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Conserved domains on  [gi|221330259|ref|NP_001137668|]
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I[[h]] channel, isoform G [Drosophila melanogaster]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13750456)

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

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
741-1209 1.78e-26

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 117.66  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  741 SGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMqqDNAEQVIL 820
Cdd:PLN03192   49 SDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYI--DPRTQLLV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  821 -DPKLIAKHYLRTWFFLDLISSIPLDYI--FLIFNQDFSDSFQILHAgraLRILRLAKllslvrllrlsrlvryVSQWee 897
Cdd:PLN03192  127 rDRKKIAVRYLSTWFLMDVASTIPFQALayLITGTVKLNLSYSLLGL---LRFWRLRR----------------VKQL-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  898 vyilqnlqkksadrrgrMNRKDKDgltksnliLKFlnmaSVF-MRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVS 976
Cdd:PLN03192  186 -----------------FTRLEKD--------IRF----SYFwIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  977 I---NELQESYWLeQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIqsLDSSRR--QY 1051
Cdd:PLN03192  237 AvipNFRETSLWI-RYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1052 REKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDV 1131
Cdd:PLN03192  314 RNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLL 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1132 VTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGE---VATSLSDGSYFGEICLLTNARRVASVRAETYCNLFS 1208
Cdd:PLN03192  394 VTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEkerVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLR 473

                  .
gi 221330259 1209 L 1209
Cdd:PLN03192  474 L 474
Ion_trans_N pfam08412
Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 ...
709-751 3.66e-22

Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 in voltage- and cyclic nucleotide-gated K/Na ion channels.


:

Pssm-ID: 400630  Cd Length: 43  Bit Score: 90.44  E-value: 3.66e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 221330259   709 LQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSS 751
Cdd:pfam08412    1 LKSLLQPSDNKLSMKLFGSKKAVEKEKERQKEAGVWIIHPCSN 43
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
741-1209 1.78e-26

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 117.66  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  741 SGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMqqDNAEQVIL 820
Cdd:PLN03192   49 SDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYI--DPRTQLLV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  821 -DPKLIAKHYLRTWFFLDLISSIPLDYI--FLIFNQDFSDSFQILHAgraLRILRLAKllslvrllrlsrlvryVSQWee 897
Cdd:PLN03192  127 rDRKKIAVRYLSTWFLMDVASTIPFQALayLITGTVKLNLSYSLLGL---LRFWRLRR----------------VKQL-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  898 vyilqnlqkksadrrgrMNRKDKDgltksnliLKFlnmaSVF-MRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVS 976
Cdd:PLN03192  186 -----------------FTRLEKD--------IRF----SYFwIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  977 I---NELQESYWLeQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIqsLDSSRR--QY 1051
Cdd:PLN03192  237 AvipNFRETSLWI-RYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1052 REKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDV 1131
Cdd:PLN03192  314 RNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLL 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1132 VTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGE---VATSLSDGSYFGEICLLTNARRVASVRAETYCNLFS 1208
Cdd:PLN03192  394 VTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEkerVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLR 473

                  .
gi 221330259 1209 L 1209
Cdd:PLN03192  474 L 474
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
1119-1228 4.23e-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: 103.94  E-value: 4.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1119 FFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGE----VATSLSDGSYFGEICLLTNARR 1194
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 221330259 1195 VASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTM 1228
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
Ion_trans_N pfam08412
Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 ...
709-751 3.66e-22

Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 in voltage- and cyclic nucleotide-gated K/Na ion channels.


Pssm-ID: 400630  Cd Length: 43  Bit Score: 90.44  E-value: 3.66e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 221330259   709 LQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSS 751
Cdd:pfam08412    1 LKSLLQPSDNKLSMKLFGSKKAVEKEKERQKEAGVWIIHPCSN 43
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
1119-1235 2.18e-20

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: 87.84  E-value: 2.18e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   1119 FFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIV--MANGE--VATSLSDGSYFGEICLLTNARR 1194
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvLEDGEeqIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 221330259   1195 VASVRAETYCnLFSLSVDHFNCVLDQYPLMRKTMETVAAER 1235
Cdd:smart00100   81 AASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
753-1049 1.44e-19

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: 89.25  E-value: 1.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   753 RFYWDLCMLLLLVANLIILPVAISF-FNDDLSTRWIAFNCLSDTIFLIDIVVNFRTgimqqdnaeqviLDPKliaKHYLR 831
Cdd:pfam00520    1 SRYFELFILLLILLNTIFLALETYFqPEEPLTTVLEILDYVFTGIFTLEMLLKIIA------------AGFK---KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   832 T-WFFLDLISSIPLDYIFLIFNQDFSDSFQILhagRALRILRLAKllslvrllrlsrlvrYVSQWEevyilqnlqkksad 910
Cdd:pfam00520   66 SpWNILDFVVVLPSLISLVLSSVGSLSGLRVL---RLLRLLRLLR---------------LIRRLE-------------- 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   911 rrgrmnrkdkdgltksnlilKFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMlQGFPSNSWVSINELQESYWLEQYS 990
Cdd:pfam00520  114 --------------------GLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGY-QLFGGKLKTWENPDNGRTNFDNFP 172
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330259   991 WALFKAMSHMLCIGYGRFPPQSLTDMW-------LTMLSMISGATCYALFLGHATNLIQSLDSSRR 1049
Cdd:pfam00520  173 NAFLWLFQTMTTEGWGDIMYDTIDGKGefwayiyFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
1120-1236 7.19e-14

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: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1120 FANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIV--MANGEVAT--SLSDGSYFGEICLLTNARRV 1195
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQIlgFLGPGDFFGELSLLGGEPSP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221330259 1196 ASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERL 1236
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
741-1209 1.78e-26

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 117.66  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  741 SGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMqqDNAEQVIL 820
Cdd:PLN03192   49 SDGWIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYI--DPRTQLLV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  821 -DPKLIAKHYLRTWFFLDLISSIPLDYI--FLIFNQDFSDSFQILHAgraLRILRLAKllslvrllrlsrlvryVSQWee 897
Cdd:PLN03192  127 rDRKKIAVRYLSTWFLMDVASTIPFQALayLITGTVKLNLSYSLLGL---LRFWRLRR----------------VKQL-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  898 vyilqnlqkksadrrgrMNRKDKDgltksnliLKFlnmaSVF-MRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVS 976
Cdd:PLN03192  186 -----------------FTRLEKD--------IRF----SYFwIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  977 I---NELQESYWLeQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIqsLDSSRR--QY 1051
Cdd:PLN03192  237 AvipNFRETSLWI-RYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLV--VEGTRRtmEF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1052 REKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDV 1131
Cdd:PLN03192  314 RNSIEAASNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLL 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1132 VTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGE---VATSLSDGSYFGEICLLTNARRVASVRAETYCNLFS 1208
Cdd:PLN03192  394 VTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEkerVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLR 473

                  .
gi 221330259 1209 L 1209
Cdd:PLN03192  474 L 474
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
1119-1228 4.23e-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: 103.94  E-value: 4.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1119 FFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGE----VATSLSDGSYFGEICLLTNARR 1194
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDgreqIVGFLGPGDLFGELALLGNGPR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 221330259 1195 VASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTM 1228
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
Ion_trans_N pfam08412
Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 ...
709-751 3.66e-22

Ion transport protein N-terminal; This metazoan domain is found to the N-terminus of pfam00520 in voltage- and cyclic nucleotide-gated K/Na ion channels.


Pssm-ID: 400630  Cd Length: 43  Bit Score: 90.44  E-value: 3.66e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 221330259   709 LQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSS 751
Cdd:pfam08412    1 LKSLLQPSDNKLSMKLFGSKKAVEKEKERQKEAGVWIIHPCSN 43
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
1119-1235 2.18e-20

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: 87.84  E-value: 2.18e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   1119 FFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIV--MANGE--VATSLSDGSYFGEICLLTNARR 1194
Cdd:smart00100    1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkvLEDGEeqIVGTLGPGDFFGELALLTNSRR 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 221330259   1195 VASVRAETYCnLFSLSVDHFNCVLDQYPLMRKTMETVAAER 1235
Cdd:smart00100   81 AASAAAVALE-LATLLRIDFRDFLQLLPELPQLLLELLLEL 120
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
753-1049 1.44e-19

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: 89.25  E-value: 1.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   753 RFYWDLCMLLLLVANLIILPVAISF-FNDDLSTRWIAFNCLSDTIFLIDIVVNFRTgimqqdnaeqviLDPKliaKHYLR 831
Cdd:pfam00520    1 SRYFELFILLLILLNTIFLALETYFqPEEPLTTVLEILDYVFTGIFTLEMLLKIIA------------AGFK---KRYFR 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   832 T-WFFLDLISSIPLDYIFLIFNQDFSDSFQILhagRALRILRLAKllslvrllrlsrlvrYVSQWEevyilqnlqkksad 910
Cdd:pfam00520   66 SpWNILDFVVVLPSLISLVLSSVGSLSGLRVL---RLLRLLRLLR---------------LIRRLE-------------- 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259   911 rrgrmnrkdkdgltksnlilKFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMlQGFPSNSWVSINELQESYWLEQYS 990
Cdd:pfam00520  114 --------------------GLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGY-QLFGGKLKTWENPDNGRTNFDNFP 172
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330259   991 WALFKAMSHMLCIGYGRFPPQSLTDMW-------LTMLSMISGATCYALFLGHATNLIQSLDSSRR 1049
Cdd:pfam00520  173 NAFLWLFQTMTTEGWGDIMYDTIDGKGefwayiyFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
1138-1221 6.36e-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: 6.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259  1138 EVFQPGDIIIKEGTIGTKMYFIQEGVVDI--VMANGE--VATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDH 1213
Cdd:pfam00027    2 RSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGReqILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81

                   ....*...
gi 221330259  1214 FNCVLDQY 1221
Cdd:pfam00027   82 FLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
1120-1236 7.19e-14

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: 7.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1120 FANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIV--MANGEVAT--SLSDGSYFGEICLLTNARRV 1195
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQIlgFLGPGDFFGELSLLGGEPSP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 221330259 1196 ASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERL 1236
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRL 121
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
1146-1236 2.50e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 43.82  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330259 1146 IIKEGTIGTKMYFIQEGVVDIVMANGE----VATSLSDGSYFGEICLL-TNARRVASVRAETYCNLFSLSVDHFNCVLDQ 1220
Cdd:PRK11753   31 LIHAGEKAETLYYIVKGSVAVLIKDEEgkemILSYLNQGDFIGELGLFeEGQERSAWVRAKTACEVAEISYKKFRQLIQV 110
                          90
                  ....*....|....*...
gi 221330259 1221 YP--LMRKTMETvaAERL 1236
Cdd:PRK11753  111 NPdiLMALSAQM--ARRL 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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