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Conserved domains on  [gi|148683242|gb|EDL15189|]
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potassium intermediate/small conductance calcium-activated channel, subfamily N, member 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
271-380 2.36e-62

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 203.21  E-value: 2.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  271 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GLYSKDSMFSLALKCLISLSTVILLGLIIAYHTREVQLFVID 349
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 148683242  350 NGADDWRIAMTYERILYISLEMLVCAIHPIP 380
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD super family cl03763
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 562-597 2.36e-17

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.


The actual alignment was detected with superfamily member pfam02888:

Pssm-ID: 470872  Cd Length: 75  Bit Score: 76.94  E-value: 2.36e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 148683242  562 DTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAK 597
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSR 36
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 469-548 6.50e-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: 67.29  E-value: 6.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  469 ISLWIIAAWTVrvcerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 548
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Prefoldin super family cl09111
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
 583-637 1.51e-03

prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits; the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes, there are two or more paralogous genes encoding each subunit, adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


The actual alignment was detected with superfamily member PRK09343:

Pssm-ID: 471851 [Multi-domain]  Cd Length: 121  Bit Score: 38.90  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148683242 583 IYKHT-KLLKKIDHAKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSL 637
Cdd:PRK09343  56 IYKIVgNLLVKVDKTKVEKELKERKELLELRSRTLEKQEKKLREKLKELQAKINEM 111
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
271-380 2.36e-62

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 203.21  E-value: 2.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  271 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GLYSKDSMFSLALKCLISLSTVILLGLIIAYHTREVQLFVID 349
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 148683242  350 NGADDWRIAMTYERILYISLEMLVCAIHPIP 380
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 562-597 2.36e-17

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: 76.94  E-value: 2.36e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 148683242  562 DTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAK 597
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSR 36
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 562-597 9.47e-17

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: 75.14  E-value: 9.47e-17
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 148683242   562 DTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAK 597
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGR 36
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 469-548 6.50e-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: 67.29  E-value: 6.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  469 ISLWIIAAWTVrvcerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 548
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 583-637 1.51e-03

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 38.90  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148683242 583 IYKHT-KLLKKIDHAKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSL 637
Cdd:PRK09343  56 IYKIVgNLLVKVDKTKVEKELKERKELLELRSRTLEKQEKKLREKLKELQAKINEM 111
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
271-380 2.36e-62

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 203.21  E-value: 2.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  271 LGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSW-GLYSKDSMFSLALKCLISLSTVILLGLIIAYHTREVQLFVID 349
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 148683242  350 NGADDWRIAMTYERILYISLEMLVCAIHPIP 380
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 562-597 2.36e-17

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: 76.94  E-value: 2.36e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 148683242  562 DTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAK 597
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSR 36
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 562-597 9.47e-17

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: 75.14  E-value: 9.47e-17
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 148683242   562 DTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAK 597
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGR 36
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 469-548 6.50e-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: 67.29  E-value: 6.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683242  469 ISLWIIAAWTVrvcerYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLE 548
Cdd:pfam07885   3 LLLVLIFGTVY-----YLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 583-637 1.51e-03

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 38.90  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148683242 583 IYKHT-KLLKKIDHAKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSL 637
Cdd:PRK09343  56 IYKIVgNLLVKVDKTKVEKELKERKELLELRSRTLEKQEKKLREKLKELQAKINEM 111
 
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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