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Conserved domains on  [gi|30696428|ref|NP_851188|]
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cyclic nucleotide-gated cation channel 4 [Arabidopsis thaliana]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13328258)

cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

CATH:  2.60.120.10
Gene Ontology:  GO:0016020|GO:0030551|GO:0005216|GO:0006811|GO:0022832
PubMed:  12087135|17601606
SCOP:  4000272
TCDB:  1.A.1

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 ...
 496-602 9.29e-15

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: 70.82  E-value: 9.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428 496 LFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDG-VKSCCMLGPGNFSGDELLSwclrr 574
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALL----- 75

                        90       100
                ....*....|....*....|....*...
gi 30696428 575 pfveRLPPSSSTLVTLETTEAFGLDAED 602
Cdd:cd00038  76 ----GNGPRSATVRALTDSELLVLPRSD 99
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 370-565 3.41e-04

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  370 IFWGLMTLST--FGNLESTTEwSEVVFNIIVLTSGLLLVTMLIGNIKVFLHATTSKKQAMHLKMRNIEWWMKKRHLPIGF 447
Cdd:PLN03192 255 IYWSITTMTTvgYGDLHAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  448 RQRVRNYERQRWAAmRGVDECEMVQNLPEGLRRDIKYHLCLDLVRQVPLFQHMDDLVLENICDRVKSLIFTKGETIQKEG 527
Cdd:PLN03192 334 KDQILAYMCLRFKA-ESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQN 412

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30696428  528 DAVQRMLFVVRGHLQ--SSQLLRDGVKSccMLGPGNFSGD 565
Cdd:PLN03192 413 EAPDDVYIVVSGEVEiiDSEGEKERVVG--TLGCGDIFGE 450
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 496-602 9.29e-15

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: 70.82  E-value: 9.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428 496 LFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDG-VKSCCMLGPGNFSGDELLSwclrr 574
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALL----- 75

                        90       100
                ....*....|....*....|....*...
gi 30696428 575 pfveRLPPSSSTLVTLETTEAFGLDAED 602
Cdd:cd00038  76 ----GNGPRSATVRALTDSELLVLPRSD 99
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 497-604 1.24e-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: 52.68  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428 497 FQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGV-KSCCMLGPGNFSGDelLSWCLRRp 575
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGReQILGFLGPGDFFGE--LSLLGGE- 77

                        90       100
                ....*....|....*....|....*....
gi 30696428 576 fverlpPSSSTLVTLETTEAFGLDAEDVK 604
Cdd:COG0664  78 ------PSPATAEALEDSELLRIPREDLE 100
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 496-603 2.30e-07

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: 50.09  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428    496 LFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDG-VKSCCMLGPGNFSGDELLSWCLRR 574
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100
                   ....*....|....*....|....*....
gi 30696428    575 pfverlpPSSSTLVTLETTEAFGLDAEDV 603
Cdd:smart00100  81 -------AASAAAVALELATLLRIDFRDF 102
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 517-603 1.62e-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: 46.45  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428   517 FTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGVKSC-CMLGPGNFSGDellswclrRPFVERlPPSSSTLVTLETTEA 595
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQIlAVLGPGDFFGE--------LALLGG-EPRSATVVALTDSEL 74


                  ....*...
gi 30696428   596 FGLDAEDV 603
Cdd:pfam00027  75 LVIPREDF 82
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 370-565 3.41e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  370 IFWGLMTLST--FGNLESTTEwSEVVFNIIVLTSGLLLVTMLIGNIKVFLHATTSKKQAMHLKMRNIEWWMKKRHLPIGF 447
Cdd:PLN03192 255 IYWSITTMTTvgYGDLHAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  448 RQRVRNYERQRWAAmRGVDECEMVQNLPEGLRRDIKYHLCLDLVRQVPLFQHMDDLVLENICDRVKSLIFTKGETIQKEG 527
Cdd:PLN03192 334 KDQILAYMCLRFKA-ESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQN 412

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30696428  528 DAVQRMLFVVRGHLQ--SSQLLRDGVKSccMLGPGNFSGD 565
Cdd:PLN03192 413 EAPDDVYIVVSGEVEiiDSEGEKERVVG--TLGCGDIFGE 450
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 496-602 9.29e-15

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: 70.82  E-value: 9.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428 496 LFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDG-VKSCCMLGPGNFSGDELLSwclrr 574
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELALL----- 75

                        90       100
                ....*....|....*....|....*...
gi 30696428 575 pfveRLPPSSSTLVTLETTEAFGLDAED 602
Cdd:cd00038  76 ----GNGPRSATVRALTDSELLVLPRSD 99
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 497-604 1.24e-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: 52.68  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428 497 FQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGV-KSCCMLGPGNFSGDelLSWCLRRp 575
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGReQILGFLGPGDFFGE--LSLLGGE- 77

                        90       100
                ....*....|....*....|....*....
gi 30696428 576 fverlpPSSSTLVTLETTEAFGLDAEDVK 604
Cdd:COG0664  78 ------PSPATAEALEDSELLRIPREDLE 100
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 496-603 2.30e-07

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: 50.09  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428    496 LFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDG-VKSCCMLGPGNFSGDELLSWCLRR 574
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100
                   ....*....|....*....|....*....
gi 30696428    575 pfverlpPSSSTLVTLETTEAFGLDAEDV 603
Cdd:smart00100  81 -------AASAAAVALELATLLRIDFRDF 102
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 517-603 1.62e-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: 46.45  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428   517 FTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGVKSC-CMLGPGNFSGDellswclrRPFVERlPPSSSTLVTLETTEA 595
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQIlAVLGPGDFFGE--------LALLGG-EPRSATVVALTDSEL 74


                  ....*...
gi 30696428   596 FGLDAEDV 603
Cdd:pfam00027  75 LVIPREDF 82
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 370-565 3.41e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  370 IFWGLMTLST--FGNLESTTEwSEVVFNIIVLTSGLLLVTMLIGNIKVFLHATTSKKQAMHLKMRNIEWWMKKRHLPIGF 447
Cdd:PLN03192 255 IYWSITTMTTvgYGDLHAVNT-IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRL 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696428  448 RQRVRNYERQRWAAmRGVDECEMVQNLPEGLRRDIKYHLCLDLVRQVPLFQHMDDLVLENICDRVKSLIFTKGETIQKEG 527
Cdd:PLN03192 334 KDQILAYMCLRFKA-ESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQN 412

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30696428  528 DAVQRMLFVVRGHLQ--SSQLLRDGVKSccMLGPGNFSGD 565
Cdd:PLN03192 413 EAPDDVYIVVSGEVEiiDSEGEKERVVG--TLGCGDIFGE 450
 
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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