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Conserved domains on  [gi|530416474|ref|XP_005258940|]
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intermediate conductance calcium-activated potassium channel protein 4 isoform X2 [Homo sapiens]

Protein Classification

potassium channel family protein( domain architecture ID 10545828)

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
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 241-312 4.95e-33

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: 117.77  E-value: 4.95e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530416474  241 DIQYTKEMKESAARVLQEAWMFYKHTR---RKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMH 312
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKlvkKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 159-227 2.70e-15

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: 69.99  E-value: 2.70e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530416474  159 LGAVRGREAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLE 227
Cdd:pfam07885   9 FGTVYYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 65-158 2.68e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416474  65 VRAGFRGAADLPAALAGIPGPRGSAAVPGHAAASLPGAPRRAPAQRRPAQRflPQHRRSQSSPLPPLVRGQALHEHAPWP 144
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDDP 748

                         90
                 ....*....|....
gi 530416474 145 PAARPHAWPLADHR 158
Cdd:PRK07764 749 PDPAGAPAQPPPPP 762
 
Name Accession Description Interval E-value
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 241-312 4.95e-33

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: 117.77  E-value: 4.95e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530416474  241 DIQYTKEMKESAARVLQEAWMFYKHTR---RKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMH 312
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKlvkKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 241-313 1.51e-32

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: 116.74  E-value: 1.51e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530416474   241 DIQYTKEMKESAARVLQEAWMFYKHT---RRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHM 313
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTklvKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 159-227 2.70e-15

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: 69.99  E-value: 2.70e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530416474  159 LGAVRGREAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLE 227
Cdd:pfam07885   9 FGTVYYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 65-158 2.68e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416474  65 VRAGFRGAADLPAALAGIPGPRGSAAVPGHAAASLPGAPRRAPAQRRPAQRflPQHRRSQSSPLPPLVRGQALHEHAPWP 144
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDDP 748

                         90
                 ....*....|....
gi 530416474 145 PAARPHAWPLADHR 158
Cdd:PRK07764 749 PDPAGAPAQPPPPP 762
 
Name Accession Description Interval E-value
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 241-312 4.95e-33

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: 117.77  E-value: 4.95e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530416474  241 DIQYTKEMKESAARVLQEAWMFYKHTR---RKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMH 312
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKlvkKRDQSRVRKHQRKLLQAIHTFRKVKMKQRKLRDQVNTMVDLSKMQ 75
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 241-313 1.51e-32

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: 116.74  E-value: 1.51e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530416474   241 DIQYTKEMKESAARVLQEAWMFYKHT---RRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHM 313
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTklvKKGDQGRLRKHQRKFLQAIHQFRSVKMKQRKLREQANSLVDLAKTQM 76
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 159-227 2.70e-15

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: 69.99  E-value: 2.70e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530416474  159 LGAVRGREAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLE 227
Cdd:pfam07885   9 FGTVYYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 65-158 2.68e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416474  65 VRAGFRGAADLPAALAGIPGPRGSAAVPGHAAASLPGAPRRAPAQRRPAQRflPQHRRSQSSPLPPLVRGQALHEHAPWP 144
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDDP 748

                         90
                 ....*....|....
gi 530416474 145 PAARPHAWPLADHR 158
Cdd:PRK07764 749 PDPAGAPAQPPPPP 762
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 66-170 3.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416474  66 RAGFRGAADLPAAlagiPGPRGSAAVPghAAASLPGAPRRAPAQRRPAQRFLPQHRRSQS------SPLPPLVRGQALHE 139
Cdd:PRK07764 384 RLGVAGGAGAPAA----AAPSAAAAAP--AAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPapappsPAGNAPAGGAPSPP 457

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530416474 140 HAPWPPaARPHAWPLADHRLGAVRGREAVNA 170
Cdd:PRK07764 458 PAAAPS-AQPAPAPAAAPEPTAAPAPAPPAA 487
 
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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