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Conserved domains on  [gi|386764484|ref|NP_001245691|]
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cyclic nucleotide-gated ion channel-like, isoform E [Drosophila melanogaster]

Protein Classification

ion transporter( domain architecture ID 1000861)

ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
234-663 6.24e-34

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  234 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 311
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  312 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 383
Cdd:PLN03192  131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  384 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 459
Cdd:PLN03192  210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  460 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 539
Cdd:PLN03192  289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  540 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 616
Cdd:PLN03192  365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386764484  617 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 663
Cdd:PLN03192  445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1688-1775 7.05e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21118:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 495  Bit Score: 44.61  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484 1688 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRNSGRSSGYREWSG 1760
Cdd:cd21118   184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                          90
                  ....*....|....*
gi 386764484 1761 AAESGhlvsGSGSSG 1775
Cdd:cd21118   264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
234-663 6.24e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  234 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 311
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  312 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 383
Cdd:PLN03192  131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  384 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 459
Cdd:PLN03192  210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  460 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 539
Cdd:PLN03192  289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  540 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 616
Cdd:PLN03192  365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386764484  617 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 663
Cdd:PLN03192  445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
240-481 4.45e-33

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: 128.92  E-value: 4.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   240 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 319
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   320 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 396
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   397 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAE------YIFTIVSYLIGVFIFATIVG 468
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIA 224
                          250
                   ....*....|...
gi 386764484   469 QVGNVITNRNANR 481
Cdd:pfam00520  225 VIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
556-668 1.11e-22

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: 94.70  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  556 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 631
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386764484  632 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 668
Cdd:cd00038    79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
556-668 3.61e-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: 90.92  E-value: 3.61e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484    556 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 631
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 386764484    632 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 668
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
557-674 1.07e-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: 71.94  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  557 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 632
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386764484  633 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 674
Cdd:COG0664    78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1688-1775 7.05e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 44.61  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484 1688 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRNSGRSSGYREWSG 1760
Cdd:cd21118   184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                          90
                  ....*....|....*
gi 386764484 1761 AAESGhlvsGSGSSG 1775
Cdd:cd21118   264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
234-663 6.24e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 6.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  234 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 311
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  312 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 383
Cdd:PLN03192  131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  384 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 459
Cdd:PLN03192  210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  460 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 539
Cdd:PLN03192  289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  540 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 616
Cdd:PLN03192  365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386764484  617 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 663
Cdd:PLN03192  445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
240-481 4.45e-33

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: 128.92  E-value: 4.45e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   240 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 319
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   320 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 396
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   397 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAE------YIFTIVSYLIGVFIFATIVG 468
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIA 224
                          250
                   ....*....|...
gi 386764484   469 QVGNVITNRNANR 481
Cdd:pfam00520  225 VIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
556-668 1.11e-22

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: 94.70  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  556 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 631
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386764484  632 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 668
Cdd:cd00038    79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
556-668 3.61e-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: 90.92  E-value: 3.61e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484    556 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 631
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 386764484    632 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 668
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
577-661 2.17e-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: 76.11  E-value: 2.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484   577 FTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILNLDglnKRTADVRSVGYSELFSLSRE 652
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGReqILAVLGPGDFFGELALLGGE---PRSATVVALTDSELLVIPRE 80

                   ....*....
gi 386764484   653 DVLAAMKDY 661
Cdd:pfam00027   81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
557-674 1.07e-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: 71.94  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  557 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 632
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386764484  633 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 674
Cdd:COG0664    78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
423-476 5.33e-08

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: 51.88  E-value: 5.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386764484   423 YLGSLYWSTLTLTTIG--DLpTPETNAEYIFTIVSYLIGVFIFATIVGQVGNVITN 476
Cdd:pfam07885   24 FLDALYFSFVTLTTVGygDI-VPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1688-1775 7.05e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 44.61  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484 1688 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRNSGRSSGYREWSG 1760
Cdd:cd21118   184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                          90
                  ....*....|....*
gi 386764484 1761 AAESGhlvsGSGSSG 1775
Cdd:cd21118   264 GSNGG----SSGNSG 274
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
582-676 2.99e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 41.12  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764484  582 SICRKGEVAREMFIIADGILEVLSE--TGK--VLTTMKAGDFFGEIGIlnLDGLNKRTADVRSVGYSELFSLSREDVLAA 657
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKdeEGKemILSYLNQGDFIGELGL--FEEGQERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100
                  ....*....|....*....|..
gi 386764484  658 MKDYPdaqEILQTLGR---KRL 676
Cdd:PRK11753  108 IQVNP---DILMALSAqmaRRL 126
 
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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