small conductance calcium-activated potassium channel protein 3 [Mus musculus]
SK_channel and CaMBD domain-containing protein( domain architecture ID 10507664)
protein containing domains SK_channel, Ion_trans_2, and CaMBD
List of domain hits
Name | Accession | Description | Interval | E-value | |||
SK_channel | pfam03530 | Calcium-activated SK potassium channel; |
271-380 | 2.62e-62 | |||
Calcium-activated SK potassium channel; : Pssm-ID: 460958 Cd Length: 111 Bit Score: 203.60 E-value: 2.62e-62
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CaMBD | pfam02888 | Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ... |
562-636 | 1.05e-43 | |||
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. : Pssm-ID: 460739 Cd Length: 75 Bit Score: 151.67 E-value: 1.05e-43
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Ion_trans_2 | pfam07885 | Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
469-548 | 2.77e-14 | |||
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. : Pssm-ID: 462301 [Multi-domain] Cd Length: 78 Bit Score: 68.45 E-value: 2.77e-14
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Name | Accession | Description | Interval | E-value | |||
SK_channel | pfam03530 | Calcium-activated SK potassium channel; |
271-380 | 2.62e-62 | |||
Calcium-activated SK potassium channel; Pssm-ID: 460958 Cd Length: 111 Bit Score: 203.60 E-value: 2.62e-62
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CaMBD | pfam02888 | Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ... |
562-636 | 1.05e-43 | |||
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. Pssm-ID: 460739 Cd Length: 75 Bit Score: 151.67 E-value: 1.05e-43
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CaMBD | smart01053 | Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ... |
562-637 | 1.24e-42 | |||
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. Pssm-ID: 198121 Cd Length: 76 Bit Score: 148.72 E-value: 1.24e-42
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Ion_trans_2 | pfam07885 | Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
469-548 | 2.77e-14 | |||
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. Pssm-ID: 462301 [Multi-domain] Cd Length: 78 Bit Score: 68.45 E-value: 2.77e-14
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Name | Accession | Description | Interval | E-value | |||
SK_channel | pfam03530 | Calcium-activated SK potassium channel; |
271-380 | 2.62e-62 | |||
Calcium-activated SK potassium channel; Pssm-ID: 460958 Cd Length: 111 Bit Score: 203.60 E-value: 2.62e-62
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CaMBD | pfam02888 | Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ... |
562-636 | 1.05e-43 | |||
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. Pssm-ID: 460739 Cd Length: 75 Bit Score: 151.67 E-value: 1.05e-43
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CaMBD | smart01053 | Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ... |
562-637 | 1.24e-42 | |||
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through this the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. Pssm-ID: 198121 Cd Length: 76 Bit Score: 148.72 E-value: 1.24e-42
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Ion_trans_2 | pfam07885 | Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
469-548 | 2.77e-14 | |||
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. Pssm-ID: 462301 [Multi-domain] Cd Length: 78 Bit Score: 68.45 E-value: 2.77e-14
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Blast search parameters | ||||
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