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Conserved domains on  [gi|116642889|ref|NP_061971|]
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cyclic nucleotide-gated cation channel beta-3 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
524-639 3.79e-23

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  Cd Length: 115  Bit Score: 96.24  E-value: 3.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 524 LFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDGTKVLV-TLKAGSVFGEISLLaagGG 601
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVgFLGPGDLFGELALL---GN 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 116642889 602 NRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILM 639
Cdd:cd00038   78 GPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
Ion_trans pfam00520
Ion transport protein; This family contains Sodium, Potassium, Calcium ion channels. This ...
255-441 1.95e-17

Ion transport protein; This family contains Sodium, Potassium, 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. A bacterial structure of the protein is known for the last two helices but is not the Pfam family due to it lacking the first four helices


:

Pssm-ID: 249927 [Multi-domain]  Cd Length: 195  Bit Score: 81.56  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  255 IADIICDIIYLYDMLfiqprLQFVRGGdiivdsneLRKHYRTSTKFQLDVASIIPFDICYLFFGFNP----------MFR 324
Cdd:pfam00520   1 ILDYVFTVIFTLEML-----LKFIALG--------FKLSYFRSPWNILDFLVVLPSLVSLILRLLGEgsegllsvlrLLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  325 ANRMLKYTSFFE-FNHHLESIMdkayiyRVIRTTGYLLFILHINACVYYWASN--YEGIGTTRWVYDGEGNE-------Y 394
Cdd:pfam00520  68 LLRLLRLLRRFPgLRTLLQSLG------RSLKSLLNVLLLLLLLLFIFAIIGVqlFGGEFDKCEDENENPINgnsnfdsY 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116642889  395 LRCYYWAVRTLITIG-GLPEPQTLFE------IVFQLLNFFSGVFVFSSLIGQM 441
Cdd:pfam00520 142 PEALLWLFRTLTTEGwGDIMPDTLDAgtvlgkIFFVIFIILGGFLLLNLLIGVI 195
Crp COG0664
cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent ...
521-648 1.68e-09

cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms]


:

Pssm-ID: 223736 [Multi-domain]  Cd Length: 214  Bit Score: 57.15  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 521 KVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDG-TKVLVTLKAGSVFGEISLLaa 598
Cdd:COG0664    4 ENPLLNLLPSELLELLALKLEVRKLPKGEVLFTEGEEADSLYIILSGIVKLYaNTEDGrEIILGFLGPGDFFGELALL-- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116642889 599 gGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQ 648
Cdd:COG0664   82 -GGDPRSASAVALTDVEVLEIPRKDFLELLAESPKLALALLRLLARRLRQ 130
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
524-639 3.79e-23

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  Cd Length: 115  Bit Score: 96.24  E-value: 3.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 524 LFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDGTKVLV-TLKAGSVFGEISLLaagGG 601
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVgFLGPGDLFGELALL---GN 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 116642889 602 NRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILM 639
Cdd:cd00038   78 GPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
524-641 4.71e-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  Cd Length: 120  Bit Score: 87.46  E-value: 4.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889   524 LFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQV--LGGPDGTKVLVTLKAGSVFGEISLLaAGGG 601
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQIVGTLGPGDFFGELALL-TNSR 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 116642889   602 NRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKK 641
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain;
545-633 6.11e-15

Cyclic nucleotide-binding domain;


Pssm-ID: 249521  Cd Length: 91  Bit Score: 71.95  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  545 YLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDGTKVLV-TLKAGSVFGEISLLaagGGNRRTANVVAHGFANLLTLDKK 622
Cdd:pfam00027   4 FKKGEVIFREGDPADSLYIVLSGKVKVYkLDEDGREQILaFLGPGDFFGELALL---GGEPRSATVVALTDSELLVIPRE 80
                          90
                  ....*....|.
gi 116642889  623 TLQEILVHYPD 633
Cdd:pfam00027  81 DFLELLEQDPE 91
Ion_trans pfam00520
Ion transport protein; This family contains Sodium, Potassium, Calcium ion channels. This ...
255-441 1.95e-17

Ion transport protein; This family contains Sodium, Potassium, 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. A bacterial structure of the protein is known for the last two helices but is not the Pfam family due to it lacking the first four helices


Pssm-ID: 249927 [Multi-domain]  Cd Length: 195  Bit Score: 81.56  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  255 IADIICDIIYLYDMLfiqprLQFVRGGdiivdsneLRKHYRTSTKFQLDVASIIPFDICYLFFGFNP----------MFR 324
Cdd:pfam00520   1 ILDYVFTVIFTLEML-----LKFIALG--------FKLSYFRSPWNILDFLVVLPSLVSLILRLLGEgsegllsvlrLLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  325 ANRMLKYTSFFE-FNHHLESIMdkayiyRVIRTTGYLLFILHINACVYYWASN--YEGIGTTRWVYDGEGNE-------Y 394
Cdd:pfam00520  68 LLRLLRLLRRFPgLRTLLQSLG------RSLKSLLNVLLLLLLLLFIFAIIGVqlFGGEFDKCEDENENPINgnsnfdsY 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116642889  395 LRCYYWAVRTLITIG-GLPEPQTLFE------IVFQLLNFFSGVFVFSSLIGQM 441
Cdd:pfam00520 142 PEALLWLFRTLTTEGwGDIMPDTLDAgtvlgkIFFVIFIILGGFLLLNLLIGVI 195
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
255-640 7.30e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 99.94  E-value: 7.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 255 IADIICDIIYLYDML------FIQPRLQFvrggdIIVDSNELRKHYrTSTKFQLDVASIIPFD-ICYLFFGFNPMFRANR 327
Cdd:PLN03192  96 IADNVVDLFFAVDIVltffvaYIDPRTQL-----LVRDRKKIAVRY-LSTWFLMDVASTIPFQaLAYLITGTVKLNLSYS 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 328 MLKYTSFF------EFNHHLESIMDKAYIY-RVIRTTGYLLFILHINACVYYW-ASNYEGIGTTrWVYDGEGN------- 392
Cdd:PLN03192 170 LLGLLRFWrlrrvkQLFTRLEKDIRFSYFWiRCARLLSVTLFLVHCAGCLYYLiADRYPHQGKT-WIGAVIPNfretslw 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 393 -EYLRCYYWAVRTLITIG-GLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYS 470
Cdd:PLN03192 249 iRYISAIYWSITTMTTVGyGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNR 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 471 IPKLVQKRVRTWYEYTWDSQRmLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDF 550
Cdd:PLN03192 329 LPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 551 VCKKGEIGKEMYIIKHGEVQVLGGpDGTK--VLVTLKAGSVFGEISLLA--AGGGNRRTANVvahgfANLLTLDKKTLQE 626
Cdd:PLN03192 408 VIMQNEAPDDVYIVVSGEVEIIDS-EGEKerVVGTLGCGDIFGEVGALCcrPQSFTFRTKTL-----SQLLRLKTSTLIE 481
                        410
                 ....*....|....
gi 116642889 627 ILVHYPDSERILMK 640
Cdd:PLN03192 482 AMQTRQEDNVVILK 495
Crp COG0664
cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent ...
521-648 1.68e-09

cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms]


Pssm-ID: 223736 [Multi-domain]  Cd Length: 214  Bit Score: 57.15  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 521 KVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDG-TKVLVTLKAGSVFGEISLLaa 598
Cdd:COG0664    4 ENPLLNLLPSELLELLALKLEVRKLPKGEVLFTEGEEADSLYIILSGIVKLYaNTEDGrEIILGFLGPGDFFGELALL-- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116642889 599 gGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQ 648
Cdd:COG0664   82 -GGDPRSASAVALTDVEVLEIPRKDFLELLAESPKLALALLRLLARRLRQ 130
PLN02868 PLN02868
acyl-CoA thioesterase family protein
545-610 1.97e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 43.17  E-value: 1.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116642889 545 YLPGDFVCKKGEIGKEMYIIKHGEVQVLG-GPDGTKVLVTLKAGSVFGEISLlaaggGNRRTANVVA 610
Cdd:PLN02868  36 YGKGEYVVREGEPGDGLYFIWKGEAEVSGpAEEESRPEFLLKRYDYFGYGLS-----GSVHSADVVA 97
 
Name Accession Description Interval E-value
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
524-639 3.79e-23

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  Cd Length: 115  Bit Score: 96.24  E-value: 3.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 524 LFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDGTKVLV-TLKAGSVFGEISLLaagGG 601
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVgFLGPGDLFGELALL---GN 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 116642889 602 NRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILM 639
Cdd:cd00038   78 GPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
524-641 4.71e-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  Cd Length: 120  Bit Score: 87.46  E-value: 4.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889   524 LFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQV--LGGPDGTKVLVTLKAGSVFGEISLLaAGGG 601
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVykVLEDGEEQIVGTLGPGDFFGELALL-TNSR 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 116642889   602 NRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKK 641
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain;
545-633 6.11e-15

Cyclic nucleotide-binding domain;


Pssm-ID: 249521  Cd Length: 91  Bit Score: 71.95  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  545 YLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDGTKVLV-TLKAGSVFGEISLLaagGGNRRTANVVAHGFANLLTLDKK 622
Cdd:pfam00027   4 FKKGEVIFREGDPADSLYIVLSGKVKVYkLDEDGREQILaFLGPGDFFGELALL---GGEPRSATVVALTDSELLVIPRE 80
                          90
                  ....*....|.
gi 116642889  623 TLQEILVHYPD 633
Cdd:pfam00027  81 DFLELLEQDPE 91
Ion_trans pfam00520
Ion transport protein; This family contains Sodium, Potassium, Calcium ion channels. This ...
255-441 1.95e-17

Ion transport protein; This family contains Sodium, Potassium, 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. A bacterial structure of the protein is known for the last two helices but is not the Pfam family due to it lacking the first four helices


Pssm-ID: 249927 [Multi-domain]  Cd Length: 195  Bit Score: 81.56  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  255 IADIICDIIYLYDMLfiqprLQFVRGGdiivdsneLRKHYRTSTKFQLDVASIIPFDICYLFFGFNP----------MFR 324
Cdd:pfam00520   1 ILDYVFTVIFTLEML-----LKFIALG--------FKLSYFRSPWNILDFLVVLPSLVSLILRLLGEgsegllsvlrLLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889  325 ANRMLKYTSFFE-FNHHLESIMdkayiyRVIRTTGYLLFILHINACVYYWASN--YEGIGTTRWVYDGEGNE-------Y 394
Cdd:pfam00520  68 LLRLLRLLRRFPgLRTLLQSLG------RSLKSLLNVLLLLLLLLFIFAIIGVqlFGGEFDKCEDENENPINgnsnfdsY 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116642889  395 LRCYYWAVRTLITIG-GLPEPQTLFE------IVFQLLNFFSGVFVFSSLIGQM 441
Cdd:pfam00520 142 PEALLWLFRTLTTEGwGDIMPDTLDAgtvlgkIFFVIFIILGGFLLLNLLIGVI 195
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
255-640 7.30e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 99.94  E-value: 7.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 255 IADIICDIIYLYDML------FIQPRLQFvrggdIIVDSNELRKHYrTSTKFQLDVASIIPFD-ICYLFFGFNPMFRANR 327
Cdd:PLN03192  96 IADNVVDLFFAVDIVltffvaYIDPRTQL-----LVRDRKKIAVRY-LSTWFLMDVASTIPFQaLAYLITGTVKLNLSYS 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 328 MLKYTSFF------EFNHHLESIMDKAYIY-RVIRTTGYLLFILHINACVYYW-ASNYEGIGTTrWVYDGEGN------- 392
Cdd:PLN03192 170 LLGLLRFWrlrrvkQLFTRLEKDIRFSYFWiRCARLLSVTLFLVHCAGCLYYLiADRYPHQGKT-WIGAVIPNfretslw 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 393 -EYLRCYYWAVRTLITIG-GLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYS 470
Cdd:PLN03192 249 iRYISAIYWSITTMTTVGyGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNR 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 471 IPKLVQKRVRTWYEYTWDSQRmLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDF 550
Cdd:PLN03192 329 LPPRLKDQILAYMCLRFKAES-LNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 551 VCKKGEIGKEMYIIKHGEVQVLGGpDGTK--VLVTLKAGSVFGEISLLA--AGGGNRRTANVvahgfANLLTLDKKTLQE 626
Cdd:PLN03192 408 VIMQNEAPDDVYIVVSGEVEIIDS-EGEKerVVGTLGCGDIFGEVGALCcrPQSFTFRTKTL-----SQLLRLKTSTLIE 481
                        410
                 ....*....|....
gi 116642889 627 ILVHYPDSERILMK 640
Cdd:PLN03192 482 AMQTRQEDNVVILK 495
Crp COG0664
cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent ...
521-648 1.68e-09

cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms]


Pssm-ID: 223736 [Multi-domain]  Cd Length: 214  Bit Score: 57.15  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642889 521 KVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVL-GGPDG-TKVLVTLKAGSVFGEISLLaa 598
Cdd:COG0664    4 ENPLLNLLPSELLELLALKLEVRKLPKGEVLFTEGEEADSLYIILSGIVKLYaNTEDGrEIILGFLGPGDFFGELALL-- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116642889 599 gGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQ 648
Cdd:COG0664   82 -GGDPRSASAVALTDVEVLEIPRKDFLELLAESPKLALALLRLLARRLRQ 130
PLN02868 PLN02868
acyl-CoA thioesterase family protein
545-610 1.97e-04

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 43.17  E-value: 1.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116642889 545 YLPGDFVCKKGEIGKEMYIIKHGEVQVLG-GPDGTKVLVTLKAGSVFGEISLlaaggGNRRTANVVA 610
Cdd:PLN02868  36 YGKGEYVVREGEPGDGLYFIWKGEAEVSGpAEEESRPEFLLKRYDYFGYGLS-----GSVHSADVVA 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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