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Conserved domains on  [gi|446567969|ref|WP_000645315|]
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MULTISPECIES: cyclic nucleotide-binding domain-containing protein [Leptospira]

Protein Classification

cyclic nucleotide-binding domain-containing protein( domain architecture ID 10034975)

cyclic nucleotide-binding domain-containing protein binds cyclic nucleotides (cAMP or cGMP) where binding of the effector leads to conformational changes; may be involved in regulating transcription, be present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK), or be part of vertebrate cyclic nucleotide-gated ion-channels.

CATH:  2.60.120.10
Gene Ontology:  GO:0030552|GO:0030551
PubMed:  6280140|12087135|17601606|11734894
SCOP:  4000272

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 32-145 6.47e-22

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: 85.07  E-value: 6.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  32 VFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERR 110
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVeVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446567969 111 TASAFALEKTTLLGFFQPDLKEIIETKPRIGIEIL 145
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 32-145 6.47e-22

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: 85.07  E-value: 6.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  32 VFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERR 110
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVeVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446567969 111 TASAFALEKTTLLGFFQPDLKEIIETKPRIGIEIL 145
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 50-136 1.37e-20

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: 81.12  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969   50 VREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERRTASAFALEKTTLLGFFQP 128
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVkVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*...
gi 446567969  129 DLKEIIET 136
Cdd:pfam00027  81 DFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 33-164 2.45e-18

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: 78.49  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  33 FGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERRT 111
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVkLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446567969 112 ASAFALEKTTLLGFFQPDLKEIIETKPRIGIEILMSLStvivERLHRTNGLLE 164
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLA----RRLRQLQERLV 129
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 32-148 1.19e-14

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: 66.66  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969    32 VFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERR 110
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVeVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 446567969   111 --TASAFALEKTTLLGFFQPDLKEIIETKPRIGIEILMSL 148
Cdd:smart00100  81 aaSAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
49-160 6.89e-10

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.76  E-value: 6.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  49 HVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTE-ERRTASAFALEKTTLLGFF 126
Cdd:PRK11753  21 HIHKYPAKSTLIHAGEKAETLYYIVKGSVaVLIKDEEGKEMILSYLNQGDFIGELGLFEEgQERSAWVRAKTACEVAEIS 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446567969 127 QPDLKEIIETKPrigiEILMSLSTVIVERLHRTN 160
Cdd:PRK11753 101 YKKFRQLIQVNP----DILMALSAQMARRLQNTS 130
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 49-160 1.10e-03

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 38.34  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969   49 HVREYQEGETVFRQGEVGAGFYLVYEG--SVVIRSVRDG---IELDLAHLDRHAFFGELSLFTEERRTASAFALEKTTLL 123
Cdd:TIGR03896   9 HQREIAAGTTLIEEGKAADFLFILLDGtfTVTTPQPEDNpltRAFELARLSRGEIVGEMSLLETRPPVATIKAVPKSRVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446567969  124 GFFQPDLKEIIETKPRIGIEILMSLSTVIVERLHRTN 160
Cdd:TIGR03896  89 SIPVGELAAKLQSDVGFAAHFYRAIAIKLALQIQNQN 125
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 32-145 6.47e-22

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: 85.07  E-value: 6.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  32 VFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERR 110
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVeVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446567969 111 TASAFALEKTTLLGFFQPDLKEIIETKPRIGIEIL 145
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 50-136 1.37e-20

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: 81.12  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969   50 VREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERRTASAFALEKTTLLGFFQP 128
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVkVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*...
gi 446567969  129 DLKEIIET 136
Cdd:pfam00027  81 DFLELLER 88
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 33-164 2.45e-18

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: 78.49  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  33 FGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERRT 111
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVkLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446567969 112 ASAFALEKTTLLGFFQPDLKEIIETKPRIGIEILMSLStvivERLHRTNGLLE 164
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLA----RRLRQLQERLV 129
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 32-148 1.19e-14

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: 66.66  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969    32 VFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTEERR 110
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVeVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 446567969   111 --TASAFALEKTTLLGFFQPDLKEIIETKPRIGIEILMSL 148
Cdd:smart00100  81 aaSAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
49-160 6.89e-10

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 55.76  E-value: 6.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  49 HVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAHLDRHAFFGELSLFTE-ERRTASAFALEKTTLLGFF 126
Cdd:PRK11753  21 HIHKYPAKSTLIHAGEKAETLYYIVKGSVaVLIKDEEGKEMILSYLNQGDFIGELGLFEEgQERSAWVRAKTACEVAEIS 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446567969 127 QPDLKEIIETKPrigiEILMSLSTVIVERLHRTN 160
Cdd:PRK11753 101 YKKFRQLIQVNP----DILMALSAQMARRLQNTS 130
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 21-100 2.56e-06

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 46.25  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969  21 QEIIRFLRETSVFGRMKKRTLIEIARMIHVREYQEGETVFRQGEVGAGFYLVYEGSV-VIRSVRDGIELDLAhLDRHAFF 99
Cdd:PLN02868   4 ESVVEFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAeVSGPAEEESRPEFL-LKRYDYF 82


                 .
gi 446567969 100 G 100
Cdd:PLN02868  83 G 83
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 49-160 1.10e-03

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 38.34  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446567969   49 HVREYQEGETVFRQGEVGAGFYLVYEG--SVVIRSVRDG---IELDLAHLDRHAFFGELSLFTEERRTASAFALEKTTLL 123
Cdd:TIGR03896   9 HQREIAAGTTLIEEGKAADFLFILLDGtfTVTTPQPEDNpltRAFELARLSRGEIVGEMSLLETRPPVATIKAVPKSRVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446567969  124 GFFQPDLKEIIETKPRIGIEILMSLSTVIVERLHRTN 160
Cdd:TIGR03896  89 SIPVGELAAKLQSDVGFAAHFYRAIAIKLALQIQNQN 125
 
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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