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Conserved domains on  [gi|2462508923|ref|XP_054192446|]
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potassium voltage-gated channel subfamily H member 1 isoform X3 [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

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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 ...
 77-187 1.46e-24

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: 98.17  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  77 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 151
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462508923 152 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 187
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 5-143 4.40e-07

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923   5 TNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLA 81
Cdd:PLN03192  307 TRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGV 385

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508923  82 SDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 143
Cdd:PLN03192  386 SREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 77-187 1.46e-24

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: 98.17  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  77 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 151
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462508923 152 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 187
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 78-194 1.36e-19

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: 84.37  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923   78 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 152
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462508923  153 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 194
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 78-191 1.61e-14

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: 72.33  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  78 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 152
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462508923 153 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 191
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 96-178 3.67e-14

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: 67.63  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  96 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 168
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 2462508923 169 KRDALQKVLE 178
Cdd:pfam00027  78 PREDFLELLE 87
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 5-143 4.40e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923   5 TNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLA 81
Cdd:PLN03192  307 TRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGV 385

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508923  82 SDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 143
Cdd:PLN03192  386 SREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
104-208 5.19e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.37  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923 104 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 178
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462508923 179 FYTAFSHSFSRNLIltynLRKRIVFRKISD 208
Cdd:PRK11753  110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 77-187 1.46e-24

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: 98.17  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  77 AFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWkeATLA 151
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreqIVGFLGPGDLFGELAL--LGNG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462508923 152 QSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSF 187
Cdd:cd00038    79 PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 78-194 1.36e-19

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: 84.37  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923   78 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDvfwkEATLAQ 152
Cdd:smart00100   2 FKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEdgeeqIVGTLGPGDFFGE----LALLTN 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462508923  153 --SCANVRALTYCdLHVIKRDALQKVLEFYTAFSHSFSRNLILT 194
Cdd:smart00100  78 srRAASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 78-191 1.61e-14

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: 72.33  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  78 FRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQ 152
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEdgreqILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462508923 153 scANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNL 191
Cdd:COG0664    81 --ATAEALEDSELLRIPREDLEELLERNPELARALLRLL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 96-178 3.67e-14

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: 67.63  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923  96 VHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVfwkeATLAQSC--ANVRALTYCDLHVI 168
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEdgreqILAVLGPGDFFGEL----ALLGGEPrsATVVALTDSELLVI 77

                          90
                  ....*....|
gi 2462508923 169 KRDALQKVLE 178
Cdd:pfam00027  78 PREDFLELLE 87
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 5-143 4.40e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923   5 TNRYHEMLNSVR---DFLKLYQVPKGLSERVMDYIVSTWSmSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLA 81
Cdd:PLN03192  307 TRRTMEFRNSIEaasNFVGRNRLPPRLKDQILAYMCLRFK-AESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGV 385

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508923  82 SDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVI----QDDEVVAILGKGDVFGDV 143
Cdd:PLN03192  386 SREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIdsegEKERVVGTLGCGDIFGEV 451
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
104-208 5.19e-07

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 50.37  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508923 104 IYHAGESVDSLCFVVSGSLEVIQDDE-----VVAILGKGDVFGDVFWKEATLAQScANVRALTYCDLHVIKRDALQKVLE 178
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEegkemILSYLNQGDFIGELGLFEEGQERS-AWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462508923 179 FYTAFSHSFSRNLIltynLRKRIVFRKISD 208
Cdd:PRK11753  110 VNPDILMALSAQMA----RRLQNTSRKVGD 135
 
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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