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Conserved domains on  [gi|82617546|ref|NP_001032406|]
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cyclic nucleotide-gated channel alpha-4 [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 ...
 34-273 4.15e-32

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: 123.92  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546    34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|.
gi 82617546   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 2.14e-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: 102.25  E-value: 2.14e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82617546   464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 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 1.80e-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: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 82617546 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 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 4.15e-32

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: 123.92  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546    34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|.
gi 82617546   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 2.14e-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: 102.25  E-value: 2.14e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82617546   464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 534
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-464 1.27e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.80  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   26 VLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPDL--QHGYLVAwlvlDYTSDLLYLLDMVVRFHTGFLEQ--GILVVD 101
Cdd:PLN03192  53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNAspKRGLEIA----DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  102 KGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLNRFLRAPRLFEAFDRTET--RTAYpnaFRI--AK 171
Cdd:PLN03192 129 RKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcAR 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  172 LMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPPPAREE-EYLFM 247
Cdd:PLN03192 205 LLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFI 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  248 VGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLERRVIDwYQHLQINKKMTNEVAILQHLP 327
Cdd:PLN03192 282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLP 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  328 ERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQY--A 405
Cdd:PLN03192 361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 82617546  406 VLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 464
Cdd:PLN03192 441 TLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 348-464 1.80e-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: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 82617546 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 464
Cdd:cd00038  77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 348-467 1.06e-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: 90.54  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546    348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikgN 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 82617546    425 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 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 7.93e-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: 7.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   366 PQTYSPGEYVCRKGDIGQEMYIIREGQLAV--VADDGITQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 82617546   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 ...
 349-518 9.71e-15

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: 73.10  E-value: 9.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikgnM 425
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 426 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQLD 505
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQERLV 129

                       170
                ....*....|....*...
gi 82617546 506 DLQTK-----FARLLAEL 518
Cdd:COG0664 130 SLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 343-414 4.62e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 45.87  E-value: 4.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82617546  343 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQYAVLGAGLYFG 414
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 ...
 34-273 4.15e-32

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: 123.92  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546    34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223

                         250
                  ....*....|.
gi 82617546   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 2.14e-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: 102.25  E-value: 2.14e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82617546   464 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 534
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-464 1.27e-24

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.80  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   26 VLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPDL--QHGYLVAwlvlDYTSDLLYLLDMVVRFHTGFLEQ--GILVVD 101
Cdd:PLN03192  53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNAspKRGLEIA----DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  102 KGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLNRFLRAPRLFEAFDRTET--RTAYpnaFRI--AK 171
Cdd:PLN03192 129 RKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcAR 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  172 LMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPPPAREE-EYLFM 247
Cdd:PLN03192 205 LLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFI 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  248 VGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLERRVIDwYQHLQINKKMTNEVAILQHLP 327
Cdd:PLN03192 282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLP 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546  328 ERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQY--A 405
Cdd:PLN03192 361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 82617546  406 VLGAGLYFGEIsiinikGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 464
Cdd:PLN03192 441 TLGCGDIFGEV------GALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 348-464 1.80e-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: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikgn 424
Cdd:cd00038   1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 82617546 425 msGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 464
Cdd:cd00038  77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 348-467 1.06e-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: 90.54  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546    348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikgN 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----T 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 82617546    425 MSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 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 7.93e-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: 7.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546   366 PQTYSPGEYVCRKGDIGQEMYIIREGQLAV--VADDGITQ-YAVLGAGLYFGEISIINikgnmsGNRRTANIKSLGYSDL 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74

                          90
                  ....*....|....*
gi 82617546   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 ...
 349-518 9.71e-15

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: 73.10  E-value: 9.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikgnM 425
Cdd:COG0664   1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------L 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82617546 426 SGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQLD 505
Cdd:COG0664  75 GGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQERLV 129

                       170
                ....*....|....*...
gi 82617546 506 DLQTK-----FARLLAEL 518
Cdd:COG0664 130 SLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 343-414 4.62e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 45.87  E-value: 4.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82617546  343 LSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQYAVLGAGLYFG 414
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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