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Conserved domains on  [gi|158186631|ref|NP_445948|]
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cyclic nucleotide-gated channel alpha-4 [Rattus norvegicus]

Protein Classification

cyclic nucleotide-gated cation channel family protein( domain architecture ID 11998063)

cyclic nucleotide-gated cation channel family protein is a nonselective cation channel opened by binding of intracellular cyclic GMP or cyclic AMP, similar to human cGMP-gated cation channel alpha-1, a subunit of the rod cyclic GMP-gated cation channel which is involved in the final stage of the phototransduction pathway

Graphical summary

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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 ...
34-273 6.83e-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: 120.45  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631   34 YYWWLNTMVFPIMYNLIIVVCRACFPDlQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQgilvvdkgmiasRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  114 SFLLDLASLVPTDAAYVQLGPHIPT-LRLNRFLRVPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPLPDREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 158186631  263 GSMSSVIYNMN 273
Cdd:pfam00520 224 AVIIDNFQELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
464-534 1.13e-26

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


:

Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.02  E-value: 1.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186631  464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 534
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-464 2.25e-24

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: 98.17  E-value: 2.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158186631 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 464
Cdd:cd00038   77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
34-273 6.83e-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: 120.45  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631   34 YYWWLNTMVFPIMYNLIIVVCRACFPDlQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQgilvvdkgmiasRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  114 SFLLDLASLVPTDAAYVQLGPHIPT-LRLNRFLRVPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPLPDREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 158186631  263 GSMSSVIYNMN 273
Cdd:pfam00520 224 AVIIDNFQELT 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
12-464 2.09e-27

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 117.28  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  12 STPPAPTKARKWlpVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFpdLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTG 91
Cdd:PLN03192  41 SYNQNHIGSDGW--IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  92 FLEQ--GILVVDKGMIASRYVRTWsFLLDLASLVPTDA-AY-----VQLGPHIPTLRLNRFLRVPRLFEAFDRTET--RT 161
Cdd:PLN03192 117 YIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQAlAYlitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 162 AYpnaFRI--AKLMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTP 236
Cdd:PLN03192 196 SY---FWIrcARLLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGD 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 237 LPDREE-EYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNKRLERRVIDwYQHLQINKK 315
Cdd:PLN03192 270 LHAVNTiEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAE 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 316 MTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAV 395
Cdd:PLN03192 349 SLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEI 428
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186631 396 VADDGVTQY--AVLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 464
Cdd:PLN03192 429 IDSEGEKERvvGTLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
464-534 1.13e-26

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.02  E-value: 1.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186631  464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 534
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-464 2.25e-24

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: 98.17  E-value: 2.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158186631 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 464
Cdd:cd00038   77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
348-467 2.08e-22

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: 92.46  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631   348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA---DDGVTQYAVLGAGLYFGEISIInikgN 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALL----T 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 158186631   425 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEK 467
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
366-457 8.17e-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: 75.72  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  366 PQTYSPGEYVCRKGDIGREMYIIREGQLAV--VADDGVTQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74
                          90
                  ....*....|....*
gi 158186631  443 FCLSKEDLREVLSEY 457
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
349-482 2.02e-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: 72.33  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQ-YAVLGAGLYFGEISIinikgnM 425
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158186631 426 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQ-AQAVMEEKGREILLKMNKLDVNA 482
Cdd:COG0664   75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA 132
PLN02868 PLN02868
acyl-CoA thioesterase family protein
343-481 1.85e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.41  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 343 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQYAVLGAGLYFGEisiin 420
Cdd:PLN02868  10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFGY----- 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186631 421 ikgNMSGNRRTANIKSLgySDLFCLS-KEDLREVLSEYPQAQAVMEEKGR---EILLKMNKLDVN 481
Cdd:PLN02868  85 ---GLSGSVHSADVVAV--SELTCLVlPHEHCHLLSPKSIWDSDKTPKDCslvERILHLEPLEVD 144
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
34-273 6.83e-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: 120.45  E-value: 6.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631   34 YYWWLNTMVFPIMYNLIIVVCRACFPDlQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQgilvvdkgmiasRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  114 SFLLDLASLVPTDAAYVQLGPHIPT-LRLNRFLRVPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPLPDREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 158186631  263 GSMSSVIYNMN 273
Cdd:pfam00520 224 AVIIDNFQELT 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
12-464 2.09e-27

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 117.28  E-value: 2.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  12 STPPAPTKARKWlpVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFpdLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTG 91
Cdd:PLN03192  41 SYNQNHIGSDGW--IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAF--LNASPKRGLEIADNVVDLFFAVDIVLTFFVA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  92 FLEQ--GILVVDKGMIASRYVRTWsFLLDLASLVPTDA-AY-----VQLGPHIPTLRLNRFLRVPRLFEAFDRTET--RT 161
Cdd:PLN03192 117 YIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQAlAYlitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 162 AYpnaFRI--AKLMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTP 236
Cdd:PLN03192 196 SY---FWIrcARLLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGD 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 237 LPDREE-EYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNKRLERRVIDwYQHLQINKK 315
Cdd:PLN03192 270 LHAVNTiEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAE 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 316 MTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAV 395
Cdd:PLN03192 349 SLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEI 428
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186631 396 VADDGVTQY--AVLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 464
Cdd:PLN03192 429 IDSEGEKERvvGTLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
464-534 1.13e-26

C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the C-terminal leucine-zipper domain of of cyclic nucleotide-gated channel proteins. The CLZ domains form homotypic trimers in solution thus constraining the channel of the CNGs to contain three cyclic nucleotide-gated subunits, CNGA. The CLZ domains formed homotypic parallel 3-helix coiled-coil domains, consistent with their proposed role in regulating subunit assembly.


Pssm-ID: 465160 [Multi-domain]  Cd Length: 70  Bit Score: 103.02  E-value: 1.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186631  464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 534
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-464 2.25e-24

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: 98.17  E-value: 2.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158186631 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 464
Cdd:cd00038   77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
348-467 2.08e-22

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: 92.46  E-value: 2.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631   348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA---DDGVTQYAVLGAGLYFGEISIInikgN 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALL----T 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 158186631   425 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEK 467
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
366-457 8.17e-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: 75.72  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631  366 PQTYSPGEYVCRKGDIGREMYIIREGQLAV--VADDGVTQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74
                          90
                  ....*....|....*
gi 158186631  443 FCLSKEDLREVLSEY 457
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
349-482 2.02e-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: 72.33  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQ-YAVLGAGLYFGEISIinikgnM 425
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158186631 426 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQ-AQAVMEEKGREILLKMNKLDVNA 482
Cdd:COG0664   75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA 132
PLN02868 PLN02868
acyl-CoA thioesterase family protein
343-481 1.85e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.41  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186631 343 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQYAVLGAGLYFGEisiin 420
Cdd:PLN02868  10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFGY----- 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186631 421 ikgNMSGNRRTANIKSLgySDLFCLS-KEDLREVLSEYPQAQAVMEEKGR---EILLKMNKLDVN 481
Cdd:PLN02868  85 ---GLSGSVHSADVVAV--SELTCLVlPHEHCHLLSPKSIWDSDKTPKDCslvERILHLEPLEVD 144
 
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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