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Conserved domains on  [gi|1370458772|ref|XP_024304121|]
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cyclic nucleotide-gated channel alpha-4 isoform X3 [Homo sapiens]

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 ...
 1-233 2.91e-29

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: 115.44  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772   1 MVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTWSFFLDLA 80
Cdd:pfam00520   8 ILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSPWNILDFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  81 SLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALSRYLGFGR 158
Cdd:pfam00520  75 VVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 159 -DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIMGSMSSVI 229
Cdd:pfam00520 155 lKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIAVIIDNF 230


                  ....
gi 1370458772 230 YNMN 233
Cdd:pfam00520 231 QELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 424-494 4.16e-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: 101.09  E-value: 4.16e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370458772 424 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 494
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 308-424 5.88e-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: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 308 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 384
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370458772 385 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 424
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 ...
 1-233 2.91e-29

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: 115.44  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772   1 MVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTWSFFLDLA 80
Cdd:pfam00520   8 ILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSPWNILDFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  81 SLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALSRYLGFGR 158
Cdd:pfam00520  75 VVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 159 -DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIMGSMSSVI 229
Cdd:pfam00520 155 lKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIAVIIDNF 230


                  ....
gi 1370458772 230 YNMN 233
Cdd:pfam00520 231 QELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 424-494 4.16e-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: 101.09  E-value: 4.16e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370458772 424 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 494
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 308-424 5.88e-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: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 308 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 384
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370458772 385 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 424
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-424 3.29e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 100.71  E-value: 3.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  31 VLDYTSDLLYLLDMVVRFHTGFLEQ--GILVVDKGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLN 102
Cdd:PLN03192   96 IADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLL 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 103 RFLRAPRLFEAFDRTET--RTAYpnaFRI--AKLMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LR 175
Cdd:PLN03192  175 RFWRLRRVKQLFTRLEKdiRFSY---FWIrcARLLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLW 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 176 RQYLYSFYFSTLILTTVGDTPPPAREE-EYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQH 254
Cdd:PLN03192  249 IRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNR 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 255 VNRKLERRVIDwYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEY 334
Cdd:PLN03192  329 LPPRLKDQILA-YMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 335 VCRKGDIGQEMYIIREGQLAVVADDGITQY--AVLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLRE 412
Cdd:PLN03192  408 VIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvGTLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIE 481

                         410
                  ....*....|..
gi 1370458772 413 VLSEYPQAQTIM 424
Cdd:PLN03192  482 AMQTRQEDNVVI 493
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 308-427 3.69e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 89.00  E-value: 3.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  308 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikgN 384
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370458772  385 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 427
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 326-417 1.80e-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: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 326 PQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 402
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1370458772 403 FCLSKEDLREVLSEY 417
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 309-478 3.41e-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: 71.56  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 309 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikgnM 385
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 386 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQLD 465
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQERLV 129

                         170
                  ....*....|....*...
gi 1370458772 466 DLQTK-----FARLLAEL 478
Cdd:COG0664   130 SLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 303-374 4.17e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 45.87  E-value: 4.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370458772 303 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQYAVLGAGLYFG 374
Cdd:PLN02868   10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFG 83
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 1-233 2.91e-29

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: 115.44  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772   1 MVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTWSFFLDLA 80
Cdd:pfam00520   8 ILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSPWNILDFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  81 SLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALSRYLGFGR 158
Cdd:pfam00520  75 VVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 159 -DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIMGSMSSVI 229
Cdd:pfam00520 155 lKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFIAVIIDNF 230


                  ....
gi 1370458772 230 YNMN 233
Cdd:pfam00520 231 QELT 234
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
 424-494 4.16e-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: 101.09  E-value: 4.16e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370458772 424 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 494
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 308-424 5.88e-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: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 308 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 384
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370458772 385 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 424
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-424 3.29e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 100.71  E-value: 3.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  31 VLDYTSDLLYLLDMVVRFHTGFLEQ--GILVVDKGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLN 102
Cdd:PLN03192   96 IADNVVDLFFAVDIVLTFFVAYIDPrtQLLVRDRKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLL 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 103 RFLRAPRLFEAFDRTET--RTAYpnaFRI--AKLMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LR 175
Cdd:PLN03192  175 RFWRLRRVKQLFTRLEKdiRFSY---FWIrcARLLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLW 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 176 RQYLYSFYFSTLILTTVGDTPPPAREE-EYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQH 254
Cdd:PLN03192  249 IRYISAIYWSITTMTTVGYGDLHAVNTiEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNR 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 255 VNRKLERRVIDwYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEY 334
Cdd:PLN03192  329 LPPRLKDQILA-YMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPRED 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 335 VCRKGDIGQEMYIIREGQLAVVADDGITQY--AVLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLRE 412
Cdd:PLN03192  408 VIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvGTLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIE 481

                         410
                  ....*....|..
gi 1370458772 413 VLSEYPQAQTIM 424
Cdd:PLN03192  482 AMQTRQEDNVVI 493
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 308-427 3.69e-21

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 89.00  E-value: 3.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772  308 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikgN 384
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1370458772  385 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 427
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 326-417 1.80e-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: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 326 PQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 402
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTleDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 1370458772 403 FCLSKEDLREVLSEY 417
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 309-478 3.41e-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: 71.56  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 309 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikgnM 385
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370458772 386 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQLD 465
Cdd:COG0664    75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQERLV 129

                         170
                  ....*....|....*...
gi 1370458772 466 DLQTK-----FARLLAEL 478
Cdd:COG0664   130 SLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 303-374 4.17e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 45.87  E-value: 4.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370458772 303 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQYAVLGAGLYFG 374
Cdd:PLN02868   10 LGSVPLLQRLPSSSLKKIAEVVVPKRYGKGEYVVREGEPGDGLYFIWKGEAEVSgpAEEESRPEFLLKRYDYFG 83
 
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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