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Conserved domains on  [gi|21450721|ref|NP_659447|]
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enkurin isoform 1 [Homo sapiens]

Protein Classification

enkurin domain-containing protein( domain architecture ID 10620564)

enkurin domain-containing protein similar to human enkurin, an adapter that functions to localize a calcium-sensitive signal transduction machinery in sperm to a calcium-permeable ion channel

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Enkurin pfam13864
Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high ...
 152-246 4.40e-34

Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high levels in the testis and vomeronasal organ and at lower levels in certain other tissues. Enkurin is a scaffold protein that binds PI3 kinase to sperm transient receptor potential (canonical) (TRPC) channels. The mammalian transient receptor potential (canonical) channels are the primary candidates for the Ca(2+) entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Calmodulin binds to the C-terminus of all TRPC channels, and dissociation of calmodulin from TRPC4 results in profound activation of the channel.


:

Pssm-ID: 464004 [Multi-domain]  Cd Length: 92  Bit Score: 118.44  E-value: 4.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450721   152 GVTPEYICKRNEEIKKAQEDYDRYIQENlkkAAMKRLSDEEREAVLQGLKKNWEEVHKEFQSLSVFIDSIPKKIRKQRLE 231
Cdd:pfam13864   1 GKVPKYLQKRKEELEKEEEEYEEYVREE---EERRLLSEEERQELLDGLKKNWDELNKEYQKLPLKIDTLSKKRRKEELE 77

                          90
                  ....*....|....*
gi 21450721   232 EEMKQLEHDIGIIEK 246
Cdd:pfam13864  78 KELAQLEKDIKKLER 92
 
Name Accession Description Interval E-value
Enkurin pfam13864
Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high ...
 152-246 4.40e-34

Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high levels in the testis and vomeronasal organ and at lower levels in certain other tissues. Enkurin is a scaffold protein that binds PI3 kinase to sperm transient receptor potential (canonical) (TRPC) channels. The mammalian transient receptor potential (canonical) channels are the primary candidates for the Ca(2+) entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Calmodulin binds to the C-terminus of all TRPC channels, and dissociation of calmodulin from TRPC4 results in profound activation of the channel.


Pssm-ID: 464004 [Multi-domain]  Cd Length: 92  Bit Score: 118.44  E-value: 4.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450721   152 GVTPEYICKRNEEIKKAQEDYDRYIQENlkkAAMKRLSDEEREAVLQGLKKNWEEVHKEFQSLSVFIDSIPKKIRKQRLE 231
Cdd:pfam13864   1 GKVPKYLQKRKEELEKEEEEYEEYVREE---EERRLLSEEERQELLDGLKKNWDELNKEYQKLPLKIDTLSKKRRKEELE 77

                          90
                  ....*....|....*
gi 21450721   232 EEMKQLEHDIGIIEK 246
Cdd:pfam13864  78 KELAQLEKDIKKLER 92
 
Name Accession Description Interval E-value
Enkurin pfam13864
Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high ...
 152-246 4.40e-34

Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high levels in the testis and vomeronasal organ and at lower levels in certain other tissues. Enkurin is a scaffold protein that binds PI3 kinase to sperm transient receptor potential (canonical) (TRPC) channels. The mammalian transient receptor potential (canonical) channels are the primary candidates for the Ca(2+) entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Calmodulin binds to the C-terminus of all TRPC channels, and dissociation of calmodulin from TRPC4 results in profound activation of the channel.


Pssm-ID: 464004 [Multi-domain]  Cd Length: 92  Bit Score: 118.44  E-value: 4.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450721   152 GVTPEYICKRNEEIKKAQEDYDRYIQENlkkAAMKRLSDEEREAVLQGLKKNWEEVHKEFQSLSVFIDSIPKKIRKQRLE 231
Cdd:pfam13864   1 GKVPKYLQKRKEELEKEEEEYEEYVREE---EERRLLSEEERQELLDGLKKNWDELNKEYQKLPLKIDTLSKKRRKEELE 77

                          90
                  ....*....|....*
gi 21450721   232 EEMKQLEHDIGIIEK 246
Cdd:pfam13864  78 KELAQLEKDIKKLER 92
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 132-240 9.98e-04

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.37  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450721   132 DKHDLEP-SGLVPKYINkkdygV--TPEYICKRNE----EIKKAQEDYDRYIQENLKKAAMKRLSDEEreavLQGLKKNW 204
Cdd:pfam09744  17 DRYGEDVvKGLMPKVVN-----VleLLESLASRNQehnvELEELREDNEQLETQYEREKALRKRAEEE----LEEIEDQW 87

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 21450721   205 EEVHKEFQSlsvfidsipkkiRKQRLEEEMKQLEHD 240
Cdd:pfam09744  88 EQETKDLLS------------QVESLEEENRRLEAD 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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