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Conserved domains on  [gi|17137122|ref|NP_477116|]
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cyclic nucleotide-gated ion channel subunit A, isoform A [Drosophila melanogaster]

Protein Classification

cyclic nucleotide-gated cation channel family protein( domain architecture ID 11998063)

cyclic nucleotide-gated cation channel family protein is a nonselective cation channel opened by binding of intracellular cyclic GMP or cyclic AMP, similar to human cGMP-gated cation channel alpha-1, a subunit of the rod cyclic GMP-gated cation channel which is involved in the final stage of the phototransduction pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 107-354 1.19e-30

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 120.45  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   107 HYRWLAIVSLAVLYNIIFVVGRAVFWEiNKSAPAFWYTLDYLCDFIYLLDTLVHMHegfldqgllvrdAFRLRRHYFHTK 186
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKII------------AAGFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   187 GWYLDVLSMLPTDLAYIWWPPETcsslylpcPVIVRLNRLLRINRLWEWFDRTETATGYPNA-FRICKVVLAILVLIHWN 265
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGS--------LSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   266 ACMYFAISYEI-GFSSDSWVYNLNGTRNntlQRQYIYSFYWSTLTLTTIG--ETPTPENDVE------YLFVVADFLAGV 336
Cdd:pfam00520 140 LFIFAIIGYQLfGGKLKTWENPDNGRTN---FDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGF 216

                         250
                  ....*....|....*...
gi 17137122   337 LIFATIVGNIGSMISNMN 354
Cdd:pfam00520 217 LLLNLFIAVIIDNFQELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 545-615 7.69e-27

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


:

Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.79  E-value: 7.69e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137122   545 LTQRGCQLLRKDGLLDEQIfADSQRVHDSIEGGIEKLELSVENLNMRLARLLAEYTASQAKIKQRLAKLEM 615
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAA-ANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 429-542 4.51e-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: 97.40  E-value: 4.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 429 IFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagn 505
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkldEDGREQIVGFLGPGDLFGELALL----- 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17137122 506 rTGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEAR 542
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 107-354 1.19e-30

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 120.45  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   107 HYRWLAIVSLAVLYNIIFVVGRAVFWEiNKSAPAFWYTLDYLCDFIYLLDTLVHMHegfldqgllvrdAFRLRRHYFHTK 186
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKII------------AAGFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   187 GWYLDVLSMLPTDLAYIWWPPETcsslylpcPVIVRLNRLLRINRLWEWFDRTETATGYPNA-FRICKVVLAILVLIHWN 265
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGS--------LSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   266 ACMYFAISYEI-GFSSDSWVYNLNGTRNntlQRQYIYSFYWSTLTLTTIG--ETPTPENDVE------YLFVVADFLAGV 336
Cdd:pfam00520 140 LFIFAIIGYQLfGGKLKTWENPDNGRTN---FDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGF 216

                         250
                  ....*....|....*...
gi 17137122   337 LIFATIVGNIGSMISNMN 354
Cdd:pfam00520 217 LLLNLFIAVIIDNFQELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 545-615 7.69e-27

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.79  E-value: 7.69e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137122   545 LTQRGCQLLRKDGLLDEQIfADSQRVHDSIEGGIEKLELSVENLNMRLARLLAEYTASQAKIKQRLAKLEM 615
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAA-ANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 104-500 1.74e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.19  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  104 LQSHYRWL-AIVSLAVLYNIIFVVGRAVFweINKSAPAFWYTLDYLCDFIYLLDTLVHMHEGFLDQ--GLLVRDAFRLRR 180
Cdd:PLN03192  57 MDSRYRWWeTLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  181 HYFHTkgWYL-DVLSMLPTD-LAYIWWPPETCSSLYlpcpVIVRLNRLLRINRLWEWFDRTETATGYpNAFRI-CKVVLA 257
Cdd:PLN03192 135 RYLST--WFLmDVASTIPFQaLAYLITGTVKLNLSY----SLLGLLRFWRLRRVKQLFTRLEKDIRF-SYFWIrCARLLS 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  258 I-LVLIHWNACMYFAISYEIGFSSDSWV-YNLNGTRNNTLQRQYIYSFYWSTLTLTTIGETPT-PENDVEYLFVVADFLA 334
Cdd:PLN03192 208 VtLFLVHCAGCLYYLIADRYPHQGKTWIgAVIPNFRETSLWIRYISAIYWSITTMTTVGYGDLhAVNTIEMIFIIFYMLF 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  335 GVLIFATIVGNIGSMISNMNVARVEFQNRMDGVKQYMAFRRVGHELEARVIRWFAYTWsQSGALDEERVLAALPDKLKAE 414
Cdd:PLN03192 288 NLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRF-KAESLNQQQLIDQLPKSICKS 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  415 IAIQVHMDTLKQVRIFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVVGDDGI--TVLATLGAGS 492
Cdd:PLN03192 367 ICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEkeRVVGTLGCGD 446


                 ....*...
gi 17137122  493 VFGEVSVL 500
Cdd:PLN03192 447 IFGEVGAL 454
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 429-542 4.51e-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: 97.40  E-value: 4.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 429 IFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagn 505
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkldEDGREQIVGFLGPGDLFGELALL----- 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17137122 506 rTGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEAR 542
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 434-548 3.67e-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: 83.60  E-value: 3.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122    434 EPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagNRTGNR 510
Cdd:smart00100   6 DAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvlEDGEEQIVGTLGPGDFFGELALL----TNSRRA 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17137122    511 RTANVRSLGYSDLFCLAKRDLWETLSDYPEARSTLTQR 548
Cdd:smart00100  82 ASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 447-538 1.87e-16

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: 74.95  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   447 LQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagnrTGNRRTANVRSLGYSDL 523
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYrtlEDGREQILAVLGPGDFFGELALL------GGEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 17137122   524 FCLAKRDLWETLSDY 538
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 430-598 3.96e-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: 71.56  E-value: 3.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 430 FHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRG--KLSVVGDDGI-TVLATLGAGSVFGEVSVLeiagnr 506
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGlvKLYRISEDGReQILGFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 507 TGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEARSTLTQRGCQLLRKdglLDEQIFADSQRvhdSIEGgieklelsve 586
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ---LQERLVSLAFL---SAEE---------- 138

                       170
                ....*....|..
gi 17137122 587 nlnmRLARLLAE 598
Cdd:COG0664 139 ----RLARFLLE 146
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 107-354 1.19e-30

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 120.45  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   107 HYRWLAIVSLAVLYNIIFVVGRAVFWEiNKSAPAFWYTLDYLCDFIYLLDTLVHMHegfldqgllvrdAFRLRRHYFHTK 186
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKII------------AAGFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   187 GWYLDVLSMLPTDLAYIWWPPETcsslylpcPVIVRLNRLLRINRLWEWFDRTETATGYPNA-FRICKVVLAILVLIHWN 265
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGS--------LSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   266 ACMYFAISYEI-GFSSDSWVYNLNGTRNntlQRQYIYSFYWSTLTLTTIG--ETPTPENDVE------YLFVVADFLAGV 336
Cdd:pfam00520 140 LFIFAIIGYQLfGGKLKTWENPDNGRTN---FDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGF 216

                         250
                  ....*....|....*...
gi 17137122   337 LIFATIVGNIGSMISNMN 354
Cdd:pfam00520 217 LLLNLFIAVIIDNFQELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 545-615 7.69e-27

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.79  E-value: 7.69e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137122   545 LTQRGCQLLRKDGLLDEQIfADSQRVHDSIEGGIEKLELSVENLNMRLARLLAEYTASQAKIKQRLAKLEM 615
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAA-ANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 104-500 1.74e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.19  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  104 LQSHYRWL-AIVSLAVLYNIIFVVGRAVFweINKSAPAFWYTLDYLCDFIYLLDTLVHMHEGFLDQ--GLLVRDAFRLRR 180
Cdd:PLN03192  57 MDSRYRWWeTLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  181 HYFHTkgWYL-DVLSMLPTD-LAYIWWPPETCSSLYlpcpVIVRLNRLLRINRLWEWFDRTETATGYpNAFRI-CKVVLA 257
Cdd:PLN03192 135 RYLST--WFLmDVASTIPFQaLAYLITGTVKLNLSY----SLLGLLRFWRLRRVKQLFTRLEKDIRF-SYFWIrCARLLS 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  258 I-LVLIHWNACMYFAISYEIGFSSDSWV-YNLNGTRNNTLQRQYIYSFYWSTLTLTTIGETPT-PENDVEYLFVVADFLA 334
Cdd:PLN03192 208 VtLFLVHCAGCLYYLIADRYPHQGKTWIgAVIPNFRETSLWIRYISAIYWSITTMTTVGYGDLhAVNTIEMIFIIFYMLF 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  335 GVLIFATIVGNIGSMISNMNVARVEFQNRMDGVKQYMAFRRVGHELEARVIRWFAYTWsQSGALDEERVLAALPDKLKAE 414
Cdd:PLN03192 288 NLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYMCLRF-KAESLNQQQLIDQLPKSICKS 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122  415 IAIQVHMDTLKQVRIFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVVGDDGI--TVLATLGAGS 492
Cdd:PLN03192 367 ICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEkeRVVGTLGCGD 446


                 ....*...
gi 17137122  493 VFGEVSVL 500
Cdd:PLN03192 447 IFGEVGAL 454
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 429-542 4.51e-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: 97.40  E-value: 4.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 429 IFHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagn 505
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkldEDGREQIVGFLGPGDLFGELALL----- 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17137122 506 rTGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEAR 542
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELA 111
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 434-548 3.67e-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: 83.60  E-value: 3.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122    434 EPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagNRTGNR 510
Cdd:smart00100   6 DAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvlEDGEEQIVGTLGPGDFFGELALL----TNSRRA 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17137122    511 RTANVRSLGYSDLFCLAKRDLWETLSDYPEARSTLTQR 548
Cdd:smart00100  82 ASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 447-538 1.87e-16

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: 74.95  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122   447 LQVFSPGDYICRKGDVGKEMYIVKRGKLSVV---GDDGITVLATLGAGSVFGEVSVLeiagnrTGNRRTANVRSLGYSDL 523
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYrtlEDGREQILAVLGPGDFFGELALL------GGEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 17137122   524 FCLAKRDLWETLSDY 538
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 430-598 3.96e-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: 71.56  E-value: 3.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 430 FHDTEPGLLEALVLKLKLQVFSPGDYICRKGDVGKEMYIVKRG--KLSVVGDDGI-TVLATLGAGSVFGEVSVLeiagnr 506
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGlvKLYRISEDGReQILGFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137122 507 TGNRRTANVRSLGYSDLFCLAKRDLWETLSDYPEARSTLTQRGCQLLRKdglLDEQIFADSQRvhdSIEGgieklelsve 586
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQ---LQERLVSLAFL---SAEE---------- 138

                       170
                ....*....|..
gi 17137122 587 nlnmRLARLLAE 598
Cdd:COG0664 139 ----RLARFLLE 146
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 302-352 2.40e-03

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 37.25  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17137122   302 SFYWSTLTLTTIG-ETPTPENDVEYLFVVADFLAGVLIFATIVGNIGSMISN 352
Cdd:pfam07885  27 ALYFSFVTLTTVGyGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
 
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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