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Conserved domains on  [gi|4506459|ref|NP_002894|]
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recoverin [Homo sapiens]

Protein Classification

EFh domain-containing protein( domain architecture ID 11473828)

EFh domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-127 6.45e-13

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.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 61.02  E-value: 6.45e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506459   65 YAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVM 127
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-175 3.01e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   42 GRITQQQFQSIYAkffpdtdpkAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNE 121
Cdd:COG5126  20 GVLERDDFEALFR---------RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506459  122 vleivmaifkmitpedVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEG 175
Cdd:COG5126  91 ----------------FRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-127 6.45e-13

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.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 61.02  E-value: 6.45e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506459   65 YAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVM 127
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-175 3.01e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   42 GRITQQQFQSIYAkffpdtdpkAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNE 121
Cdd:COG5126  20 GVLERDDFEALFR---------RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506459  122 vleivmaifkmitpedVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEG 175
Cdd:COG5126  91 ----------------FRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-130 2.29e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 2.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   41 TGRITQQQFQSIYAKFFPDTDPKAYAQhVFRSFDSNLDGTLDFKEYviALHMTTAGKTNQKLEWAFSLYDVDGNGTISKN 120
Cdd:COG5126  47 DGRISREEFVAGMESLFEATVEPFARA-AFDLLDTDGDGKISADEF--RRLLTALGVSEEEADELFARLDTDGDGKISFE 123

                        90
                ....*....|
gi 4506459  121 EVLEIVMAIF 130
Cdd:COG5126 124 EFVAAVRDYY 133
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 101-175 1.11e-07

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.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 47.16  E-value: 1.11e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506459  101 KLEWAFSLYDVDGNGTISKNEVLEIVMAIfkmitpedvkllpdDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEG 175
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL--------------GEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
100-174 1.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 1.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506459    100 QKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLlpddentpekraEKIWKYFGKNDDDKLTEKEFIE 174
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEV------------EELFKEFDLDKDGRISFEEFLE 64
EF-hand_7 pfam13499
EF-hand domain pair;
63-127 1.31e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 1.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506459     63 KAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGK--TNQKLEWAFSLYDVDGNGTISKNEVLEIVM 127
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 101-129 1.72e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.36  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 4506459     101 KLEWAFSLYDVDGNGTISKNEVLEIVMAI 129
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00184 PTZ00184
calmodulin; Provisional
 67-138 1.96e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.05  E-value: 1.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506459    67 QHVFRSFDSNLDGTLDFKEYVIAL-HMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDV 138
Cdd:PTZ00184  50 QDMINEVDADGNGTIDFPEFLTLMaRKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV 122
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-127 6.45e-13

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.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 61.02  E-value: 6.45e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506459   65 YAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVM 127
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-175 3.01e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   42 GRITQQQFQSIYAkffpdtdpkAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNE 121
Cdd:COG5126  20 GVLERDDFEALFR---------RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506459  122 vleivmaifkmitpedVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEG 175
Cdd:COG5126  91 ----------------FRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-130 2.29e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 2.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   41 TGRITQQQFQSIYAKFFPDTDPKAYAQhVFRSFDSNLDGTLDFKEYviALHMTTAGKTNQKLEWAFSLYDVDGNGTISKN 120
Cdd:COG5126  47 DGRISREEFVAGMESLFEATVEPFARA-AFDLLDTDGDGKISADEF--RRLLTALGVSEEEADELFARLDTDGDGKISFE 123

                        90
                ....*....|
gi 4506459  121 EVLEIVMAIF 130
Cdd:COG5126 124 EFVAAVRDYY 133
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 27-124 5.10e-08

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).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 50.29  E-value: 5.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   27 ELCSWYQSFLKDCpTGRITQQQFQSIYAK----FFPDTdpkayAQHVFRSFDSNLDGTLDFKEYViALHmttagKTNQKL 102
Cdd:cd16185   1 ELRQWFRAVDRDR-SGSIDVNELQKALAGggllFSLAT-----AEKLIRMFDRDGNGTIDFEEFA-ALH-----QFLSNM 68

                        90       100
                ....*....|....*....|..
gi 4506459  103 EWAFSLYDVDGNGTISKNEVLE 124
Cdd:cd16185  69 QNGFEQRDTSRSGRLDANEVHE 90
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 101-175 1.11e-07

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.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 47.16  E-value: 1.11e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506459  101 KLEWAFSLYDVDGNGTISKNEVLEIVMAIfkmitpedvkllpdDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEG 175
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL--------------GEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
100-174 1.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 1.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506459    100 QKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLlpddentpekraEKIWKYFGKNDDDKLTEKEFIE 174
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEV------------EELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
100-172 2.01e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459  100 QKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKM------------ITPEDVK--LLPDDENTPEKRAEKIWKYFGKNDDD 165
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATlfseadtdgdgrISREEFVagMESLFEATVEPFARAAFDLLDTDGDG 84


                ....*..
gi 4506459  166 KLTEKEF 172
Cdd:COG5126  85 KISADEF 91
EF-hand_7 pfam13499
EF-hand domain pair;
63-127 1.31e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 1.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506459     63 KAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGK--TNQKLEWAFSLYDVDGNGTISKNEVLEIVM 127
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 27-121 1.39e-04

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+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 40.59  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   27 ELCSWYQSFLKDCpTGRITQQQFQSI-----YAKFFPDTdpkayAQHVFRSFDSNLDGTLDFKEYViALHmttagKTNQK 101
Cdd:cd16180   1 ELRRIFQAVDRDR-SGRISAKELQRAlsngdWTPFSIET-----VRLMINMFDRDRSGTINFDEFV-GLW-----KYIQD 68

                        90       100
                ....*....|....*....|
gi 4506459  102 LEWAFSLYDVDGNGTISKNE 121
Cdd:cd16180  69 WRRLFRRFDRDRSGSIDFNE 88
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 101-129 1.72e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.36  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 4506459     101 KLEWAFSLYDVDGNGTISKNEVLEIVMAI 129
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 65-171 4.40e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 40.03  E-value: 4.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   65 YAQHVFRSFDSNLDGTLDFKE--------------YVIALHMTTagkTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIF 130
Cdd:cd15902 135 YTKLILKEFDANKDGKLELDEmakllpvqenfllkFQILGAMDL---TKEDFEKVFEHYDKDNNGVIEGNELDALLKDLL 211

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4506459  131 KMITPEdvkllpDDENTPEKRAEKIWKYFGKNDDDKLTEKE 171
Cdd:cd15902 212 EKNKAD------IDKPDLENFRDAILRACDKNKDGKIQKTE 246
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 5-118 6.25e-04

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+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.66  E-value: 6.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459    5 KSGALSKEileELQL------NTKFSEEELCSWYQSFLKDcPTGRITQQQFQSIYaKFFpdtdpkAYAQHVFRSFDSNLD 78
Cdd:cd16180  13 RSGRISAK---ELQRalsngdWTPFSIETVRLMINMFDRD-RSGTINFDEFVGLW-KYI------QDWRRLFRRFDRDRS 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4506459   79 GTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTIS 118
Cdd:cd16180  82 GSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSIS 121
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 54-173 1.45e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 38.58  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506459   54 AKFFPDTDP---KAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVleIVMAIF 130
Cdd:cd15899  22 AEEFDQLTPeesKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEY--KNDTYG 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4506459  131 KMITPEDVKLLPDDENTPEK----RAEKIWKYFGKNDDDKLTEKEFI 173
Cdd:cd15899 100 SVGDDEENVADNIKEDEEYKklllKDKKRFEAADQDGDLILTLEEFL 146
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 101-129 1.59e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.68  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....*....
gi 4506459    101 KLEWAFSLYDVDGNGTISKNEVLEIVMAI 129
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
PTZ00184 PTZ00184
calmodulin; Provisional
 67-138 1.96e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.05  E-value: 1.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506459    67 QHVFRSFDSNLDGTLDFKEYVIAL-HMTTAGKTNQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDV 138
Cdd:PTZ00184  50 QDMINEVDADGNGTIDFPEFLTLMaRKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV 122
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 99-159 5.52e-03

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.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 34.25  E-value: 5.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506459   99 NQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMITPEDVKLLPDDENtpekraekiWKYF 159
Cdd:cd22949   2 EEKFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDALPASMN---------WDQF 53
EF-hand_6 pfam13405
EF-hand domain;
101-129 5.64e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.30  E-value: 5.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 4506459    101 KLEWAFSLYDVDGNGTISKNEVLEIVMAI 129
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EF-hand_8 pfam13833
EF-hand domain pair;
40-90 9.38e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 33.44  E-value: 9.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4506459     40 PTGRITQQQFQSIYAKFFPDTDPKAYAQHVFRSFDSNLDGTLDFKEYVIAL 90
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
 
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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