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cyclic nucleotide-gated cation channel alpha-3 isoform X1 [Homo sapiens]
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
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
CLZ | pfam16526 | C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ... |
653-722 | 2.97e-36 | |||||
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: 130.75 E-value: 2.97e-36
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Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
223-465 | 9.09e-35 | |||||
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: 132.39 E-value: 9.09e-35
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CAP_ED | cd00038 | effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
537-653 | 2.83e-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: 2.83e-24
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Name | Accession | Description | Interval | E-value | |||||||
CLZ | pfam16526 | C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ... |
653-722 | 2.97e-36 | |||||||
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: 130.75 E-value: 2.97e-36
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Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
223-465 | 9.09e-35 | |||||||
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: 132.39 E-value: 9.09e-35
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CAP_ED | cd00038 | effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
537-653 | 2.83e-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: 2.83e-24
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PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
212-648 | 8.56e-22 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 101.10 E-value: 8.56e-22
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cNMP | smart00100 | Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
537-656 | 2.54e-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: 2.54e-21
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cNMP_binding | pfam00027 | Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
558-646 | 3.28e-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: 3.28e-16
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Crp | COG0664 | cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
538-705 | 1.94e-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: 70.02 E-value: 1.94e-13
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COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
636-725 | 1.51e-03 | |||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.51e-03
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Name | Accession | Description | Interval | E-value | |||||||
CLZ | pfam16526 | C-terminal leucine zipper domain of cyclic nucleotide-gated channels; The CLZ domain is the ... |
653-722 | 2.97e-36 | |||||||
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: 130.75 E-value: 2.97e-36
|
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Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
223-465 | 9.09e-35 | |||||||
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: 132.39 E-value: 9.09e-35
|
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CAP_ED | cd00038 | effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
537-653 | 2.83e-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: 2.83e-24
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PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
212-648 | 8.56e-22 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 101.10 E-value: 8.56e-22
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cNMP | smart00100 | Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
537-656 | 2.54e-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: 2.54e-21
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cNMP_binding | pfam00027 | Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
558-646 | 3.28e-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: 3.28e-16
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Crp | COG0664 | cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
538-705 | 1.94e-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: 70.02 E-value: 1.94e-13
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COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
636-725 | 1.51e-03 | |||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.51e-03
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Blast search parameters | ||||
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