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Conserved domains on  [gi|17556791|ref|NP_499033|]
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Cyclic nucleotide-gated channel [Caenorhabditis elegans]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13328420)

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

Gene Ontology:  GO:0016020|GO:0030551|GO:0005216
PubMed:  12087135|17601606

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 ...
 493-610 4.20e-26

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: 103.17  E-value: 4.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 493 IFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV--DDDGKKVFV-TLQEGSVFGELSILniags 569
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYklDEDGREQIVgFLGPGDLFGELALL----- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17556791 570 kNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLL 610
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 609-675 9.44e-26

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: 100.70  E-value: 9.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   609 LLAKGREILKKDNLLDE---NAPEEQKTVEEIAEHLNNAVKVLQTRMARLIVEHSSTEGKLMKRIEMLEK 675
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEaaaNAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 208-564 2.88e-19

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  208 DLLMDCVYLIDTFLNYRMGYMDQ--GLVVREAEKVTKAYWqSKQYRIDGISLIPLD----YILGWPIPYINWRGLPILRL 281
Cdd:PLN03192  98 DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAVRYL-STWFLMDVASTIPFQalayLITGTVKLNLSYSLLGLLRF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  282 NRLIRYKRVRNCLERtETRSSMpnaF--RVVVVVWYIVIIIHWNACLYFWISE--------WIGlgtdawvyghlnkQSL 351
Cdd:PLN03192 177 WRLRRVKQLFTRLEK-DIRFSY---FwiRCARLLSVTLFLVHCAGCLYYLIADryphqgktWIG-------------AVI 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  352 PDDITDTLLRRYVYSFYWSTLILTTIGEVPSPVRN-IEYAFVTLDLMCGVLIFATIVGNVGSMISNMSAARTEFQNKMDG 430
Cdd:PLN03192 240 PNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNtIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEA 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  431 IKQYMELRKVSKQLEIRVIKWFdYLWTNKQSLSDQQVLKVLPDKLQAEIAMQVHFETLRKVRIFQDCEAGLLAELVLKLQ 510
Cdd:PLN03192 320 ASNFVGRNRLPPRLKDQILAYM-CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMK 398

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17556791  511 LQVFSPGDFICKKGDIGREMYIVKRGRLQVVDDDGKK--VFVTLQEGSVFGELSIL 564
Cdd:PLN03192 399 AEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKerVVGTLGCGDIFGEVGAL 454
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 493-610 4.20e-26

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: 103.17  E-value: 4.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 493 IFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV--DDDGKKVFV-TLQEGSVFGELSILniags 569
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYklDEDGREQIVgFLGPGDLFGELALL----- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17556791 570 kNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLL 610
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 609-675 9.44e-26

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: 100.70  E-value: 9.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   609 LLAKGREILKKDNLLDE---NAPEEQKTVEEIAEHLNNAVKVLQTRMARLIVEHSSTEGKLMKRIEMLEK 675
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEaaaNAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 493-612 1.12e-22

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: 93.62  E-value: 1.12e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791    493 IFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV---DDDGKKVFVTLQEGSVFGELSILNiags 569
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvlEDGEEQIVGTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17556791    570 KNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLLAK 612
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 208-564 2.88e-19

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  208 DLLMDCVYLIDTFLNYRMGYMDQ--GLVVREAEKVTKAYWqSKQYRIDGISLIPLD----YILGWPIPYINWRGLPILRL 281
Cdd:PLN03192  98 DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAVRYL-STWFLMDVASTIPFQalayLITGTVKLNLSYSLLGLLRF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  282 NRLIRYKRVRNCLERtETRSSMpnaF--RVVVVVWYIVIIIHWNACLYFWISE--------WIGlgtdawvyghlnkQSL 351
Cdd:PLN03192 177 WRLRRVKQLFTRLEK-DIRFSY---FwiRCARLLSVTLFLVHCAGCLYYLIADryphqgktWIG-------------AVI 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  352 PDDITDTLLRRYVYSFYWSTLILTTIGEVPSPVRN-IEYAFVTLDLMCGVLIFATIVGNVGSMISNMSAARTEFQNKMDG 430
Cdd:PLN03192 240 PNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNtIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEA 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  431 IKQYMELRKVSKQLEIRVIKWFdYLWTNKQSLSDQQVLKVLPDKLQAEIAMQVHFETLRKVRIFQDCEAGLLAELVLKLQ 510
Cdd:PLN03192 320 ASNFVGRNRLPPRLKDQILAYM-CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMK 398

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17556791  511 LQVFSPGDFICKKGDIGREMYIVKRGRLQVVDDDGKK--VFVTLQEGSVFGELSIL 564
Cdd:PLN03192 399 AEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKerVVGTLGCGDIFGEVGAL 454
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 511-602 3.22e-17

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: 76.88  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   511 LQVFSPGDFICKKGDIGREMYIVKRGRLQV--VDDDGKKVFV-TLQEGSVFGELSILniagskNGNRRTANVRSVGYTDL 587
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQILaVLGPGDFFGELALL------GGEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 17556791   588 FVLSKTDLWNALREY 602
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 494-660 3.47e-17

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: 80.80  E-value: 3.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 494 FQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV--DDDGKKVFV-TLQEGSVFGELSILniagsk 570
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 571 NGNRRTANVRSVGYTDLFVLSKTDLWNALREYPD-ARKLLLAKGREILKKDNLLDENApeeQKTVEEiaehlnnavkvlq 649
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA---FLSAEE------------- 138

                       170
                ....*....|.
gi 17556791 650 tRMARLIVEHS 660
Cdd:COG0664 139 -RLARFLLELA 148
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 176-421 3.44e-16

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: 78.46  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   176 MLTNMKEMPTYSQYPDLgwskyWHFRMLWVFFDLLMDCVYLIDTFLNYRMGYMDqglvvreaekvtKAYWQSKQYRIDGI 255
Cdd:pfam00520  12 ILLNTIFLALETYFQPE-----EPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFRSPWNILDFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   256 SLIPLDYILGWPIPYinwrGLPILRLNRLIRYKRVRNCLERTETRSSMPNA-FRVVVVVWYIVIIIHWNACLYFWISEWI 334
Cdd:pfam00520  75 VVLPSLISLVLSSVG----SLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIGYQL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   335 GLGT-DAWVYGhlnkqslpdDITDTLLRRYVYSFYWSTLILTTIG--EVPSPVRNIEYA------FVTLDLMCGVLIFAT 405
Cdd:pfam00520 151 FGGKlKTWENP---------DNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKGEfwayiyFVSFIILGGFLLLNL 221

                         250
                  ....*....|....*.
gi 17556791   406 IVGNVGSMISNMSAAR 421
Cdd:pfam00520 222 FIAVIIDNFQELTERT 237
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 493-610 4.20e-26

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: 103.17  E-value: 4.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 493 IFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV--DDDGKKVFV-TLQEGSVFGELSILniags 569
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYklDEDGREQIVgFLGPGDLFGELALL----- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17556791 570 kNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLL 610
Cdd:cd00038  76 -GNGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 609-675 9.44e-26

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: 100.70  E-value: 9.44e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   609 LLAKGREILKKDNLLDE---NAPEEQKTVEEIAEHLNNAVKVLQTRMARLIVEHSSTEGKLMKRIEMLEK 675
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEaaaNAGAEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 493-612 1.12e-22

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: 93.62  E-value: 1.12e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791    493 IFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV---DDDGKKVFVTLQEGSVFGELSILNiags 569
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvlEDGEEQIVGTLGPGDFFGELALLT---- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17556791    570 KNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLLAK 612
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 208-564 2.88e-19

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 92.62  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  208 DLLMDCVYLIDTFLNYRMGYMDQ--GLVVREAEKVTKAYWqSKQYRIDGISLIPLD----YILGWPIPYINWRGLPILRL 281
Cdd:PLN03192  98 DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAVRYL-STWFLMDVASTIPFQalayLITGTVKLNLSYSLLGLLRF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  282 NRLIRYKRVRNCLERtETRSSMpnaF--RVVVVVWYIVIIIHWNACLYFWISE--------WIGlgtdawvyghlnkQSL 351
Cdd:PLN03192 177 WRLRRVKQLFTRLEK-DIRFSY---FwiRCARLLSVTLFLVHCAGCLYYLIADryphqgktWIG-------------AVI 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  352 PDDITDTLLRRYVYSFYWSTLILTTIGEVPSPVRN-IEYAFVTLDLMCGVLIFATIVGNVGSMISNMSAARTEFQNKMDG 430
Cdd:PLN03192 240 PNFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNtIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEA 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791  431 IKQYMELRKVSKQLEIRVIKWFdYLWTNKQSLSDQQVLKVLPDKLQAEIAMQVHFETLRKVRIFQDCEAGLLAELVLKLQ 510
Cdd:PLN03192 320 ASNFVGRNRLPPRLKDQILAYM-CLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMK 398

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17556791  511 LQVFSPGDFICKKGDIGREMYIVKRGRLQVVDDDGKK--VFVTLQEGSVFGELSIL 564
Cdd:PLN03192 399 AEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKerVVGTLGCGDIFGEVGAL 454
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 511-602 3.22e-17

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: 76.88  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   511 LQVFSPGDFICKKGDIGREMYIVKRGRLQV--VDDDGKKVFV-TLQEGSVFGELSILniagskNGNRRTANVRSVGYTDL 587
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQILaVLGPGDFFGELALL------GGEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 17556791   588 FVLSKTDLWNALREY 602
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 494-660 3.47e-17

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: 80.80  E-value: 3.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 494 FQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVV--DDDGKKVFV-TLQEGSVFGELSILniagsk 570
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQILgFLGPGDFFGELSLL------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791 571 NGNRRTANVRSVGYTDLFVLSKTDLWNALREYPD-ARKLLLAKGREILKKDNLLDENApeeQKTVEEiaehlnnavkvlq 649
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA---FLSAEE------------- 138

                       170
                ....*....|.
gi 17556791 650 tRMARLIVEHS 660
Cdd:COG0664 139 -RLARFLLELA 148
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 176-421 3.44e-16

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: 78.46  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   176 MLTNMKEMPTYSQYPDLgwskyWHFRMLWVFFDLLMDCVYLIDTFLNYRMGYMDqglvvreaekvtKAYWQSKQYRIDGI 255
Cdd:pfam00520  12 ILLNTIFLALETYFQPE-----EPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFRSPWNILDFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   256 SLIPLDYILGWPIPYinwrGLPILRLNRLIRYKRVRNCLERTETRSSMPNA-FRVVVVVWYIVIIIHWNACLYFWISEWI 334
Cdd:pfam00520  75 VVLPSLISLVLSSVG----SLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIGYQL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556791   335 GLGT-DAWVYGhlnkqslpdDITDTLLRRYVYSFYWSTLILTTIG--EVPSPVRNIEYA------FVTLDLMCGVLIFAT 405
Cdd:pfam00520 151 FGGKlKTWENP---------DNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKGEfwayiyFVSFIILGGFLLLNL 221

                         250
                  ....*....|....*.
gi 17556791   406 IVGNVGSMISNMSAAR 421
Cdd:pfam00520 222 FIAVIIDNFQELTERT 237
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 530-558 9.83e-04

11S legumin seed storage globulin, C-terminal cupin domain; This family contains the C-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380370  Cd Length: 155  Bit Score: 40.15  E-value: 9.83e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 17556791 530 MYIVK-RGRLQVVDDDGKKVFVT-LQEGSVF 558
Cdd:cd02243  51 IYVTRgSGRVQVVGDNGKRVLDGeVREGQLL 81
 
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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