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Conserved domains on  [gi|2462602455|ref|XP_054208537|]
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small conductance calcium-activated potassium channel protein 2 isoform X1 [Homo sapiens]

Protein Classification

small conductance calcium-activated potassium channel protein( domain architecture ID 10507665)

small conductance calcium-activated potassium channel protein forms a voltage-independent potassium channel activated by intracellular calcium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
400-509 4.50e-62

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 204.75  E-value: 4.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 400 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVD 478
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462602455 479 NGADDWRIAMTYERIFFICLEILVCAIHPIP 509
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 691-766 2.24e-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: 198121  Cd Length: 76  Bit Score: 151.41  E-value: 2.24e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602455  691 DTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQN 766
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 598-677 1.00e-13

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: 66.91  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 598 ISLWIIAAWTVracerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 677
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
400-509 4.50e-62

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 204.75  E-value: 4.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 400 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVD 478
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462602455 479 NGADDWRIAMTYERIFFICLEILVCAIHPIP 509
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 691-766 2.24e-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: 198121  Cd Length: 76  Bit Score: 151.41  E-value: 2.24e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602455  691 DTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQN 766
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 691-765 2.97e-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: 148.20  E-value: 2.97e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462602455 691 DTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQ 765
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 598-677 1.00e-13

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: 66.91  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 598 ISLWIIAAWTVracerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 677
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
400-509 4.50e-62

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 204.75  E-value: 4.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 400 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVD 478
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462602455 479 NGADDWRIAMTYERIFFICLEILVCAIHPIP 509
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 691-766 2.24e-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: 198121  Cd Length: 76  Bit Score: 151.41  E-value: 2.24e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462602455  691 DTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQN 766
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 691-765 2.97e-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: 148.20  E-value: 2.97e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462602455 691 DTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQ 765
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 598-677 1.00e-13

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: 66.91  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 598 ISLWIIAAWTVracerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 677
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 725-796 1.97e-04

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 41.44  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462602455 725 AKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQNIMY------------DMISDLNERSEDFEKRIVTLETK 792
Cdd:pfam01920   2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKligdvlvkqdkeEVKEQLEERKETLEKEIKTLEKQ 81


                  ....
gi 2462602455 793 LETL 796
Cdd:pfam01920  82 LEKL 85
 
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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