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Conserved domains on  [gi|293324810|emb|CBL43424|]
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Calmodulin-binding domain-containing protein [Caenorhabditis elegans]

Protein Classification

small conductance calcium-activated potassium channel protein; potassium channel family protein( domain architecture ID 10507660)

small conductance calcium-activated potassium channel protein forms a voltage-independent potassium channel activated by intracellular calcium| potassium channel family protein spans the cell membrane to form a conduction pathway or pore, through which selective ions such as potassium, sodium, and calcium translocate across cell membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
11-124 1.86e-32

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 118.85  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810   11 WKIRRRLSDLKVKLCDATLILAVGGLILAMLDVEFTATRILESfvnTSDLSFILRTAAIITTIALLFFLLFYHFIDIKIQ 90
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSK---GSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLF 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 293324810   91 LVETGTSNWRVGITSERVLNTLLEVAICAICPIP 124
Cdd:pfam03530  78 MVDNGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD super family cl03763
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 308-380 3.28e-27

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 smart01053:

Pssm-ID: 470872  Cd Length: 76  Bit Score: 103.26  E-value: 3.28e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 293324810   308 ENNITNEHKNAAACVLQNTWRTvlraRDYQKSSSRRNQQRLAKMQRMLLCSVITFRKTRWKLRMQMEDEDDFF 380
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLI----YKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLV 69
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 206-294 2.05e-09

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: 53.81  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810  206 LFVLSIASLMFWCVVSWMLTqceryaypsisgfqhFADYLWFEIITFFSIGYGDVQVNTYCGRGLAMLTAIVGTLFSSTL 285
Cdd:pfam07885   4 LLVLIFGTVYYLLEEGWEWS---------------FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIF 68


                  ....*....
gi 293324810  286 IALISRKLI 294
Cdd:pfam07885  69 LAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
11-124 1.86e-32

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 118.85  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810   11 WKIRRRLSDLKVKLCDATLILAVGGLILAMLDVEFTATRILESfvnTSDLSFILRTAAIITTIALLFFLLFYHFIDIKIQ 90
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSK---GSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLF 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 293324810   91 LVETGTSNWRVGITSERVLNTLLEVAICAICPIP 124
Cdd:pfam03530  78 MVDNGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 308-380 3.28e-27

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: 103.26  E-value: 3.28e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 293324810   308 ENNITNEHKNAAACVLQNTWRTvlraRDYQKSSSRRNQQRLAKMQRMLLCSVITFRKTRWKLRMQMEDEDDFF 380
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLI----YKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLV 69
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 308-386 6.57e-24

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: 94.27  E-value: 6.57e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 293324810  308 ENNITNEHKNAAACVLQNTWrTVLRARDYQKsssRRNQQRLAKMQRMLLCSVITFRKTRWKLRMQMEDEDDFFTARRAF 386
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETW-LIYKHTKLVK---KRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 206-294 2.05e-09

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: 53.81  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810  206 LFVLSIASLMFWCVVSWMLTqceryaypsisgfqhFADYLWFEIITFFSIGYGDVQVNTYCGRGLAMLTAIVGTLFSSTL 285
Cdd:pfam07885   4 LLVLIFGTVYYLLEEGWEWS---------------FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIF 68


                  ....*....
gi 293324810  286 IALISRKLI 294
Cdd:pfam07885  69 LAVLGRFLT 77
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
11-124 1.86e-32

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 118.85  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810   11 WKIRRRLSDLKVKLCDATLILAVGGLILAMLDVEFTATRILESfvnTSDLSFILRTAAIITTIALLFFLLFYHFIDIKIQ 90
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTALGVYSK---GSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLF 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 293324810   91 LVETGTSNWRVGITSERVLNTLLEVAICAICPIP 124
Cdd:pfam03530  78 MVDNGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 308-380 3.28e-27

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: 103.26  E-value: 3.28e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 293324810   308 ENNITNEHKNAAACVLQNTWRTvlraRDYQKSSSRRNQQRLAKMQRMLLCSVITFRKTRWKLRMQMEDEDDFF 380
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLI----YKHTKLVKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLV 69
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 308-386 6.57e-24

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: 94.27  E-value: 6.57e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 293324810  308 ENNITNEHKNAAACVLQNTWrTVLRARDYQKsssRRNQQRLAKMQRMLLCSVITFRKTRWKLRMQMEDEDDFFTARRAF 386
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETW-LIYKHTKLVK---KRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 206-294 2.05e-09

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: 53.81  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293324810  206 LFVLSIASLMFWCVVSWMLTqceryaypsisgfqhFADYLWFEIITFFSIGYGDVQVNTYCGRGLAMLTAIVGTLFSSTL 285
Cdd:pfam07885   4 LLVLIFGTVYYLLEEGWEWS---------------FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIF 68


                  ....*....
gi 293324810  286 IALISRKLI 294
Cdd:pfam07885  69 LAVLGRFLT 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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