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Conserved domains on  [gi|2462522969|ref|XP_054223664|]
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cyclic nucleotide-gated channel alpha-4 isoform X1 [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 3.82e-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: 3.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 2462522969 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 ...
466-536 2.13e-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: 102.25  E-value: 2.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462522969 466 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 536
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-466 3.23e-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: 97.40  E-value: 3.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikat 424
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462522969 425 gnmsGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 466
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 3.82e-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: 3.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 2462522969 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 ...
466-536 2.13e-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: 102.25  E-value: 2.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462522969 466 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 536
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
26-466 7.31e-25

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.57  E-value: 7.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  26 VLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPDL--QHGYLVAwlvlDYTSDLLYLLDMVVRFHTGFLEQ--GILVVD 101
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNAspKRGLEIA----DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 102 KGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLNRFLRAPRLFEAFDRTET--RTAYpnaFRI--AK 171
Cdd:PLN03192  129 RKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcAR 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 172 LMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPPPAREE-EYLFM 247
Cdd:PLN03192  205 LLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFI 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 248 VGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLERRVIDwYQHLQINKKMTNEVAILQHLP 327
Cdd:PLN03192  282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLP 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 328 ERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQY--A 405
Cdd:PLN03192  361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462522969 406 VLGAGLYFGEISIINIKATGnmsgnrRTANIKSLgySDLFCLSKEDLREVLSEYPQAQTIM 466
Cdd:PLN03192  441 TLGCGDIFGEVGALCCRPQS------FTFRTKTL--SQLLRLKTSTLIEAMQTRQEDNVVI 493
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-466 3.23e-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: 97.40  E-value: 3.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikat 424
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462522969 425 gnmsGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 466
Cdd:cd00038    77 ----NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
348-469 1.85e-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: 89.77  E-value: 1.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikat 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462522969  425 gNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 469
Cdd:smart00100  76 -TNSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
366-459 1.44e-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: 74.95  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 366 PQTYSPGEYVCRKGDIGQEMYIIREGQLAV--VADDGITQ-YAVLGAGLYFGEISIINikatgnmsGNRRTANIKSLGYS 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG--------GEPRSATVVALTDS 72
                          90
                  ....*....|....*..
gi 2462522969 443 DLFCLSKEDLREVLSEY 459
Cdd:pfam00027  73 ELLVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
349-520 1.74e-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: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikatg 425
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 426 nMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQ 505
Cdd:COG0664    74 -LGGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQER 127
                         170       180
                  ....*....|....*....|
gi 2462522969 506 LDDLQTK-----FARLLAEL 520
Cdd:COG0664   128 LVSLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
343-414 4.44e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 46.25  E-value: 4.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462522969 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 3.82e-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: 3.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  34 YYWWLNTMVFPVMYNLIILVCRACFPDlQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQgilvvdkgrissRYVRTW 113
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQP-EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKK------------RYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 114 SFFLDLASLMPTDVVYVRLGPHTPT-LRLNRFLRAPRLFEAFDRTETRTAYPNA-FRIAKLMLYIFVVIHWNSCLYFALS 191
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVGSLSgLRVLRLLRLLRLLRLIRRLEGLRTLVNSlIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 192 RYLGFGR-DAWVYPDPAQPGFERlrrqYLYSFYFSTLILTTVG--DTPPPAREEE------YLFMVGDFLLAVMGFATIM 262
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNFDN----FPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|.
gi 2462522969 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 ...
466-536 2.13e-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: 102.25  E-value: 2.13e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462522969 466 MEEKGREILLKMNKLDVNAEAAEiALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEW 536
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAG-AEQKDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLEK 70
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
26-466 7.31e-25

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 109.57  E-value: 7.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  26 VLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPDL--QHGYLVAwlvlDYTSDLLYLLDMVVRFHTGFLEQ--GILVVD 101
Cdd:PLN03192   53 IISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNAspKRGLEIA----DNVVDLFFAVDIVLTFFVAYIDPrtQLLVRD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 102 KGRISSRYVRTWsFFLDLASLMPTDVV------YVRLGPHTPTLRLNRFLRAPRLFEAFDRTET--RTAYpnaFRI--AK 171
Cdd:PLN03192  129 RKKIAVRYLSTW-FLMDVASTIPFQALaylitgTVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKdiRFSY---FWIrcAR 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 172 LMLYIFVVIHWNSCLYFALS-RYLGFGRdAWVypDPAQPGFER--LRRQYLYSFYFSTLILTTVGDTPPPAREE-EYLFM 247
Cdd:PLN03192  205 LLSVTLFLVHCAGCLYYLIAdRYPHQGK-TWI--GAVIPNFREtsLWIRYISAIYWSITTMTTVGYGDLHAVNTiEMIFI 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 248 VGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLERRVIDwYQHLQINKKMTNEVAILQHLP 327
Cdd:PLN03192  282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILA-YMCLRFKAESLNQQQLIDQLP 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 328 ERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQY--A 405
Cdd:PLN03192  361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462522969 406 VLGAGLYFGEISIINIKATGnmsgnrRTANIKSLgySDLFCLSKEDLREVLSEYPQAQTIM 466
Cdd:PLN03192  441 TLGCGDIFGEVGALCCRPQS------FTFRTKTL--SQLLRLKTSTLIEAMQTRQEDNVVI 493
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
348-466 3.23e-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: 97.40  E-value: 3.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVA--DDGITQY-AVLGAGLYFGEISIINikat 424
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462522969 425 gnmsGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIM 466
Cdd:cd00038    77 ----NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
348-469 1.85e-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: 89.77  E-value: 1.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969  348 IFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVAD--DGITQ-YAVLGAGLYFGEISIInikat 424
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVleDGEEQiVGTLGPGDFFGELALL----- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462522969  425 gNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEK 469
Cdd:smart00100  76 -TNSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
366-459 1.44e-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: 74.95  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 366 PQTYSPGEYVCRKGDIGQEMYIIREGQLAV--VADDGITQ-YAVLGAGLYFGEISIINikatgnmsGNRRTANIKSLGYS 442
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG--------GEPRSATVVALTDS 72
                          90
                  ....*....|....*..
gi 2462522969 443 DLFCLSKEDLREVLSEY 459
Cdd:pfam00027  73 ELLVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
349-520 1.74e-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: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 349 FQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVV--ADDGITQ-YAVLGAGLYFGEISIinikatg 425
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSL------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462522969 426 nMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTimeekgreillkmnkldvnaeaaeiALQEATESRLRGLDQQ 505
Cdd:COG0664    74 -LGGEPSPATAEALEDSELLRIPREDLEELLERNPELAR-------------------------ALLRLLARRLRQLQER 127
                         170       180
                  ....*....|....*....|
gi 2462522969 506 LDDLQTK-----FARLLAEL 520
Cdd:COG0664   128 LVSLAFLsaeerLARFLLEL 147
PLN02868 PLN02868
acyl-CoA thioesterase family protein
343-414 4.44e-05

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 46.25  E-value: 4.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462522969 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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