKGALSSILIRLANSYGEkktdk 160
Cdd:COG0664    80 PATAEALEDSELLRIPREDLEELLERN-PELARALLRLLARRLRQlQERLVSLAFLSAEERLARFLLELADRLDG----- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1840401234 161 siQISEKFTHSELASLCATSREVVNRLLQEFKKEKVISEENGYLTIHRLDYLQQF 215
Cdd:COG0664   154 --RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERL 206
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-114 3.60e-16

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: 71.59  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   1 MFDAVPQIVQQIFKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTpLIT 80
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLG-NGP 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1840401234  81 YPLSAKVLDCCTIFSISKEQLEHELSENLAALRE 114
Cdd:cd00038    80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARR 113
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 19-108 5.17e-15

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: 68.02  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  19 KHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPlITYPLSAKVLDCCTIFSISK 98
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGG-EPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1840401234  99 EQLEHELSEN 108
Cdd:pfam00027  80 EDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 15-114 1.18e-12

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: 62.42  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234   15 AHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPL-ITYPLSAKVLDCCTI 93
Cdd:smart00100  15 DALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSrRAASAAAVALELATL 94

                           90       100
                   ....*....|....*....|.
gi 1840401234   94 FSISKEQLEHELSENLAALRE 114
Cdd:smart00100  95 LRIDFRDFLQLLPELPQLLLE 115
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 142-215 2.06e-10

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: 54.77  E-value: 2.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840401234 142 LSSILIRLANSYGEkktdksIQISEKFTHSELASLCATSREVVNRLLQEFKKEKVIseENGYLTIHRLDYLQQF 215
Cdd:pfam13545   3 LARFLLELAARDGG------GRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLI--ERGRITILDPEALEAL 68
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
13-198 6.27e-08

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 51.14  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  13 FKAHGTKHHFVRHQHICTAGEAATHLYFVEKGRIAITKESVGGKELTLCIATKNDCIGESILFTPLITYPLSAKVLDCCT 92
Cdd:PRK11753   16 FLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840401234  93 IFSISKEQLeHELSENLAALRECLTWIQIQRMREQT-KLRDLLLYGKKGALSSILIRLAnsygeKKTD-----KSIQIse 166
Cdd:PRK11753   96 VAEISYKKF-RQLIQVNPDILMALSAQMARRLQNTSrKVGDLAFLDVTGRIAQTLLDLA-----KQPDamthpDGMQI-- 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840401234 167 KFTHSELASLCATSREVVNRLLQEFKKEKVIS 198
Cdd:PRK11753  168 KITRQEIGRIVGCSREMVGRVLKMLEDQGLIS 199
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 138-208 2.60e-06

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: 43.81  E-value: 2.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840401234 138 KKGALSSILIRLANSYGEKktdksIQISEKFTHSELASLCATSREVVNRLLQEFKKEKVIS-EENGYLTIHR 208
Cdd:cd00092     1 AKERLASFLLNLSLRYGAG-----DLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISrRGRGKYRVNP 67
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
161-207 1.60e-05

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 40.89  E-value: 1.60e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1840401234  161 SIQISEKFTHSELASLCATSREVVNRLLQEFKKEKVISEENGYLTIH 207
Cdd:smart00419   2 GIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVIL 48
 
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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