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Conserved domains on  [gi|1905437361|ref|NP_001373904|]
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small conductance calcium-activated potassium channel protein 1 isoform 2 [Homo sapiens]

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;
93-202 3.51e-63

Calcium-activated SK potassium channel;


:

Pssm-ID: 460958  Cd Length: 111  Bit Score: 202.06  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361  93 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 171
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905437361 172 NGADDWRIAMTCERVFLISLELAVCAIHPVP 202
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 387-464 1.13e-40

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: 141.40  E-value: 1.13e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905437361  387 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 464
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 291-373 6.84e-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: 66.91  E-value: 6.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 291 ISSWIIAAWTvrvcerenMYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVAR 370
Cdd:pfam07885   3 LLLVLIFGTV--------YYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGR 74


                  ...
gi 1905437361 371 KLE 373
Cdd:pfam07885  75 FLT 77
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 420-510 1.32e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 420 QARVRKHQRKFLQAIHQA-----QKLRSVKIEQGKLNDQANTLTD-LAKTQtvmyDLVSELHAQHEELEARLATLESRLD 493
Cdd:COG4942    18 QADAAAEAEAELEQLQQEiaeleKELAALKKEEKALLKQLAALERrIAALA----RRIRALEQELAALEAELAELEKEIA 93

                          90
                  ....*....|....*..
gi 1905437361 494 ALGASLQALPGLIAQAI 510
Cdd:COG4942    94 ELRAELEAQKEELAELL 110
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
93-202 3.51e-63

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 202.06  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361  93 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 171
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905437361 172 NGADDWRIAMTCERVFLISLELAVCAIHPVP 202
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 387-464 1.13e-40

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: 141.40  E-value: 1.13e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905437361  387 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 464
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQ 75
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 387-464 3.69e-40

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: 140.11  E-value: 3.69e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905437361 387 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 464
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHT---FRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 291-373 6.84e-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: 66.91  E-value: 6.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 291 ISSWIIAAWTvrvcerenMYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVAR 370
Cdd:pfam07885   3 LLLVLIFGTV--------YYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGR 74


                  ...
gi 1905437361 371 KLE 373
Cdd:pfam07885  75 FLT 77
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
387-510 9.10e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 387 DTQLTKRVKNAAANVlretwliYKHTRLVKKPDQARvrkHQRKFLQAihQAQKLRSvKIEQ--GKLND--QANTLTDLAK 462
Cdd:COG3206   146 DPELAAAVANALAEA-------YLEQNLELRREEAR---KALEFLEE--QLPELRK-ELEEaeAALEEfrQKNGLVDLSE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1905437361 463 TQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAI 510
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 420-510 1.32e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 420 QARVRKHQRKFLQAIHQA-----QKLRSVKIEQGKLNDQANTLTD-LAKTQtvmyDLVSELHAQHEELEARLATLESRLD 493
Cdd:COG4942    18 QADAAAEAEAELEQLQQEiaeleKELAALKKEEKALLKQLAALERrIAALA----RRIRALEQELAALEAELAELEKEIA 93

                          90
                  ....*....|....*..
gi 1905437361 494 ALGASLQALPGLIAQAI 510
Cdd:COG4942    94 ELRAELEAQKEELAELL 110
 
Name Accession Description Interval E-value
SK_channel pfam03530
Calcium-activated SK potassium channel;
93-202 3.51e-63

Calcium-activated SK potassium channel;


Pssm-ID: 460958  Cd Length: 111  Bit Score: 202.06  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361  93 LGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSW-GVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVD 171
Cdd:pfam03530   1 LRRRKELLERRRRLSDFALVLALFGIVLMVIETELTAlGVYSKGSMYSLALKSLISLSTVLLLGLIVAYHAIEIQLFMVD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1905437361 172 NGADDWRIAMTCERVFLISLELAVCAIHPVP 202
Cdd:pfam03530  81 NGADDWRVAMTSERILQILLELLVCAIHPIP 111
CaMBD smart01053
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 387-464 1.13e-40

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: 141.40  E-value: 1.13e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905437361  387 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 464
Cdd:smart01053   1 DTQLTKRVKNAAANVLRETWLIYKHTKLVKKGDQGRLRKHQRKFLQAIHQ---FRSVKMKQRKLREQANSLVDLAKTQ 75
CaMBD pfam02888
Calmodulin binding domain; Small-conductance Ca2+-activated K+ channels (SK channels) are ...
 387-464 3.69e-40

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: 140.11  E-value: 3.69e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905437361 387 DTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQaqkLRSVKIEQGKLNDQANTLTDLAKTQ 464
Cdd:pfam02888   1 DTQLTKELKNAAANVLRETWLIYKHTKLVKKRDQSRVRKHQRKLLQAIHT---FRKVKMKQRKLRDQVNTMVDLSKMQ 75
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 291-373 6.84e-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: 66.91  E-value: 6.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 291 ISSWIIAAWTvrvcerenMYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVAR 370
Cdd:pfam07885   3 LLLVLIFGTV--------YYLLEEGWEWSFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGR 74


                  ...
gi 1905437361 371 KLE 373
Cdd:pfam07885  75 FLT 77
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
387-510 9.10e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 387 DTQLTKRVKNAAANVlretwliYKHTRLVKKPDQARvrkHQRKFLQAihQAQKLRSvKIEQ--GKLND--QANTLTDLAK 462
Cdd:COG3206   146 DPELAAAVANALAEA-------YLEQNLELRREEAR---KALEFLEE--QLPELRK-ELEEaeAALEEfrQKNGLVDLSE 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1905437361 463 TQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAI 510
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 420-510 1.32e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905437361 420 QARVRKHQRKFLQAIHQA-----QKLRSVKIEQGKLNDQANTLTD-LAKTQtvmyDLVSELHAQHEELEARLATLESRLD 493
Cdd:COG4942    18 QADAAAEAEAELEQLQQEiaeleKELAALKKEEKALLKQLAALERrIAALA----RRIRALEQELAALEAELAELEKEIA 93

                          90
                  ....*....|....*..
gi 1905437361 494 ALGASLQALPGLIAQAI 510
Cdd:COG4942    94 ELRAELEAQKEELAELL 110
 
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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