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Conserved domains on  [gi|1969800135|ref|XP_039152254|]
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pneumococcal serine-rich repeat protein isoform X7 [Drosophila simulans]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 11997992)

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
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 242-511 1.48e-31

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: 124.69  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  242 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 321
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  322 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 398
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  399 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAEPNFsvdgprsiprrgiksrllqfgsS 476
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKGEF----------------------W 202

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1969800135  477 YGYIFTIVSYLIGVFIFATIVGQVGNVITNRNANR 511
Cdd:pfam00520  203 AYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 586-698 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 1969800135  586 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 661
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1969800135  662 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 698
Cdd:cd00038     79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1687-1774 3.70e-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: 41.91  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135 1687 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1759
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263

                           90
                   ....*....|....*
gi 1969800135 1760 AAESGhlvsGSGSSG 1774
Cdd:cd21118    264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 242-511 1.48e-31

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: 124.69  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  242 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 321
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  322 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 398
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  399 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAEPNFsvdgprsiprrgiksrllqfgsS 476
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKGEF----------------------W 202

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1969800135  477 YGYIFTIVSYLIGVFIFATIVGQVGNVITNRNANR 511
Cdd:pfam00520  203 AYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 236-693 1.93e-29

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 127.68  E-value: 1.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  236 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 313
Cdd:PLN03192    53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  314 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 385
Cdd:PLN03192   131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  386 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTI--GDLPTPETnaepnfsvdgprsi 461
Cdd:PLN03192   210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVgyGDLHAVNT-------------- 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  462 prrgiksrllqfgssYGYIFTIVSYLIGVFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRw 541
Cdd:PLN03192   276 ---------------IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA- 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  542 ydYSWSRGRIQGGGDiNTALGLLPDKLKTELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAR 621
Cdd:PLN03192   340 --YMCLRFKAESLNQ-QQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPD 416

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969800135  622 EMFIIADGILEVLSETG---KVLTTMKAGDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 693
Cdd:PLN03192   417 DVYIVVSGEVEIIDSEGekeRVVGTLGCGDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 586-698 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 1969800135  586 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 661
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1969800135  662 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 698
Cdd:cd00038     79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 586-698 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 1969800135   586 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 661
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1969800135   662 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 698
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 607-691 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 1969800135  607 FTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILNLDglnKRTADVRSVGYSELFSLSRE 682
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGReqILAVLGPGDFFGELALLGGE---PRSATVVALTDSELLVIPRE 80


                   ....*....
gi 1969800135  683 DVLAAMKDY 691
Cdd:pfam00027   81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 587-704 1.11e-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: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  587 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 662
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1969800135  663 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 704
Cdd:COG0664     78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
612-706 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 1969800135  612 SICRKGEVAREMFIIADGILEVLSE--TGK--VLTTMKAGDFFGEIGIlnLDGLNKRTADVRSVGYSELFSLSREDVLAA 687
Cdd:PRK11753    30 TLIHAGEKAETLYYIVKGSVAVLIKdeEGKemILSYLNQGDFIGELGL--FEEGQERSAWVRAKTACEVAEISYKKFRQL 107

                           90       100
                   ....*....|....*....|..
gi 1969800135  688 MKDYPdaqEILQTLGR---KRL 706
Cdd:PRK11753   108 IQVNP---DILMALSAqmaRRL 126
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1687-1774 3.70e-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: 41.91  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135 1687 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1759
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263

                           90
                   ....*....|....*
gi 1969800135 1760 AAESGhlvsGSGSSG 1774
Cdd:cd21118    264 GSNGG----SSGNSG 274
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 242-511 1.48e-31

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: 124.69  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  242 NFYFYWLMMLtvCVLYNLWTLIVRQSFPElQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEqglmvyddrklaCHYVH 321
Cdd:pfam00520    1 SRYFELFILL--LILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFK------------KRYFR 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  322 SRDFIFDMIALIP--LDLLQLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHILLILAHWFGCFYFL 398
Cdd:pfam00520   66 SPWNILDFVVVLPslISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLiRSLKSLGNLLLLLLLFLFIFAI 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  399 LSeAEGFQGDWVYPYRPGDYATLTRKYLGSLYWSTLTLTTIG--DLPTPETNAEPNFsvdgprsiprrgiksrllqfgsS 476
Cdd:pfam00520  146 IG-YQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGwgDIMYDTIDGKGEF----------------------W 202

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1969800135  477 YGYIFTIVSYLIGVFIFATIVGQVGNVITNRNANR 511
Cdd:pfam00520  203 AYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 236-693 1.93e-29

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 127.68  E-value: 1.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  236 VVNPDENFYFYWLMMLTVCVLYNLWTLIVRQSFpeLQQSVPTFWLICDSMTDVVFILDIIVQLRTGYLEQ--GLMVYDDR 313
Cdd:PLN03192    53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRK 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  314 KLACHYVhSRDFIFDMIALIPLDLL-------QLKMGTHPLLRFTRFFKVYRSVRFYYIVESRTVWPNLW-RVVNLIHIL 385
Cdd:PLN03192   131 KIAVRYL-STWFLMDVASTIPFQALaylitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWiRCARLLSVT 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  386 LILAHWFGCFYFLLSEAEGFQGD-WVYPYRPG-DYATLTRKYLGSLYWSTLTLTTI--GDLPTPETnaepnfsvdgprsi 461
Cdd:PLN03192   210 LFLVHCAGCLYYLIADRYPHQGKtWIGAVIPNfRETSLWIRYISAIYWSITTMTTVgyGDLHAVNT-------------- 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  462 prrgiksrllqfgssYGYIFTIVSYLIGVFIFATIVGQVGNVITNRNANRLEFERLLDGAKTYMRHHKVPGGMKRRVLRw 541
Cdd:PLN03192   276 ---------------IEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA- 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  542 ydYSWSRGRIQGGGDiNTALGLLPDKLKTELALHVNLSVLKKVTIFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAR 621
Cdd:PLN03192   340 --YMCLRFKAESLNQ-QQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPD 416

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969800135  622 EMFIIADGILEVLSETG---KVLTTMKAGDFFGEIGILNldgLNKRTADVRSVGYSELFSLSREDVLAAMKDYPD 693
Cdd:PLN03192   417 DVYIVVSGEVEIIDSEGekeRVVGTLGCGDIFGEVGALC---CRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQE 488
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 586-698 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 1969800135  586 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSETG----KVLTTMKAGDFFGEIGILNLDgl 661
Cdd:cd00038      1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEdgreQIVGFLGPGDLFGELALLGNG-- 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1969800135  662 nKRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 698
Cdd:cd00038     79 -PRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 586-698 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 1969800135   586 IFQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEVLSET----GKVLTTMKAGDFFGEIGILNLDGL 661
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELALLTNSRR 80

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1969800135   662 NkRTADVRSVGYSELFSLSREDVLAAMKDYPDAQEIL 698
Cdd:smart00100   81 A-ASAAAVALELATLLRIDFRDFLQLLPELPQLLLEL 116
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 607-691 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 1969800135  607 FTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILNLDglnKRTADVRSVGYSELFSLSRE 682
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGReqILAVLGPGDFFGELALLGGE---PRSATVVALTDSELLVIPRE 80


                   ....*....
gi 1969800135  683 DVLAAMKDY 691
Cdd:pfam00027   81 DFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 587-704 1.11e-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: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135  587 FQECQPEFLHDLVLKMKAYIFTPGDSICRKGEVAREMFIIADGILEV--LSETGK--VLTTMKAGDFFGEIGILnldGLN 662
Cdd:COG0664      1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDGReqILGFLGPGDFFGELSLL---GGE 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1969800135  663 KRTADVRSVGYSELFSLSREDVLAAMKDYPD-AQEILQTLGRK 704
Cdd:COG0664     78 PSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARR 120
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
612-706 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 1969800135  612 SICRKGEVAREMFIIADGILEVLSE--TGK--VLTTMKAGDFFGEIGIlnLDGLNKRTADVRSVGYSELFSLSREDVLAA 687
Cdd:PRK11753    30 TLIHAGEKAETLYYIVKGSVAVLIKdeEGKemILSYLNQGDFIGELGL--FEEGQERSAWVRAKTACEVAEISYKKFRQL 107

                           90       100
                   ....*....|....*....|..
gi 1969800135  688 MKDYPdaqEILQTLGR---KRL 706
Cdd:PRK11753   108 IQVNP---DILMALSAqmaRRL 126
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1687-1774 3.70e-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: 41.91  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969800135 1687 TSSPPIQGGRRS-------TSPGPSRHHAASANALNCPSSYYGGPGSLSSRHAQSHPSFYSGQGNGRSSGRSSGYREWSG 1759
Cdd:cd21118    184 AVAQPGYGTVRGnnqnsgcTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSG 263

                           90
                   ....*....|....*
gi 1969800135 1760 AAESGhlvsGSGSSG 1774
Cdd:cd21118    264 GSNGG----SSGNSG 274
 
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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