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Conserved domains on  [gi|1825751504|ref|NP_001366199|]
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cyclic nucleotide-gated channel alpha-1 [Homo sapiens]

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 ...
 161-403 9.84e-38

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: 140.48  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 161 YYNWLFCITLPVMYNWTMVIARACFDElQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLeqgllvkeelklINKYKSNL 240
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 241 QFKLDVLSLIPTDL-LYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPN-IFRISNLVMYIVIIIHWNACVFYSIS 318
Cdd:pfam00520  68 WNILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 319 KAIGFGN-DTWVYPDINDPEFgrlaRKYVYSLYWSTLTLTTIG--ETPPPVRDSE------YVFVVVDFLIGVLIFATIV 389
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|....
gi 1825751504 390 GNIGSMISNMNAAR 403
Cdd:pfam00520 224 AVIIDNFQELTERT 237
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 591-660 4.03e-37

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: 132.68  E-value: 4.03e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 591 LEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEK 660
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 475-591 6.14e-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: 97.01  E-value: 6.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 475 IFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 551
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1825751504 552 kaGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTML 591
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 161-403 9.84e-38

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: 140.48  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 161 YYNWLFCITLPVMYNWTMVIARACFDElQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLeqgllvkeelklINKYKSNL 240
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 241 QFKLDVLSLIPTDL-LYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPN-IFRISNLVMYIVIIIHWNACVFYSIS 318
Cdd:pfam00520  68 WNILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 319 KAIGFGN-DTWVYPDINDPEFgrlaRKYVYSLYWSTLTLTTIG--ETPPPVRDSE------YVFVVVDFLIGVLIFATIV 389
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|....
gi 1825751504 390 GNIGSMISNMNAAR 403
Cdd:pfam00520 224 AVIIDNFQELTERT 237
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 591-660 4.03e-37

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: 132.68  E-value: 4.03e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 591 LEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEK 660
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 153-615 3.76e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.03  E-value: 3.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 153 VIDPSGNTYYNWLFCITLPVMYN-WTMVIARACFDELQSDYLEywlILDYVSDIVYLIDMFVRTRTGYLEQ--GLLVKEE 229
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLNASPKRGLE---IADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 230 LKLINKYKSNLqFKLDVLSLIPTDLL-YF-----KLGWNYPEIRLNRLLRFSRMFEFFQRTET--RTNYPNIfRISNLVM 301
Cdd:PLN03192  130 KKIAVRYLSTW-FLMDVASTIPFQALaYLitgtvKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSYFWI-RCARLLS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 302 YIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDS-EYVFVVVDFLI 380
Cdd:PLN03192  208 VTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFYMLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 381 GVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHfRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAE 460
Cdd:PLN03192  288 NLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVG-RNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKS 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 461 IAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV--LSDGS 538
Cdd:PLN03192  367 ICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVgtLGCGD 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 539 YFGEISILNIKgSKAGNRRTANIksigySDLFCLSKDDLMEALTEYP-DAKTMLEEKGK-QILMKD-GLLDLNIANAGSD 615
Cdd:PLN03192  447 IFGEVGALCCR-PQSFTFRTKTL-----SQLLRLKTSTLIEAMQTRQeDNVVILKNFLQhHKELHDlNVGDLLGDNGGEH 520
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 475-591 6.14e-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: 97.01  E-value: 6.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 475 IFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 551
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1825751504 552 kaGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTML 591
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 475-594 3.11e-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: 89.38  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504  475 IFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgs 551
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQIVgTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1825751504  552 kaGNRRTANIKSIGYSD--LFCLSKDDLMEALTEYPDAKTMLEEK 594
Cdd:smart00100  77 --NSRRAASAAAVALELatLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 493-584 2.26e-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: 74.57  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 493 PQVYSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgskaGNRRTANIKSIGYSDL 569
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQILaVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1825751504 570 FCLSKDDLMEALTEY 584
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 476-644 9.02e-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: 67.70  E-value: 9.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 476 FADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVV--ADDGVTQFV-VLSDGSYFGEISILNikgsk 552
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLLG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 553 aGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPD-AKTMLEEKGKQILMKDGLLDLNIANagsDPKD-----LEEKVTRM 626
Cdd:COG0664    76 -GEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLAFL---SAEErlarfLLELADRL 151

                         170
                  ....*....|....*...
gi 1825751504 627 EGSVDLLQTRfaRILAEY 644
Cdd:COG0664   152 DGRIDLPLTQ--EEIASY 167
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 161-403 9.84e-38

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: 140.48  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 161 YYNWLFCITLPVMYNWTMVIARACFDElQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLeqgllvkeelklINKYKSNL 240
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 241 QFKLDVLSLIPTDL-LYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPN-IFRISNLVMYIVIIIHWNACVFYSIS 318
Cdd:pfam00520  68 WNILDFVVVLPSLIsLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 319 KAIGFGN-DTWVYPDINDPEFgrlaRKYVYSLYWSTLTLTTIG--ETPPPVRDSE------YVFVVVDFLIGVLIFATIV 389
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|....
gi 1825751504 390 GNIGSMISNMNAAR 403
Cdd:pfam00520 224 AVIIDNFQELTERT 237
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 591-660 4.03e-37

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: 132.68  E-value: 4.03e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 591 LEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEK 660
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 153-615 3.76e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.03  E-value: 3.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 153 VIDPSGNTYYNWLFCITLPVMYN-WTMVIARACFDELQSDYLEywlILDYVSDIVYLIDMFVRTRTGYLEQ--GLLVKEE 229
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLNASPKRGLE---IADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 230 LKLINKYKSNLqFKLDVLSLIPTDLL-YF-----KLGWNYPEIRLNRLLRFSRMFEFFQRTET--RTNYPNIfRISNLVM 301
Cdd:PLN03192  130 KKIAVRYLSTW-FLMDVASTIPFQALaYLitgtvKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSYFWI-RCARLLS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 302 YIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDS-EYVFVVVDFLI 380
Cdd:PLN03192  208 VTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIPNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFYMLF 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 381 GVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHfRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAE 460
Cdd:PLN03192  288 NLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVG-RNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKS 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 461 IAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV--LSDGS 538
Cdd:PLN03192  367 ICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVgtLGCGD 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 539 YFGEISILNIKgSKAGNRRTANIksigySDLFCLSKDDLMEALTEYP-DAKTMLEEKGK-QILMKD-GLLDLNIANAGSD 615
Cdd:PLN03192  447 IFGEVGALCCR-PQSFTFRTKTL-----SQLLRLKTSTLIEAMQTRQeDNVVILKNFLQhHKELHDlNVGDLLGDNGGEH 520
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 475-591 6.14e-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: 97.01  E-value: 6.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 475 IFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVV---LSDGSYFGEISILNikgs 551
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIvgfLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1825751504 552 kaGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTML 591
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 475-594 3.11e-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: 89.38  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504  475 IFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgs 551
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQIVgTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1825751504  552 kaGNRRTANIKSIGYSD--LFCLSKDDLMEALTEYPDAKTMLEEK 594
Cdd:smart00100  77 --NSRRAASAAAVALELatLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 493-584 2.26e-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: 74.57  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 493 PQVYSPGDYICKKGDIGREMYIIKEGKLAVVAD--DGVTQFV-VLSDGSYFGEISILNikgskaGNRRTANIKSIGYSDL 569
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQILaVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1825751504 570 FCLSKDDLMEALTEY 584
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 476-644 9.02e-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: 67.70  E-value: 9.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 476 FADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVV--ADDGVTQFV-VLSDGSYFGEISILNikgsk 552
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLLG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825751504 553 aGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPD-AKTMLEEKGKQILMKDGLLDLNIANagsDPKD-----LEEKVTRM 626
Cdd:COG0664    76 -GEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLAFL---SAEErlarfLLELADRL 151

                         170
                  ....*....|....*...
gi 1825751504 627 EGSVDLLQTRfaRILAEY 644
Cdd:COG0664   152 DGRIDLPLTQ--EEIASY 167
 
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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