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Conserved domains on  [gi|1720422260|ref|XP_030098357|]
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cyclic nucleotide-gated cation channel alpha-4 isoform X2 [Mus musculus]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13328420)

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

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List of domain hits

 Name Accession Description Interval E-value
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 361-431 1.28e-25

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: 99.16  E-value: 1.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422260 361 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 431
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 245-361 4.06e-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: 96.63  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 245 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 321
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720422260 322 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 2-361 4.15e-21

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 96.86  E-value: 4.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260   2 IASRYVRTWsFLLDLASLVPTDA-AY-----VQLGPHIPTLRLNRFLRVPRLFEAFDRTET--RTAYpnaFRI--AKLMI 71
Cdd:PLN03192  132 IAVRYLSTW-FLMDVASTIPFQAlAYlitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcARLLS 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  72 YIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPLPAREE-EYLFMVGD 147
Cdd:PLN03192  208 VTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFY 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 148 FLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRRLERRVIDwYQHLQINKKMTNEVAILQHLPERL 227
Cdd:PLN03192  285 MLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLPKSI 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 228 RAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQY--AVLG 305
Cdd:PLN03192  364 CKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvGTLG 443

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422260 306 AGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:PLN03192  444 CGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
 
Name Accession Description Interval E-value
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 361-431 1.28e-25

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: 99.16  E-value: 1.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422260 361 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 431
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 245-361 4.06e-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: 96.63  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 245 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 321
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720422260 322 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 245-364 5.46e-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: 90.92  E-value: 5.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  245 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA---DDGVTQYAVLGAGLYFGEISIInikgN 321
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720422260  322 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEK 364
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-361 4.15e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 96.86  E-value: 4.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260   2 IASRYVRTWsFLLDLASLVPTDA-AY-----VQLGPHIPTLRLNRFLRVPRLFEAFDRTET--RTAYpnaFRI--AKLMI 71
Cdd:PLN03192  132 IAVRYLSTW-FLMDVASTIPFQAlAYlitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcARLLS 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  72 YIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPLPAREE-EYLFMVGD 147
Cdd:PLN03192  208 VTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFY 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 148 FLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRRLERRVIDwYQHLQINKKMTNEVAILQHLPERL 227
Cdd:PLN03192  285 MLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLPKSI 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 228 RAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQY--AVLG 305
Cdd:PLN03192  364 CKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvGTLG 443

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422260 306 AGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:PLN03192  444 CGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 5-170 4.78e-21

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: 91.94  E-value: 4.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260   5 RYVRTWSFLLDLASLVPTDAAYVQLGPHIPT-LRLNRFLRVPRLFEAFDRTETRTAYPNA-FRIAKLMIYIFVVIHWNSC 82
Cdd:pfam00520  62 RYFRSPWNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  83 LYFALSRYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPLPAREEE------YLFMVGDFLLAVM 153
Cdd:pfam00520 142 IFAIIGYQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFL 217

                         170
                  ....*....|....*..
gi 1720422260 154 GFATIMGSMSSVIYNMN 170
Cdd:pfam00520 218 LLNLFIAVIIDNFQELT 234
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 263-354 1.34e-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: 74.57  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 263 PQTYSPGEYVCRKGDIGREMYIIREGQLAV--VADDGVTQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 339
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1720422260 340 FCLSKEDLREVLSEY 354
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 246-379 7.54e-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: 70.40  E-value: 7.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 246 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQ-YAVLGAGLYFGEISIinikgnM 322
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422260 323 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQ-AQAVMEEKGREILLKMNKLDVNA 379
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA 132
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 240-378 1.53e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.02  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 240 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQYAVLGAGLYFGEisiin 317
Cdd:PLN02868   10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFGY----- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422260 318 ikgNMSGNRRTANIKSLgySDLFCLS-KEDLREVLSEYPQAQAVMEEKGR---EILLKMNKLDVN 378
Cdd:PLN02868   85 ---GLSGSVHSADVVAV--SELTCLVlPHEHCHLLSPKSIWDSDKTPKDCslvERILHLEPLEVD 144
 
Name Accession Description Interval E-value
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 361-431 1.28e-25

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: 99.16  E-value: 1.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422260 361 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 431
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 245-361 4.06e-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: 96.63  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 245 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA--DDGVTQY-AVLGAGLYFGEISIINikgn 321
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720422260 322 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 245-364 5.46e-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: 90.92  E-value: 5.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  245 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVA---DDGVTQYAVLGAGLYFGEISIInikgN 321
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720422260  322 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEK 364
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-361 4.15e-21

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 96.86  E-value: 4.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260   2 IASRYVRTWsFLLDLASLVPTDA-AY-----VQLGPHIPTLRLNRFLRVPRLFEAFDRTET--RTAYpnaFRI--AKLMI 71
Cdd:PLN03192  132 IAVRYLSTW-FLMDVASTIPFQAlAYlitgtVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcARLLS 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  72 YIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPLPAREE-EYLFMVGD 147
Cdd:PLN03192  208 VTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFY 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 148 FLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRRLERRVIDwYQHLQINKKMTNEVAILQHLPERL 227
Cdd:PLN03192  285 MLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLPKSI 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 228 RAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQY--AVLG 305
Cdd:PLN03192  364 CKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvGTLG 443

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422260 306 AGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVM 361
Cdd:PLN03192  444 CGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 5-170 4.78e-21

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: 91.94  E-value: 4.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260   5 RYVRTWSFLLDLASLVPTDAAYVQLGPHIPT-LRLNRFLRVPRLFEAFDRTETRTAYPNA-FRIAKLMIYIFVVIHWNSC 82
Cdd:pfam00520  62 RYFRSPWNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260  83 LYFALSRYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPLPAREEE------YLFMVGDFLLAVM 153
Cdd:pfam00520 142 IFAIIGYQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFL 217

                         170
                  ....*....|....*..
gi 1720422260 154 GFATIMGSMSSVIYNMN 170
Cdd:pfam00520 218 LLNLFIAVIIDNFQELT 234
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 263-354 1.34e-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: 74.57  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 263 PQTYSPGEYVCRKGDIGREMYIIREGQLAV--VADDGVTQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 339
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1720422260 340 FCLSKEDLREVLSEY 354
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 246-379 7.54e-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: 70.40  E-value: 7.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 246 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQ-YAVLGAGLYFGEISIinikgnM 322
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422260 323 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQ-AQAVMEEKGREILLKMNKLDVNA 379
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPElARALLRLLARRLRQLQERLVSLA 132
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 240-378 1.53e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 47.02  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422260 240 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVV--ADDGVTQYAVLGAGLYFGEisiin 317
Cdd:PLN02868   10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFGY----- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422260 318 ikgNMSGNRRTANIKSLgySDLFCLS-KEDLREVLSEYPQAQAVMEEKGR---EILLKMNKLDVN 378
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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