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Conserved domains on  [gi|33859524|ref|NP_034048|]
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cyclic nucleotide-gated channel alpha-3 isoform 2 [Mus musculus]

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
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 539-608 2.51e-35

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: 127.28  E-value: 2.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   539 LEEKGRQILMKDNLIDEDLVAARVDTRDVEEKVEYLESSLDILQTRFARLLAEYSASQMKLKQRLTRLES 608
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 109-349 9.95e-35

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: 131.62  E-value: 9.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   109 YYRWLTAIALPVFYNWCLLVCRACFDElQSEHLTLWLVLDYSADVLYVLDMLVRARTGfleqglmvrdtkRLWKHYTKTL 188
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAA------------GFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   189 HFKLDILSLIPTDLAY-LKLGVNYPELRFNRLLKFSRLFEFFDRTETRTNYPN-VFRIGNLVLYTLIIIHWNACIYFAIS 266
Cdd:pfam00520  68 WNILDFVVVLPSLISLvLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   267 KFIGFGT-DSWVYPNTSKPEYarlsRKYIYSLYWSTLTLTTIG--ETPPPVKDEE------YLFVVIDFLVGILIFATIV 337
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|..
gi 33859524   338 GNVGSMISNMNA 349
Cdd:pfam00520 224 AVIIDNFQELTE 235
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 423-539 2.00e-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: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524 423 IFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 499
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 33859524 500 ksGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRAL 539
Cdd:cd00038  77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 539-608 2.51e-35

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: 127.28  E-value: 2.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   539 LEEKGRQILMKDNLIDEDLVAARVDTRDVEEKVEYLESSLDILQTRFARLLAEYSASQMKLKQRLTRLES 608
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 109-349 9.95e-35

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: 131.62  E-value: 9.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   109 YYRWLTAIALPVFYNWCLLVCRACFDElQSEHLTLWLVLDYSADVLYVLDMLVRARTGfleqglmvrdtkRLWKHYTKTL 188
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAA------------GFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   189 HFKLDILSLIPTDLAY-LKLGVNYPELRFNRLLKFSRLFEFFDRTETRTNYPN-VFRIGNLVLYTLIIIHWNACIYFAIS 266
Cdd:pfam00520  68 WNILDFVVVLPSLISLvLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   267 KFIGFGT-DSWVYPNTSKPEYarlsRKYIYSLYWSTLTLTTIG--ETPPPVKDEE------YLFVVIDFLVGILIFATIV 337
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|..
gi 33859524   338 GNVGSMISNMNA 349
Cdd:pfam00520 224 AVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 88-534 4.39e-25

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 110.73  E-value: 4.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   88 PPDGGEGRKEEPI-----VVDPSSNIYYRWLTAIALPVFYN-WCLLVCRACFDELQSEHLTlwlVLDYSADVLYVLDMLV 161
Cdd:PLN03192  35 PPLGVPSYNQNHIgsdgwIISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLNASPKRGLE---IADNVVDLFFAVDIVL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  162 RARTGFLEQ--GLMVRDTKRLWKHYTKTLhFKLDILSLIPTD-LAYL-----KLGVNYPELRFNRLLKFSRLFEFFDRTE 233
Cdd:PLN03192 112 TFFVAYIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQaLAYLitgtvKLNLSYSLLGLLRFWRLRRVKQLFTRLE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  234 TRTNYpNVFRI--GNLVLYTLIIIHWNACIYFAISKFIGFGTDSW---VYPNTSKpeyARLSRKYIYSLYWSTLTLTTIG 308
Cdd:PLN03192 191 KDIRF-SYFWIrcARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWigaVIPNFRE---TSLWIRYISAIYWSITTMTTVG 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  309 ETP-PPVKDEEYLFVVIDFLVGILIFATIVGNVGSMISNMNAPRVEFQAKIDSVKQYMQFRKVTKDLETRVIRWFdYLWA 387
Cdd:PLN03192 267 YGDlHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM-CLRF 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  388 NRKTVDEKEVLKNLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGK 467
Cdd:PLN03192 346 KAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGE 425

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33859524  468 LAVVADDGVTQFVV--LSDGSYFGEISILnikgskSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPD 534
Cdd:PLN03192 426 VEIIDSEGEKERVVgtLGCGDIFGEVGAL------CCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 423-539 2.00e-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: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524 423 IFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 499
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 33859524 500 ksGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRAL 539
Cdd:cd00038  77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 423-542 6.85e-21

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: 88.61  E-value: 6.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524    423 IFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgs 499
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQIVgTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 33859524    500 KSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRALEEK 542
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 444-532 2.53e-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: 74.18  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   444 FSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgsksGNRRTANIRSIGYSDLFCL 520
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQILaVLGPGDFFGELALLG------GEPRSATVVALTDSELLVI 77

                          90
                  ....*....|..
gi 33859524   521 SKDDLMEALTEY 532
Cdd:pfam00027  78 PREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 424-574 2.78e-13

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: 69.25  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524 424 FQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVV--ADDGVTQFV-VLSDGSYFGEISILnikgsk 500
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33859524 501 SGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRALEekgrQILMKDNLIDEDLVAARVdTRDVEEKVEYL 574
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALL----RLLARRLRQLQERLVSLA-FLSAEERLARF 143
 
Name Accession Description Interval E-value
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 539-608 2.51e-35

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: 127.28  E-value: 2.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   539 LEEKGRQILMKDNLIDEDLVAARVDTRDVEEKVEYLESSLDILQTRFARLLAEYSASQMKLKQRLTRLES 608
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 109-349 9.95e-35

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: 131.62  E-value: 9.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   109 YYRWLTAIALPVFYNWCLLVCRACFDElQSEHLTLWLVLDYSADVLYVLDMLVRARTGfleqglmvrdtkRLWKHYTKTL 188
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAA------------GFKKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   189 HFKLDILSLIPTDLAY-LKLGVNYPELRFNRLLKFSRLFEFFDRTETRTNYPN-VFRIGNLVLYTLIIIHWNACIYFAIS 266
Cdd:pfam00520  68 WNILDFVVVLPSLISLvLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   267 KFIGFGT-DSWVYPNTSKPEYarlsRKYIYSLYWSTLTLTTIG--ETPPPVKDEE------YLFVVIDFLVGILIFATIV 337
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|..
gi 33859524   338 GNVGSMISNMNA 349
Cdd:pfam00520 224 AVIIDNFQELTE 235
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 88-534 4.39e-25

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 110.73  E-value: 4.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   88 PPDGGEGRKEEPI-----VVDPSSNIYYRWLTAIALPVFYN-WCLLVCRACFDELQSEHLTlwlVLDYSADVLYVLDMLV 161
Cdd:PLN03192  35 PPLGVPSYNQNHIgsdgwIISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLNASPKRGLE---IADNVVDLFFAVDIVL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  162 RARTGFLEQ--GLMVRDTKRLWKHYTKTLhFKLDILSLIPTD-LAYL-----KLGVNYPELRFNRLLKFSRLFEFFDRTE 233
Cdd:PLN03192 112 TFFVAYIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQaLAYLitgtvKLNLSYSLLGLLRFWRLRRVKQLFTRLE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  234 TRTNYpNVFRI--GNLVLYTLIIIHWNACIYFAISKFIGFGTDSW---VYPNTSKpeyARLSRKYIYSLYWSTLTLTTIG 308
Cdd:PLN03192 191 KDIRF-SYFWIrcARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWigaVIPNFRE---TSLWIRYISAIYWSITTMTTVG 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  309 ETP-PPVKDEEYLFVVIDFLVGILIFATIVGNVGSMISNMNAPRVEFQAKIDSVKQYMQFRKVTKDLETRVIRWFdYLWA 387
Cdd:PLN03192 267 YGDlHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM-CLRF 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524  388 NRKTVDEKEVLKNLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGK 467
Cdd:PLN03192 346 KAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGE 425

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33859524  468 LAVVADDGVTQFVV--LSDGSYFGEISILnikgskSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPD 534
Cdd:PLN03192 426 VEIIDSEGEKERVVgtLGCGDIFGEVGAL------CCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 423-539 2.00e-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: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524 423 IFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 499
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 33859524 500 ksGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRAL 539
Cdd:cd00038  77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 423-542 6.85e-21

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: 88.61  E-value: 6.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524    423 IFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgs 499
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQIVgTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 33859524    500 KSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRALEEK 542
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 444-532 2.53e-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: 74.18  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524   444 FSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgsksGNRRTANIRSIGYSDLFCL 520
Cdd:pfam00027   4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQILaVLGPGDFFGELALLG------GEPRSATVVALTDSELLVI 77

                          90
                  ....*....|..
gi 33859524   521 SKDDLMEALTEY 532
Cdd:pfam00027  78 PREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 424-574 2.78e-13

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: 69.25  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859524 424 FQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGREMYIIKEGKLAVV--ADDGVTQFV-VLSDGSYFGEISILnikgsk 500
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33859524 501 SGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPDAKRALEekgrQILMKDNLIDEDLVAARVdTRDVEEKVEYL 574
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELARALL----RLLARRLRQLQERLVSLA-FLSAEERLARF 143
 
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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