EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 5453740   32 EFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMNEA 76
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREV 45

EF-hand domain;

                          10        20        30
                  ....*....|....*....|....*....|
gi 5453740     32 EFKEAFNMIDQNRDGFIDKEDLHDMLASLG 61
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30

centrin; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453740    25 FDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMM----NEAPGPINFTMFLTMFGEKLNGTDPED 100
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPRE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453740   101 VIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILK 163
Cdd:PTZ00183  91 EILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMK 153

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453740   31 QEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMmneaPGPINFTMFLTMFGEKLNGTDP 98
Cdd:cd22949   3 EKFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66

EF-hand domain;

                          10        20        30
                  ....*....|....*....|....*....|
gi 5453740     32 EFKEAFNMIDQNRDGFIDKEDLHDMLASLG 61
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30

EF-hand domain; This domain is found predominantly in DJ binding proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5453740    102 IRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEF 158
Cdd:pfam08976  22 ITQEFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDF 78

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453740   32 EFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMN----EAPGPINFTMFLTMFGEKLNgtdpedvIRNAFA 107
Cdd:cd16185   1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRmfdrDGNGTIDFEEFAALHQFLSN-------MQNGFE 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5453740  108 CFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFN---YIEFT 159
Cdd:cd16185  74 QRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGfddYIELC 128

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453740   30 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMN----EAPGPINFTMF------LTMFgeklngTDpe 99
Cdd:cd16184  66 IQQWKQVFQQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSkydpRARRSLTLDQFiqvcvqLQSL------TD-- 137

                        90       100       110
                ....*....|....*....|....*....|...
gi 5453740  100 dvirnAFACFDEEATGTIQ---EDYLRELLTTM 129
Cdd:cd16184 138 -----AFRQRDTQMTGTITisyEDFLTMALLNK 165

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453740   75 EAPGPINFTMFLTMFGEKlngTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTM---GDRFTDEEVDELYREAPIDKKG 151
Cdd:cd16251  12 RAHGSFNYKKFFEHVGLK---QKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLAAGDTDGDG 88

                        90
                ....*....|..
gi 5453740  152 NFNYIEFTRILK 163
Cdd:cd16251  89 KIGVEEFATLVA 100

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453740   30 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLDAMMN----EAPGPINFTMF--LTMFGEKlngtdpedvIR 103
Cdd:cd16185  65 LSNMQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRkfdpDRGGSLGFDDYieLCIFLAS---------AR 135

                        90
                ....*....|....
gi 5453740  104 NAFACFDEEATGTI 117
Cdd:cd16185 136 NLFQAFDRQRTGRV 149

EF hand;

                          10        20
                  ....*....|....*....|....*
gi 5453740     33 FKEAFNMIDQNRDGFIDKEDLHDML 57
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25