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Conserved domains on  [gi|334187699|ref|NP_974783|]
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Cyclic nucleotide-regulated ion channel family protein [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

 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 ...
 530-640 2.63e-17

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: 78.14  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 530 LFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG-VLATSTLEPGGYLGDELLswclrr 608
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELAL------ 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334187699 609 pFLDrlPPSSATFVCLENIEAFSLGSEDLRYI 640
Cdd:cd00038   75 -LGN--GPRSATVRALTDSELLVLPRSDFRRL 103
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 387-599 3.85e-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: 53.72  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 387 LPVISSNSLAVKILYPIFWGLMTLSTFA-NDLEpTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLhaVMAKKRKMQIR- 464
Cdd:PLN03192 239 IPNFRETSLWIRYISAIYWSITTMTTVGyGDLH-AVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRTMEFRn 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 465 -CRDMEWWMKRRQLPSRLRQRVR-----RFERQRWNalggedELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLI 538
Cdd:PLN03192 316 sIEAASNFVGRNRLPPRLKDQILaymclRFKAESLN------QQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREI 389

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187699 539 LDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGD 599
Cdd:PLN03192 390 LLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGE 450
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 530-640 2.63e-17

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: 78.14  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 530 LFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG-VLATSTLEPGGYLGDELLswclrr 608
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELAL------ 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334187699 609 pFLDrlPPSSATFVCLENIEAFSLGSEDLRYI 640
Cdd:cd00038   75 -LGN--GPRSATVRALTDSELLVLPRSDFRRL 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 531-638 7.39e-11

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: 62.31  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 531 FRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLAT-STLEPGGYLGDELLswclrrp 609
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQIlGFLGPGDFFGELSL------- 73

                         90       100
                 ....*....|....*....|....*....
gi 334187699 610 FLDRlpPSSATFVCLENIEAFSLGSEDLR 638
Cdd:COG0664   74 LGGE--PSPATAEALEDSELLRIPREDLE 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 548-638 3.72e-09

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: 54.15  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699  548 PRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG-VLATSTLEPGGYLGDellswclrRPFLDRlPPSSATFVCLEN 626
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGrEQILAVLGPGDFFGE--------LALLGG-EPRSATVVALTD 71

                          90
                  ....*....|..
gi 334187699  627 IEAFSLGSEDLR 638
Cdd:pfam00027  72 SELLVIPREDFL 83
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 530-609 4.77e-09

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: 54.71  E-value: 4.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699   530 LFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG---VLAtsTLEPGGYLGDELLSWCL 606
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeeqIVG--TLGPGDFFGELALLTNS 78


                   ...
gi 334187699   607 RRP 609
Cdd:smart00100  79 RRA 81
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 387-599 3.85e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 387 LPVISSNSLAVKILYPIFWGLMTLSTFA-NDLEpTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLhaVMAKKRKMQIR- 464
Cdd:PLN03192 239 IPNFRETSLWIRYISAIYWSITTMTTVGyGDLH-AVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRTMEFRn 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 465 -CRDMEWWMKRRQLPSRLRQRVR-----RFERQRWNalggedELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLI 538
Cdd:PLN03192 316 sIEAASNFVGRNRLPPRLKDQILaymclRFKAESLN------QQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREI 389

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187699 539 LDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGD 599
Cdd:PLN03192 390 LLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGE 450
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 523-603 5.83e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 39.70  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 523 DLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELL 602
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFLLKRYDYFGYGLS 87


                 .
gi 334187699 603 S 603
Cdd:PLN02868  88 G 88
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 530-640 2.63e-17

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: 78.14  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 530 LFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG-VLATSTLEPGGYLGDELLswclrr 608
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGrEQIVGFLGPGDLFGELAL------ 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334187699 609 pFLDrlPPSSATFVCLENIEAFSLGSEDLRYI 640
Cdd:cd00038   75 -LGN--GPRSATVRALTDSELLVLPRSDFRRL 103
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 531-638 7.39e-11

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: 62.31  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 531 FRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLAT-STLEPGGYLGDELLswclrrp 609
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQIlGFLGPGDFFGELSL------- 73

                         90       100
                 ....*....|....*....|....*....
gi 334187699 610 FLDRlpPSSATFVCLENIEAFSLGSEDLR 638
Cdd:COG0664   74 LGGE--PSPATAEALEDSELLRIPREDLE 100
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 548-638 3.72e-09

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: 54.15  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699  548 PRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG-VLATSTLEPGGYLGDellswclrRPFLDRlPPSSATFVCLEN 626
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGrEQILAVLGPGDFFGE--------LALLGG-EPRSATVVALTD 71

                          90
                  ....*....|..
gi 334187699  627 IEAFSLGSEDLR 638
Cdd:pfam00027  72 SELLVIPREDFL 83
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 530-609 4.77e-09

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: 54.71  E-value: 4.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699   530 LFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKG---VLAtsTLEPGGYLGDELLSWCL 606
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGeeqIVG--TLGPGDFFGELALLTNS 78


                   ...
gi 334187699   607 RRP 609
Cdd:smart00100  79 RRA 81
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 387-599 3.85e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 387 LPVISSNSLAVKILYPIFWGLMTLSTFA-NDLEpTSNWLEVIFSIVMVLSGLLLFTLLIGNIQVFLhaVMAKKRKMQIR- 464
Cdd:PLN03192 239 IPNFRETSLWIRYISAIYWSITTMTTVGyGDLH-AVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRTMEFRn 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 465 -CRDMEWWMKRRQLPSRLRQRVR-----RFERQRWNalggedELELIHDLPPGLRRDIKRYLCFDLINKVPLFRGMDDLI 538
Cdd:PLN03192 316 sIEAASNFVGRNRLPPRLKDQILaymclRFKAESLN------QQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREI 389

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187699 539 LDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGD 599
Cdd:PLN03192 390 LLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGE 450
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 523-603 5.83e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 39.70  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187699 523 DLINKVPLFRGMDDLILDNICDRAKPRVFSKDEKIIREGDPVQRMIFIMRGRVKRIQSLSKGVLATSTLEPGGYLGDELL 602
Cdd:PLN02868   8 EFLGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFLLKRYDYFGYGLS 87


                 .
gi 334187699 603 S 603
Cdd:PLN02868  88 G 88
 
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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