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Conserved domains on  [gi|281359898|ref|NP_525078|]
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small conductance calcium-activated potassium channel, isoform L [Drosophila melanogaster]

Protein Classification

SK_channel and CaMBD domain-containing protein( domain architecture ID 10507664)

protein containing domains SK_channel, Ion_trans_2, and CaMBD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
67-177 1.52e-61

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.59  E-value: 1.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898   67 LGKRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYTKASFYSTALKTLISVSTVILLGLIVAYHALEVQLFMID 146
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 281359898  147 NCADDWRIAMTWQRISQIGLELFICAIHPIP 177
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 358-432 8.05e-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: 460739  Cd Length: 75  Bit Score: 144.73  E-value: 8.05e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359898  358 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 432
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 265-344 2.84e-11

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: 59.59  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898  265 FMVSLWIIASWTLRQCERFhdeEHANLLNSMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMVGAGCTALLVAVVSRKLE 344
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
67-177 1.52e-61

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.59  E-value: 1.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898   67 LGKRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYTKASFYSTALKTLISVSTVILLGLIVAYHALEVQLFMID 146
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 281359898  147 NCADDWRIAMTWQRISQIGLELFICAIHPIP 177
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 358-432 8.05e-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: 460739  Cd Length: 75  Bit Score: 144.73  E-value: 8.05e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359898  358 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 432
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 358-433 5.75e-41

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: 142.55  E-value: 5.75e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359898   358 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQN 433
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 265-344 2.84e-11

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: 59.59  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898  265 FMVSLWIIASWTLRQCERFhdeEHANLLNSMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMVGAGCTALLVAVVSRKLE 344
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
67-177 1.52e-61

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.59  E-value: 1.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898   67 LGKRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYTKASFYSTALKTLISVSTVILLGLIVAYHALEVQLFMID 146
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 281359898  147 NCADDWRIAMTWQRISQIGLELFICAIHPIP 177
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 358-432 8.05e-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: 460739  Cd Length: 75  Bit Score: 144.73  E-value: 8.05e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281359898  358 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 432
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 358-433 5.75e-41

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: 142.55  E-value: 5.75e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281359898   358 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQN 433
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 265-344 2.84e-11

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: 59.59  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281359898  265 FMVSLWIIASWTLRQCERFhdeEHANLLNSMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMVGAGCTALLVAVVSRKLE 344
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
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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