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Conserved domains on  [gi|1969800137|ref|XP_039152255|]
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pneumococcal serine-rich repeat protein isoform X8 [Drosophila simulans]

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

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List of domain hits

Name Accession Description Interval E-value
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
221-650 6.16e-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: 6.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  221 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 298
Cdd:PLN03192    53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  299 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 370
Cdd:PLN03192   131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  371 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 446
Cdd:PLN03192   210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  447 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 526
Cdd:PLN03192   289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  527 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 603
Cdd:PLN03192   365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1969800137  604 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 650
Cdd:PLN03192   445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1672-1759 2.87e-03

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: 42.29  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137 1672 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1744
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                           90
                   ....*....|....*
gi 1969800137 1745 AAESGhlvsGSGSSG 1759
Cdd:cd21118    264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
221-650 6.16e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 6.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  221 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 298
Cdd:PLN03192    53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  299 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 370
Cdd:PLN03192   131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  371 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 446
Cdd:PLN03192   210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  447 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 526
Cdd:PLN03192   289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  527 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 603
Cdd:PLN03192   365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1969800137  604 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 650
Cdd:PLN03192   445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
227-468 4.41e-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: 4.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  227 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 306
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  307 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 383
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  384 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAE------YIFTIVSYLIGVFIFATIVG 455
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIA 224
                          250
                   ....*....|...
gi 1969800137  456 QVGNVITNRNANR 468
Cdd:pfam00520  225 VIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
543-655 1.10e-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: 1.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  543 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 618
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1969800137  619 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 655
Cdd:cd00038     79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
543-655 3.58e-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: 3.58e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137   543 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 618
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1969800137   619 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 655
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
544-661 1.06e-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: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  544 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 619
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1969800137  620 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 661
Cdd:COG0664     78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1672-1759 2.87e-03

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: 42.29  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137 1672 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1744
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                           90
                   ....*....|....*
gi 1969800137 1745 AAESGhlvsGSGSSG 1759
Cdd:cd21118    264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
221-650 6.16e-34

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 142.31  E-value: 6.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  221 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 298
Cdd:PLN03192    53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  299 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 370
Cdd:PLN03192   131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  371 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTIG--DLPTPETnAEYIFTIVSYLIG 446
Cdd:PLN03192   210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVGygDLHAVNT-IEMIFIIFYMLFN 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  447 VFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRwydYSWSRGRIQGGGDiNTALGLLPDKLK 526
Cdd:PLN03192   289 LGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA---YMCLRFKAESLNQ-QQLIDQLPKSIC 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  527 TELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG---KVLTTMKA 603
Cdd:PLN03192   365 KSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGekeRVVGTLGC 444
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1969800137  604 GDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 650
Cdd:PLN03192   445 GDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
227-468 4.41e-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: 4.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  227 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 306
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  307 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 383
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  384 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAE------YIFTIVSYLIGVFIFATIVG 455
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIA 224
                          250
                   ....*....|...
gi 1969800137  456 QVGNVITNRNANR 468
Cdd:pfam00520  225 VIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
543-655 1.10e-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: 1.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  543 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 618
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1969800137  619 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 655
Cdd:cd00038     79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
543-655 3.58e-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: 3.58e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137   543 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 618
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1969800137   619 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 655
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
564-648 2.15e-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: 2.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  564 FTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILNLDglnKRTADVRSVGYSELFSLSRE 639
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGReqILAVLGPGDFFGELALLGGE---PRSATVVALTDSELLVIPRE 80

                   ....*....
gi 1969800137  640 DVLAAMKDY 648
Cdd:pfam00027   81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
544-661 1.06e-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: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  544 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 619
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1969800137  620 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 661
Cdd:COG0664     78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
410-463 5.29e-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: 5.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1969800137  410 YLGSLYWSTLTLTTIG--DLpTPETNAEYIFTIVSYLIGVFIFATIVGQVGNVITN 463
Cdd:pfam07885   24 FLDALYFSFVTLTTVGygDI-VPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1672-1759 2.87e-03

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: 42.29  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137 1672 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1744
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263
                           90
                   ....*....|....*
gi 1969800137 1745 AAESGhlvsGSGSSG 1759
Cdd:cd21118    264 GSNGG----SSGNSG 274
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
569-663 2.97e-03

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 41.12  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800137  569 SICRKGEVAREMFIIADGILEVLSE--TGK--VLTTMKAGDFFGEIGIlnLDGLNKRTADVRSVGYSELFSLSREDVLAA 644
Cdd:PRK11753    30 TLIHAGEKAETLYYIVKGSVAVLIKdeEGKemILSYLNQGDFIGELGL--FEEGQERSAWVRAKTACEVAEISYKKFRQL 107
                           90       100
                   ....*....|....*....|..
gi 1969800137  645 MKDYPdaqEILQTLGR---KRL 663
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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