2ZN9,1Y1X


Conserved Protein Domain Family
EFh_PEF_Group_I

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cd16180: EFh_PEF_Group_I 
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Penta-EF hand, calcium binding motifs, found in Group I PEF proteins
The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.
Statistics
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PSSM-Id: 320055
View PSSM: cd16180
Aligned: 40 rows
Threshold Bit Score: 183.113
Threshold Setting Gi: 391326853
Created: 18-Nov-2014
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:Ca binding site [ion binding site]
Evidence:
  • Comment:Due to the presence of unfavorable residues at the Ca2+-coordinating positions, the EF5 hand of some family members may not be able to bind Ca2+ ion.
  • Structure:2ZN9; Homo sapiens ALG-2 binds three Ca2+ ions through its EF1, EF3 and EF5 hands.
    View structure with Cn3D
  • Structure:1Y1X; Leishmania major Friedlin PDCD6-like protein binds two Ca2+ ions through its EF1 and EF2 hands.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                 # # #      #                                                           
2ZN9_A         8 FLWNVFQRVDKDRSGVISDTELQQALSNGTwtpf--npvTVRSIISMF--DRENKAGVNFSEFTGVWKYITDWQNVFRTY 83
1Y1X_A        28 ELMEWFRAVDTDGSGAISVPELNAALSSAGvpf---slaTTEKLLHMY--DKNHSGEITFDEFKDLHHFILSMREGFRKR 102
gi 685828986  11 AADAFFLILDRNRSGTISMDEFQRGMSNGTterf--dmdTVSLLFAMI--DREGHKKLNMSQFRVVFSFVEAWKRAFHAV 86
gi 75331395  168 NIVACFQAADRDNSGFIDDKELQGALSSYNqsf---sirTVHLLMYLF--TNSNVRKIGPKEFTSLFFSLQNWRSIFERF 242
gi 661889322 125 GVIRTFQMVDRDGSGFIEESELRQALSSGYqrf---smrTIRLLIFLFknPSDSALRIGPKEFSALWSCLGQWRAIFERF 201
gi 193806742  56 EIVRSFESADRNRSGFLEESELRQALSLSGydgi--snrTIRLLLFIYkiPVDSLLRLGPKEYVELWNCLAQWRAIFNRY 133
gi 148908351  87 EIIRSFQMCDQDGSGFIDDKELQRALSSAShsf---slrTVHLLMFEF--TRNNSMKIGPQEFTSLWHSLQAWRAIFERF 161
gi 168010009   8 EVTRLFQMADLDRSGTIDAHELGRVLSTGRvaf---sprTLRLMLHLFgdLKNDSTRIGPVGFAKLWKEIQQWNKKFSEF 84
gi 198418004  11 RLWAKFQACDKDKNGSITVDELRASLLSGCdyqrpfsyeVCRMMMSMY--DKNRNGRLTFDEYVNLDGYIRNWYGYFTRN 88
gi 391326853  28 KIEELFRMMDVAGRGRLDKPELVEGMKYYNgisl--kteTIVLLAGMY--GSEATGGLTLEDFKRLHHTLMTWSSLFRRH 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        # # #      #                                                        # # #       
2ZN9_A        84 DrDNSGMIDKNELKQALSGFGyrlsdqFHDILIRKFDRq--GRGQIAFDDFIQGCIVLQRLTDIFRRYDtDQDGWIQVSY 161
1Y1X_A       103 DsSGDGRLDSNEVRAALLSSGyqvseqTFQALMRKFDRq--RRGSLGFDDYVELSIFVCRVRNVFAFYDrERTGQVTFTF 180
gi 685828986  87 DrDRSGAIEVREFKELLYHMGykisdaSIMLFVNKFARk--RPMTLFFDDFIRSVISLQLLTDAFKVKDiGKQGFIQLSY 164
gi 75331395  243 DkDRSGRIDTNELRDALMSLGfsvspvILDLLVSKFDKsggRNRAIEYDNFIECCLTVKGLTEKFKEKDtALSGSAIFNY 322
gi 661889322 202 DrDRSGKIDATELRDALNGIGytvppsVFQVLISRYEEgngRRVELSFDSFVECGMIVKGLTEKFKEKDpRYTGSATMTY 281
gi 193806742 134 DrDRSGKMNSTQLRDAFYNLGcvlptsVHQLIVSQFDDgtgKTVDLCFDSFLECGMIVKGLTEKFRENDpGYTGYATLSY 213
gi 148908351 162 DrDRSGKIETMELRDALLSLGysisptILQTLVSKYDKt-gQSRGIDYDNFIECSLVVKGLTDKFKEKDkSYVGSASLTY 240
gi 168010009  85 DrDGSGSIDAQELHQALMSFNfnippsVLQMLVSKYDVt-gGSRSIGYDNFVECGFVVKGLTEKFKGQDkSLTGNATFDY 163
gi 198418004  89 DvNRDGRLEHRDFQTAITGLGfrlnqdFFNQIWMDLMKg-aGSNGVVFDQFMHVCIVMQMLTNAWNKRVpNNVTTLEIEH 167
gi 391326853 104 DvDSQEYLLHHSLCSALHELGykldrtTTRSLTRKLGR---QAKYIQEDAFVRICCLLRRLSTAFKKKDlNRQKNIQLSY 180
                        170
                 ....*....|
Feature 1                  
2ZN9_A       162 EQYLSMVFSI 171
1Y1X_A       181 DTFIGGSVSI 190
gi 685828986 165 EEFLLILGQS 174
gi 75331395  323 ENFMLTVLPF 332
gi 661889322 282 DSFMSMIIPF 291
gi 193806742 214 DVFMLMVIPF 223
gi 148908351 241 EEFMQIVLPF 250
gi 168010009 164 TSFMLMVIPF 173
gi 198418004 168 VDFASIIMGI 177
gi 391326853 181 YEVLHMALDS 190

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