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Conserved domains on  [gi|1953105646|ref|XP_038444780|]
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cyclic nucleotide-gated olfactory channel [Canis lupus familiaris]

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 ...
140-382 6.27e-37

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: 138.17  E-value: 6.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 140 YYRWLFVIAMPVLYNWCLLVARACFSDLQKgYYLVWLVLDYFSDVVYITDLFIRLRTGFLeqgllvkdskklRDNYIHTL 219
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEP-LTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 220 QFKLDVASIIPTDLIYFAVGI-HRPELRFNRLLHFARMFEFFDRTETRTSYPN-IFRISNLVLYILVIIHWNACIYYAIS 297
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVgSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 298 KSIGFGV-DTWVYPNITDPEYgylaREYIYCLYWSTLTLTTIG--ETPPPVKDEE------YLFVIFDFLIGVLIFATIV 368
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|....
gi 1953105646 369 GNVGSMISNMNATR 382
Cdd:pfam00520 224 AVIIDNFQELTERT 237
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
570-637 2.50e-27

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: 104.94  E-value: 2.50e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953105646 570 LEERGREILMKEGLLDETEVAASMDI-DVQEKLEQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLE 637
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQkDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
454-570 1.67e-23

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: 95.86  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 454 IFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVA--DDGVTQY-ALLSAGSCFGEISILNikgs 530
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953105646 531 kmGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVL 570
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 ...
140-382 6.27e-37

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: 138.17  E-value: 6.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 140 YYRWLFVIAMPVLYNWCLLVARACFSDLQKgYYLVWLVLDYFSDVVYITDLFIRLRTGFLeqgllvkdskklRDNYIHTL 219
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEP-LTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 220 QFKLDVASIIPTDLIYFAVGI-HRPELRFNRLLHFARMFEFFDRTETRTSYPN-IFRISNLVLYILVIIHWNACIYYAIS 297
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVgSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 298 KSIGFGV-DTWVYPNITDPEYgylaREYIYCLYWSTLTLTTIG--ETPPPVKDEE------YLFVIFDFLIGVLIFATIV 368
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|....
gi 1953105646 369 GNVGSMISNMNATR 382
Cdd:pfam00520 224 AVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
131-565 1.46e-27

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 118.82  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 131 FVLDPAGDWYYRWLFVIAMPVLYN-WCLLVARACF-SDLQKGYYLVWLVLDYFSDVVYITDLF---IRLRTGfleqgLLV 205
Cdd:PLN03192   52 WIISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLnASPKRGLEIADNVVDLFFAVDIVLTFFvayIDPRTQ-----LLV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 206 KDSKKLRDNYIHTLqFKLDVASIIPTD-LIYFAVGIHRPELRFN-----RLLHFARMFEFFDRTET--RTSYPNIfRISN 277
Cdd:PLN03192  127 RDRKKIAVRYLSTW-FLMDVASTIPFQaLAYLITGTVKLNLSYSllgllRFWRLRRVKQLFTRLEKdiRFSYFWI-RCAR 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 278 LVLYILVIIHWNACIYYAISKSIGFGVDTW---VYPNITDPEygyLAREYIYCLYWSTLTLTTIGETP-PPVKDEEYLFV 353
Cdd:PLN03192  205 LLSVTLFLVHCAGCLYYLIADRYPHQGKTWigaVIPNFRETS---LWIRYISAIYWSITTMTTVGYGDlHAVNTIEMIFI 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 354 IFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKEMEAKVIKWFdYLWTNKKSVDEREVLKNLP 433
Cdd:PLN03192  282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM-CLRFKAESLNQQQLIDQLP 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 434 AKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQY--A 511
Cdd:PLN03192  361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953105646 512 LLSAGSCFGEISILNIKGSKMgnrrTANIRSLgySDLFCLSKDDLMEAVTEYPD 565
Cdd:PLN03192  441 TLGCGDIFGEVGALCCRPQSF----TFRTKTL--SQLLRLKTSTLIEAMQTRQE 488
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
570-637 2.50e-27

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: 104.94  E-value: 2.50e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953105646 570 LEERGREILMKEGLLDETEVAASMDI-DVQEKLEQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLE 637
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQkDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
454-570 1.67e-23

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: 95.86  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 454 IFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVA--DDGVTQY-ALLSAGSCFGEISILNikgs 530
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953105646 531 kmGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVL 570
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
454-573 7.53e-20

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: 85.53  E-value: 7.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646  454 IFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVA---DDGVTQYALLSAGSCFGEISILNikgs 530
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALLT---- 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1953105646  531 KMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEER 573
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
472-563 2.70e-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: 74.18  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 472 PQVFSPGDYICRKGDIGKEMYIIKEGKLAV--VADDGVTQ-YALLSAGSCFGEISILNikgskmGNRRTANIRSLGYSDL 548
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74
                          90
                  ....*....|....*
gi 1953105646 549 FCLSKDDLMEAVTEY 563
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
455-625 2.52e-13

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: 69.25  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 455 FQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVV--ADDGVTQ-YALLSAGSCFGEISILNikgsk 531
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSLLG----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 532 mGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLeerGREILMKEGLLDETEVAASMDiDVQEKLEQLetnMETL 611
Cdd:COG0664    76 -GEPSPATAEALEDSELLRIPREDLEELLERNPELARAL---LRLLARRLRQLQERLVSLAFL-SAEERLARF---LLEL 147
                         170       180
                  ....*....|....*....|...
gi 1953105646 612 YTRFGRL---------LAEYTGA 625
Cdd:COG0664   148 ADRLDGRidlpltqeeIASYLGL 170
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
140-382 6.27e-37

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: 138.17  E-value: 6.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 140 YYRWLFVIAMPVLYNWCLLVARACFSDLQKgYYLVWLVLDYFSDVVYITDLFIRLRTGFLeqgllvkdskklRDNYIHTL 219
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEP-LTTVLEILDYVFTGIFTLEMLLKIIAAGF------------KKRYFRSP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 220 QFKLDVASIIPTDLIYFAVGI-HRPELRFNRLLHFARMFEFFDRTETRTSYPN-IFRISNLVLYILVIIHWNACIYYAIS 297
Cdd:pfam00520  68 WNILDFVVVLPSLISLVLSSVgSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNsLIRSLKSLGNLLLLLLLFLFIFAIIG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 298 KSIGFGV-DTWVYPNITDPEYgylaREYIYCLYWSTLTLTTIG--ETPPPVKDEE------YLFVIFDFLIGVLIFATIV 368
Cdd:pfam00520 148 YQLFGGKlKTWENPDNGRTNF----DNFPNAFLWLFQTMTTEGwgDIMYDTIDGKgefwayIYFVSFIILGGFLLLNLFI 223
                         250
                  ....*....|....
gi 1953105646 369 GNVGSMISNMNATR 382
Cdd:pfam00520 224 AVIIDNFQELTERT 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
131-565 1.46e-27

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 118.82  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 131 FVLDPAGDWYYRWLFVIAMPVLYN-WCLLVARACF-SDLQKGYYLVWLVLDYFSDVVYITDLF---IRLRTGfleqgLLV 205
Cdd:PLN03192   52 WIISPMDSRYRWWETLMVVLVAYSaWVYPFEVAFLnASPKRGLEIADNVVDLFFAVDIVLTFFvayIDPRTQ-----LLV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 206 KDSKKLRDNYIHTLqFKLDVASIIPTD-LIYFAVGIHRPELRFN-----RLLHFARMFEFFDRTET--RTSYPNIfRISN 277
Cdd:PLN03192  127 RDRKKIAVRYLSTW-FLMDVASTIPFQaLAYLITGTVKLNLSYSllgllRFWRLRRVKQLFTRLEKdiRFSYFWI-RCAR 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 278 LVLYILVIIHWNACIYYAISKSIGFGVDTW---VYPNITDPEygyLAREYIYCLYWSTLTLTTIGETP-PPVKDEEYLFV 353
Cdd:PLN03192  205 LLSVTLFLVHCAGCLYYLIADRYPHQGKTWigaVIPNFRETS---LWIRYISAIYWSITTMTTVGYGDlHAVNTIEMIFI 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 354 IFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKEMEAKVIKWFdYLWTNKKSVDEREVLKNLP 433
Cdd:PLN03192  282 IFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKDQILAYM-CLRFKAESLNQQQLIDQLP 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 434 AKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQY--A 511
Cdd:PLN03192  361 KSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERvvG 440
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953105646 512 LLSAGSCFGEISILNIKGSKMgnrrTANIRSLgySDLFCLSKDDLMEAVTEYPD 565
Cdd:PLN03192  441 TLGCGDIFGEVGALCCRPQSF----TFRTKTL--SQLLRLKTSTLIEAMQTRQE 488
CLZ pfam16526
C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ...
570-637 2.50e-27

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: 104.94  E-value: 2.50e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953105646 570 LEERGREILMKEGLLDETEVAASMDI-DVQEKLEQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLE 637
Cdd:pfam16526   1 LEEKGRQILLKDGLLDEAAANAGAEQkDLEEKVERLESSLDVLQTRLARLLAELESSQLKLKQRITKLE 69
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
454-570 1.67e-23

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: 95.86  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 454 IFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVA--DDGVTQY-ALLSAGSCFGEISILNikgs 530
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKldEDGREQIvGFLGPGDLFGELALLG---- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953105646 531 kmGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVL 570
Cdd:cd00038    77 --NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
454-573 7.53e-20

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: 85.53  E-value: 7.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646  454 IFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVA---DDGVTQYALLSAGSCFGEISILNikgs 530
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKvleDGEEQIVGTLGPGDFFGELALLT---- 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1953105646  531 KMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEER 573
Cdd:smart00100  77 NSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
472-563 2.70e-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: 74.18  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 472 PQVFSPGDYICRKGDIGKEMYIIKEGKLAV--VADDGVTQ-YALLSAGSCFGEISILNikgskmGNRRTANIRSLGYSDL 548
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVyrTLEDGREQiLAVLGPGDFFGELALLG------GEPRSATVVALTDSEL 74
                          90
                  ....*....|....*
gi 1953105646 549 FCLSKDDLMEAVTEY 563
Cdd:pfam00027  75 LVIPREDFLELLERD 89
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
455-625 2.52e-13

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: 69.25  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 455 FQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVV--ADDGVTQ-YALLSAGSCFGEISILNikgsk 531
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYriSEDGREQiLGFLGPGDFFGELSLLG----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953105646 532 mGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLeerGREILMKEGLLDETEVAASMDiDVQEKLEQLetnMETL 611
Cdd:COG0664    76 -GEPSPATAEALEDSELLRIPREDLEELLERNPELARAL---LRLLARRLRQLQERLVSLAFL-SAEERLARF---LLEL 147
                         170       180
                  ....*....|....*....|...
gi 1953105646 612 YTRFGRL---------LAEYTGA 625
Cdd:COG0664   148 ADRLDGRidlpltqeeIASYLGL 170
 
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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