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InterPro: IPR011992 EF-hand-like domain

Protein matchesHelp
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UniProtKB
Matches:
14393 proteins
AccessionHelp
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IPR011992 EF-hand-like_dom
TypeHelp
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Children IPR003299 Flagellar calcium-binding protein (calflagin)
IPR014741 Adaptor protein Cbl, EF hand-like
IPR015359 Phospholipase C, phosphoinositol-specific, EF-hand-like
IPR019577 SPARC/Testican, calcium-binding domain
Found in IPR001125 Recoverin
IPR001217 STAT transcription factor, core
IPR008080 Parvalbumin
IPR013801 STAT transcription factor, DNA-binding
IPR015754 Calcium binding protein
IPR015756 Guanylate cyclase activating protein 2
IPR015757 Calcineurin B protein
IPR016344 Dystrophin/utrophin
IPR016359 SPARC-like protein 1
IPR017432 Distrobrevin
IPR017433 Dystrophin-related protein 2
IPR020639 Calcyphosin-like
IPR020642 Calcium-dependent protein kinase
Contains IPR001751 S100/CaBP-9k-type, calcium binding
IPR001999 Osteonectin-like, conserved site
IPR002048 Calcium-binding EF-hand
IPR013566 EF hand associated, type-1
IPR013567 EF hand associated, type-2
IPR013623 NADPH oxidase Respiratory burst
IPR013787 S100/CaBP-9k-type, calcium binding, subdomain
IPR014837 EF-hand, Ca insensitive
IPR015153 EF-hand domain, type 1
IPR015154 EF-hand domain, type 2
IPR018247 EF-Hand 1, calcium-binding site
IPR018248 EF-Hand domain
IPR018249 EF-HAND 2
GO Term annotationHelp
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Function GO:0005509 calcium ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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This domain consists of a duplication of two EF-hand units, where each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain [1, 2]. These include: calbindin D9K, S100 proteins such as calcyclin, polcalcin phl p 7 (a calcium-binding pollen allergen), osteonectin, parvalbumin, calmodulin [3] family of proteins (troponin C, caltractin, cdc4p, myosin essential chain, calcineurin, recoverin, neurocalcin), plasmodial-specific CaII-binding protein Cbp40, penta-EF-Hand proteins [4] (sorcin, grancalcin, calpain), as well as multidomain proteins such as phosphoinositide-specific phospholipase C, dystrophin, Cb1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
Structural linksHelp
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PDB - click here
1a03 , 1a29 , 1a2x , 1a4p , 1a75 , 1ahr , 1aj4 , 1ak8 , 1alv , 1alw , 1ap4 , 1aui , 1avs , 1b1g , 1b47 , 1b4c , 1b7t , 1b8c , 1b8l , 1b8r , 1b9a , 1bf5 , 1bg1 , 1bjf , 1blq , 1bmo , 1boc , 1bod , 1br1 , 1br4 , 1bt6 , 1bu3 , 1c07 , 1c7v , 1c7w , 1cb1 , 1cdl , 1cdm , 1cdn , 1cdp , 1cfc , 1cfd , 1cff , 1cfp , 1ckk , 1clb , 1cll , 1clm , 1cm1 , 1cm4 , 1cmf , 1cmg , 1cnp , 1cta , 1ctd , 1ctr , 1d1o , 1deg , 1df0 , 1dfk , 1dfl , 1dgu , 1dgv , 1djg , 1djh , 1dji , 1djw , 1djx , 1djy , 1djz , 1dmo , 1dt7 , 1dtl , 1e8a , 1eg3 , 1eg4 , 1eh2 , 1ej3 , 1el4 , 1exr , 1f4o , 1f4q , 1f54 , 1f55 , 1f70 , 1f71 , 1f8h , 1fbv , 1ff1 , 1fi5 , 1fi6 , 1fpw , 1fw4 , 1g33 , 1g4y , 1g8i , 1ggw , 1ggz , 1gjy , 1gqm , 1h4b , 1h8b , 1hci , 1hqv , 1ht9 , 1ig5 , 1igv , 1ih0 , 1ij5 , 1ij6 , 1iku , 1iq3 , 1iq5 , 1irj , 1iwq , 1j1d , 1j1e , 1j55 , 1j7o , 1j7p , 1j7q , 1j7r , 1jba , 1jc2 , 1jf0 , 1jf2 , 1jfj , 1jfk , 1jsa , 1juo , 1jwd , 1k2h , 1k8u , 1k90 , 1k93 , 1k94 , 1k95 , 1k96 , 1k9k , 1k9p , 1k9u , 1kcy , 1kfu , 1kfx , 1kk7 , 1kk8 , 1kqm , 1kqv , 1ksm , 1kso , 1kwo , 1l2o , 1l7z , 1la0 , 1la3 , 1lin , 1lkj , 1lvc , 1lxf , 1m31 , 1m39 , 1m45 , 1m46 , 1m63 , 1mf8 , 1mho , 1mq1 , 1mr8 , 1mux , 1mwn , 1mxe , 1mxl , 1n0y , 1n2d , 1n65 , 1ncx , 1ncy , 1ncz , 1niw , 1npq , 1nsh , 1nub , 1nwd , 1nx0 , 1nx1 , 1nx2 , 1nx3 , 1nya , 1odb , 1oe9 , 1omd , 1omr , 1omv , 1ooj , 1oqp , 1osa , 1ozo , 1ozs , 1pal , 1pk0 , 1pon , 1prw , 1psb , 1psr , 1pva , 1pvb , 1q80 , 1qas , 1qat , 1qiv , 1qiw , 1qjt , 1qlk , 1qls , 1quu , 1qv0 , 1qv1 , 1qvi , 1qx2 , 1qx5 , 1qx7 , 1qxp , 1r2u , 1r6p , 1rec , 1rfj , 1rjv , 1rk9 , 1rro , 1rtp , 1rwy , 1s1e , 1s26 , 1s36 , 1s3p , 1s5g , 1s6c , 1s6i , 1s6j , 1sbj , 1scm , 1scv , 1sk6 , 1skt , 1sl7 , 1sl8 , 1sl9 , 1smg , 1snl , 1spy , 1sr6 , 1sra , 1sw8 , 1sy9 , 1sym , 1tcf , 1tco , 1tiz , 1tn4 , 1tnp , 1tnq , 1tnw , 1tnx , 1top , 1trf , 1ttx , 1u5i , 1uhh , 1uhi , 1uhj , 1uhk , 1uhn , 1up5 , 1uur , 1uus , 1uwo , 1v1f , 1v1g , 1w7i , 1w7j , 1wdc , 1wlz , 1wrk , 1wrl , 1wrz , 1x02 , 1xa5 , 1xfu , 1xfv , 1xfw , 1xfx , 1xfy , 1xfz , 1xk4 , 1xo5 , 1xvj , 1xyd , 1y0v , 1y1a , 1y1x , 1y6w , 1yr5 , 1yrt , 1yru , 1ytz , 1yur , 1yus , 1yut , 1yuu , 1yv0 , 1yvl , 1zac , 1zfs , 1zot , 1zuz , 2bbm , 2bbn , 2bca , 2bcb , 2bcx , 2be6 , 2bec , 2bkh , 2bki , 2bl0 , 2cbl , 2cnp , 2col , 2ct9 , 2ctn , 2d8n , 2ec6 , 2ehb , 2ekv , 2ekw , 2f3y , 2f3z , 2f8p , 2fce , 2fju , 2fot , 2ggm , 2h61 , 2het , 2hf5 , 2hps , 2hq8 , 2hqw , 2i2r , 2i94 , 2isd , 2ix7 , 2jpt , 2jt0 , 2jt3 , 2jt8 , 2jtt , 2jtz , 2ju0 , 2jul , 2jww , 2jxc , 2k0e , 2k0f , 2k2f , 2k3s , 2mys , 2nln , 2nz0 , 2o5g , 2o60 , 2obh , 2opo , 2os8 , 2otg , 2ovk , 2oy6 , 2p6b , 2pal , 2pas , 2pq3 , 2pru , 2psr , 2pvb , 2q91 , 2r28 , 2rgi , 2sas , 2scp , 2tn4 , 2v01 , 2v02 , 2vas , 2vay , 2vb6 , 2zfd , 2zkm , 3b32 , 3bum , 3bun , 3buo , 3buw , 3bux , 3bxk , 3bxl , 3c1v , 3cga , 3cln , 3cr2 , 3cr4 , 3cr5 , 3ctn , 3icb , 3pal , 3pat , 3psr , 4cln , 4cpv , 4icb , 4pal , 4tnc , 5cpv , 5pal , 5tnc

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR011992 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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O14815 Calpain-9

O16305 Calmodulin

O70200 Allograft inflammatory factor 1

P06704 Cell division control protein 31

P13395 Spectrin alpha chain

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011992 EF-hand-like domain
IPR002048 Calcium-binding EF-hand
IPR001452 Src homology-3 domain
IPR001300 Peptidase C2, calpain
IPR018159 Spectrin/alpha-actinin
IPR018247 EF-Hand 1, calcium-binding site
IPR018249 EF-HAND 2
IPR018248 EF-Hand domain
IPR000169 Peptidase, cysteine peptidase active site
IPR013315 Spectrin alpha chain, SH3 domain
IPR014837 EF-hand, Ca insensitive
IPR020473 Src homology-3, region
IPR002017 Spectrin repeat
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
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1. Ikura M, Osawa M, Ames JB.
The role of calcium-binding proteins in the control of transcription: structure to function.
Bioessays 24 625-36 2002 [PubMed: 12111723]
http://dx.doi.org/10.1002/bies.10105
2. Lewit-Bentley A, Rety S.
EF-hand calcium-binding proteins.
Curr. Opin. Struct. Biol. 10 637-43 2000 [PubMed: 11114499]
http://dx.doi.org/10.1016/S0959-440X(00)00142-1
3. Vetter SW, Leclerc E.
Novel aspects of calmodulin target recognition and activation.
Eur. J. Biochem. 270 404-14 2003 [PubMed: 12542690]
http://dx.doi.org/10.1046/j.1432-1033.2003.03414.x
4. Maki M, Kitaura Y, Satoh H, Ohkouchi S, Shibata H.
Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins.
Biochim. Biophys. Acta 1600 51-60 2002 [PubMed: 12445459]
http://dx.doi.org/10.1016/S1570-9639(02)00444-2

Additional ReadingHelp
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Hicks SN, Jezyk MR, Gershburg S, Seifert JP, Harden TK, Sondek J.
General and versatile autoinhibition of PLC isozymes.
Mol. Cell 31 2008 383-94 [PubMed: 18691970]
http://dx.doi.org/10.1016/j.molcel.2008.06.018
Zhukov I, Ejchart A, Bierzynski A.
Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol.
Biochemistry 47 2008 640-50 [PubMed: 18088104]
http://dx.doi.org/10.1021/bi701762v
Stepanyuk GA, Liu ZJ, Markova SS, Frank LA, Lee J, Vysotski ES, Wang BC.
Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 A: why it is not a calcium-regulated photoprotein.
Photochem. Photobiol. Sci. 7 2008 442-7 [PubMed: 18385886]
http://dx.doi.org/10.1039/b716535h
Lusin JD, Vanarotti M, Li C, Valiveti A, Ames JB.
NMR structure of DREAM: Implications for Ca(2+)-dependent DNA binding and protein dimerization.
Biochemistry 47 2008 2252-64 [PubMed: 18201103]
http://dx.doi.org/10.1021/bi7017267
Halling DB, Georgiou DK, Black DJ, Yang G, Fallon JL, Quiocho FA, Pedersen SE, Hamilton SL.
Determinants in CaV1 channels that regulate the Ca2+ sensitivity of bound calmodulin.
J. Biol. Chem. 284 2009 20041-51 [PubMed: 19473981]
http://dx.doi.org/10.1074/jbc.M109.013326
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InterPro 23.1