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Conserved domains on  [gi|1907143297|ref|XP_036018459|]
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cyclic nucleotide-binding domain-containing protein 2 isoform X2 [Mus musculus]

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 ...
 200-308 7.04e-19

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: 82.37  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 200 ILQALDcyrsytESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLDphptLLHRGGSFG 278
Cdd:cd00038     1 LFSGLD------DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVG----FLGPGDLFG 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907143297 279 EMGLLSTTVRSATVVCMEETEFLVVDREDF 308
Cdd:cd00038    71 ELALLGNGPRSATVRALTDSELLVLPRSDF 100
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 200-308 7.04e-19

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: 82.37  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 200 ILQALDcyrsytESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLDphptLLHRGGSFG 278
Cdd:cd00038     1 LFSGLD------DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVG----FLGPGDLFG 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907143297 279 EMGLLSTTVRSATVVCMEETEFLVVDREDF 308
Cdd:cd00038    71 ELALLGNGPRSATVRALTDSELLVLPRSDF 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 224-308 1.09e-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: 72.64  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 224 FERFGRRRVIVKKGQMGNSFYFIYLGTVAI-TEDEDGSSAFLDphptLLHRGGSFGEMGLLSTTVRSATVVCMEETEFLV 302
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyRTLEDGREQILA----VLGPGDFFGELALLGGEPRSATVVALTDSELLV 76


                  ....*.
gi 1907143297 303 VDREDF 308
Cdd:pfam00027  77 IPREDF 82
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 207-354 2.06e-12

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: 66.55  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 207 YRSYTESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAI-TEDEDGSSAFLDphptLLHRGGSFGEMGLLST 285
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyRISEDGREQILG----FLGPGDFFGELSLLGG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143297 286 TVRSATVVCMEETEFLVVDREDFVanklgDEVQKETQYRYNFFRNLDIFQSWSEEKLWKLV---ALGRIERF 354
Cdd:COG0664    77 EPSPATAEALEDSELLRIPREDLE-----ELLERNPELARALLRLLARRLRQLQERLVSLAflsAEERLARF 143
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 208-308 6.52e-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: 62.80  E-value: 6.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297  208 RSYTESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLDphptLLHRGGSFGEMGLL--S 284
Cdd:smart00100   3 KNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVG----TLGPGDFFGELALLtnS 78

                           90       100
                   ....*....|....*....|....
gi 1907143297  285 TTVRSATVVCMEETEFLVVDREDF 308
Cdd:smart00100  79 RRAASAAAVALELATLLRIDFRDF 102
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 218-306 1.26e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.79  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 218 LAKVIRFERFGRRRVIVKKGQMGNSFYFIYLG--TVAITEDEDGSSAFldphptLLHRGGSFGEmGLLStTVRSATVVCM 295
Cdd:PLN02868   27 IAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGeaEVSGPAEEESRPEF------LLKRYDYFGY-GLSG-SVHSADVVAV 98

                          90
                  ....*....|.
gi 1907143297 296 EETEFLVVDRE 306
Cdd:PLN02868   99 SELTCLVLPHE 109
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 200-308 7.04e-19

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: 82.37  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 200 ILQALDcyrsytESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLDphptLLHRGGSFG 278
Cdd:cd00038     1 LFSGLD------DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVG----FLGPGDLFG 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907143297 279 EMGLLSTTVRSATVVCMEETEFLVVDREDF 308
Cdd:cd00038    71 ELALLGNGPRSATVRALTDSELLVLPRSDF 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 224-308 1.09e-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: 72.64  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 224 FERFGRRRVIVKKGQMGNSFYFIYLGTVAI-TEDEDGSSAFLDphptLLHRGGSFGEMGLLSTTVRSATVVCMEETEFLV 302
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyRTLEDGREQILA----VLGPGDFFGELALLGGEPRSATVVALTDSELLV 76


                  ....*.
gi 1907143297 303 VDREDF 308
Cdd:pfam00027  77 IPREDF 82
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 207-354 2.06e-12

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: 66.55  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 207 YRSYTESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAI-TEDEDGSSAFLDphptLLHRGGSFGEMGLLST 285
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyRISEDGREQILG----FLGPGDFFGELSLLGG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143297 286 TVRSATVVCMEETEFLVVDREDFVanklgDEVQKETQYRYNFFRNLDIFQSWSEEKLWKLV---ALGRIERF 354
Cdd:COG0664    77 EPSPATAEALEDSELLRIPREDLE-----ELLERNPELARALLRLLARRLRQLQERLVSLAflsAEERLARF 143
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 208-308 6.52e-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: 62.80  E-value: 6.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297  208 RSYTESLQLLLAKVIRFERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLDphptLLHRGGSFGEMGLL--S 284
Cdd:smart00100   3 KNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVG----TLGPGDFFGELALLtnS 78

                           90       100
                   ....*....|....*....|....
gi 1907143297  285 TTVRSATVVCMEETEFLVVDREDF 308
Cdd:smart00100  79 RRAASAAAVALELATLLRIDFRDF 102
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 218-306 1.26e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.79  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 218 LAKVIRFERFGRRRVIVKKGQMGNSFYFIYLG--TVAITEDEDGSSAFldphptLLHRGGSFGEmGLLStTVRSATVVCM 295
Cdd:PLN02868   27 IAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGeaEVSGPAEEESRPEF------LLKRYDYFGY-GLSG-SVHSADVVAV 98

                          90
                  ....*....|.
gi 1907143297 296 EETEFLVVDRE 306
Cdd:PLN02868   99 SELTCLVLPHE 109
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
212-299 5.25e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 41.89  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143297 212 ESLQLLLAKVIRfERFGRRRVIVKKGQMGNSFYFIYLGTVAIT-EDEDGSSAFLdphpTLLHRGGSFGEMGLL-STTVRS 289
Cdd:PRK11753   11 PTLEWFLSHCHI-HKYPAKSTLIHAGEKAETLYYIVKGSVAVLiKDEEGKEMIL----SYLNQGDFIGELGLFeEGQERS 85

                          90
                  ....*....|
gi 1907143297 290 ATVVCMEETE 299
Cdd:PRK11753   86 AWVRAKTACE 95
 
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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