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Conserved domains on  [gi|1008426590|ref|XP_015835760|]
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small conductance calcium-activated potassium channel protein isoform X1 [Tribolium castaneum]

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;
342-452 6.47e-60

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.20  E-value: 6.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 342 LGRRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYRKDDFYSIALKTLISVSTVILLGLIVAYHALEVQLFMID 421
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1008426590 422 NCADDWRIAMTWQRICQITMELVICAVHPIP 452
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 634-708 5.60e-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: 147.04  E-value: 5.60e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008426590 634 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 708
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 541-620 2.60e-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: 65.75  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 541 FMVSLWIIASWTLRQCERFhdeEHANLLNAMWLIAITFLSVGFGDIVPNTYCGRGIAVSTGIMGAGCTALLVAVVSRKLE 620
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
342-452 6.47e-60

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.20  E-value: 6.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 342 LGRRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYRKDDFYSIALKTLISVSTVILLGLIVAYHALEVQLFMID 421
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1008426590 422 NCADDWRIAMTWQRICQITMELVICAVHPIP 452
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 634-708 5.60e-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: 147.04  E-value: 5.60e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008426590 634 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 708
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 634-709 3.83e-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: 144.86  E-value: 3.83e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008426590  634 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQN 709
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 541-620 2.60e-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: 65.75  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 541 FMVSLWIIASWTLRQCERFhdeEHANLLNAMWLIAITFLSVGFGDIVPNTYCGRGIAVSTGIMGAGCTALLVAVVSRKLE 620
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
342-452 6.47e-60

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 198.20  E-value: 6.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 342 LGRRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYRKDDFYSIALKTLISVSTVILLGLIVAYHALEVQLFMID 421
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1008426590 422 NCADDWRIAMTWQRICQITMELVICAVHPIP 452
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 634-708 5.60e-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: 147.04  E-value: 5.60e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008426590 634 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQ 708
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 634-709 3.83e-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: 144.86  E-value: 3.83e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008426590  634 DTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQN 709
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 541-620 2.60e-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: 65.75  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 541 FMVSLWIIASWTLRQCERFhdeEHANLLNAMWLIAITFLSVGFGDIVPNTYCGRGIAVSTGIMGAGCTALLVAVVSRKLE 620
Cdd:pfam07885   1 IVLLLVLIFGTVYYLLEEG---WEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 487-616 6.95e-03

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: 39.17  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008426590 487 FLRLYLICRVMLLHSKLftdassRSIGALNRINFNTrfvLKTLMTICpgtVLLVFMVSLWIIASWTLRQCERFHDEEHA- 565
Cdd:pfam00520  96 VLRLLRLLRLLRLIRRL------EGLRTLVNSLIRS---LKSLGNLL---LLLLLFLFIFAIIGYQLFGGKLKTWENPDn 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008426590 566 ------NLLNAMWLIAITFLSVGFGDIVPNTYCGRGIAVSTG-------IMGAGCTALLVAVVS 616
Cdd:pfam00520 164 grtnfdNFPNAFLWLFQTMTTEGWGDIMYDTIDGKGEFWAYIyfvsfiiLGGFLLLNLFIAVII 227
 
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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