NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21751890|dbj|BAC04062|]
View 

unnamed protein product [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 331-434 5.37e-09

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: 53.87  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890 331 IYELIALLKWKKFPPGHVIVESGNIISFVGYINSGCCNIYRSiigfvklrsnkvKRSQKLVYMGKLKEKESFGEISVLLQ 410
Cdd:cd00038  10 LEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELALLGN 77

                        90       100
                ....*....|....*....|....
gi 21751890 411 VPFTCTIITKKEVEMAIIeDKDLF 434
Cdd:cd00038  78 GPRSATVRALTDSELLVL-PRSDF 100
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 331-434 5.37e-09

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: 53.87  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890 331 IYELIALLKWKKFPPGHVIVESGNIISFVGYINSGCCNIYRSiigfvklrsnkvKRSQKLVYMGKLKEKESFGEISVLLQ 410
Cdd:cd00038  10 LEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELALLGN 77

                        90       100
                ....*....|....*....|....
gi 21751890 411 VPFTCTIITKKEVEMAIIeDKDLF 434
Cdd:cd00038  78 GPRSATVRALTDSELLVL-PRSDF 100
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 333-433 4.18e-07

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: 50.37  E-value: 4.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890 333 ELIALLKWKKFPPGHVIVESGNIISFVGYINSGCCNIYRS-------IIGFvklrsnkvkrsqklvymgkLKEKESFGEI 405
Cdd:COG0664  11 ALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIsedgreqILGF-------------------LGPGDFFGEL 71

                        90       100
                ....*....|....*....|....*...
gi 21751890 406 SVLLQVPFTCTIITKKEVEMAIIEDKDL 433
Cdd:COG0664  72 SLLGGEPSPATAEALEDSELLRIPREDL 99
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 341-434 1.72e-06

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: 46.06  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890   341 KKFPPGHVIVESGNIISFVGYINSGCCNIYRsiigfvklrsnkVKRSQKLVYMGKLKEKESFGEISVLLQVPFTCTIITK 420
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYR------------TLEDGREQILAVLGPGDFFGELALLGGEPRSATVVAL 69

                          90
                  ....*....|....
gi 21751890   421 KEVEMAIIeDKDLF 434
Cdd:pfam00027  70 TDSELLVI-PREDF 82
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 331-434 5.37e-09

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: 53.87  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890 331 IYELIALLKWKKFPPGHVIVESGNIISFVGYINSGCCNIYRSiigfvklrsnkvKRSQKLVYMGKLKEKESFGEISVLLQ 410
Cdd:cd00038  10 LEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELALLGN 77

                        90       100
                ....*....|....*....|....
gi 21751890 411 VPFTCTIITKKEVEMAIIeDKDLF 434
Cdd:cd00038  78 GPRSATVRALTDSELLVL-PRSDF 100
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 333-433 4.18e-07

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: 50.37  E-value: 4.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890 333 ELIALLKWKKFPPGHVIVESGNIISFVGYINSGCCNIYRS-------IIGFvklrsnkvkrsqklvymgkLKEKESFGEI 405
Cdd:COG0664  11 ALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRIsedgreqILGF-------------------LGPGDFFGEL 71

                        90       100
                ....*....|....*....|....*...
gi 21751890 406 SVLLQVPFTCTIITKKEVEMAIIEDKDL 433
Cdd:COG0664  72 SLLGGEPSPATAEALEDSELLRIPREDL 99
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 341-434 1.72e-06

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: 46.06  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21751890   341 KKFPPGHVIVESGNIISFVGYINSGCCNIYRsiigfvklrsnkVKRSQKLVYMGKLKEKESFGEISVLLQVPFTCTIITK 420
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYR------------TLEDGREQILAVLGPGDFFGELALLGGEPRSATVVAL 69

                          90
                  ....*....|....
gi 21751890   421 KEVEMAIIeDKDLF 434
Cdd:pfam00027  70 TDSELLVI-PREDF 82
 
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