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Conserved domains on  [gi|512949370|ref|XP_004837133|]
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EF-hand calcium-binding domain-containing protein 11 isoform X2 [Heterocephalus glaber]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-158 1.73e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.96  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  21 RKWVEVFKACDEDNKGYLSREDFKVAVVMLFGYKPSKIEADSvmssinpntSGIVLGEFLNIIRKKKEAQLYRNEIRHIF 100
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG---------DGRISREEFVAGMESLFEATVEPFARAAF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 512949370 101 TAFDVHYRGYLTLEDFKKAFSqvAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMKH 158
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-158 1.73e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.96  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  21 RKWVEVFKACDEDNKGYLSREDFKVAVVMLFGYKPSKIEADSvmssinpntSGIVLGEFLNIIRKKKEAQLYRNEIRHIF 100
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG---------DGRISREEFVAGMESLFEATVEPFARAAF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 512949370 101 TAFDVHYRGYLTLEDFKKAFSqvAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMKH 158
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 25-157 5.03e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 60.09  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  25 EVFKACDEDNKGYLSREDFKVAVVMLfGYKPSKIEADSVMSSINPNTSGIV-LGEFLNIIRKKKEAQLYRNEIRHIFTAF 103
Cdd:PTZ00183  21 EAFDLFDTDGSGTIDPKELKVAMRSL-GFEPKKEEIKQMIADVDKDGSGKIdFEEFLDIMTKKLGERDPREEILKAFRLF 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 512949370 104 DVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:PTZ00183 100 DDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMK 153
EF-hand_7 pfam13499
EF-hand domain pair;
93-157 4.72e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.72e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512949370   93 RNEIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERT--VLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDeeVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 95-157 1.17e-08

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: 49.08  E-value: 1.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512949370  95 EIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 132-157 4.46e-03

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: 33.12  E-value: 4.46e-03
                           10        20
                   ....*....|....*....|....*.
gi 512949370   132 VLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-158 1.73e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.96  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  21 RKWVEVFKACDEDNKGYLSREDFKVAVVMLFGYKPSKIEADSvmssinpntSGIVLGEFLNIIRKKKEAQLYRNEIRHIF 100
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDG---------DGRISREEFVAGMESLFEATVEPFARAAF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 512949370 101 TAFDVHYRGYLTLEDFKKAFSqvAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMKH 158
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 25-157 5.03e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 60.09  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  25 EVFKACDEDNKGYLSREDFKVAVVMLfGYKPSKIEADSVMSSINPNTSGIV-LGEFLNIIRKKKEAQLYRNEIRHIFTAF 103
Cdd:PTZ00183  21 EAFDLFDTDGSGTIDPKELKVAMRSL-GFEPKKEEIKQMIADVDKDGSGKIdFEEFLDIMTKKLGERDPREEILKAFRLF 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 512949370 104 DVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:PTZ00183 100 DDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMK 153
PTZ00184 PTZ00184
calmodulin; Provisional
 25-152 3.76e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 52.46  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  25 EVFKACDEDNKGYLSREDFKVaVVMLFGYKPSKIEADSVMSSINPNTSG-IVLGEFLNIIRKKKEAQLYRNEIRHIFTAF 103
Cdd:PTZ00184  15 EAFSLFDKDGDGTITTKELGT-VMRSLGQNPTEAELQDMINEVDADGNGtIDFPEFLTLMARKMKDTDSEEEIKEAFKVF 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 512949370 104 DVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDF 152
Cdd:PTZ00184  94 DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
EF-hand_7 pfam13499
EF-hand domain pair;
93-157 4.72e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.72e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512949370   93 RNEIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERT--VLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDeeVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 95-157 1.17e-08

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: 49.08  E-value: 1.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512949370  95 EIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 24-156 1.15e-06

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: 45.98  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  24 VEVFKACDEDNKGYLSREDFKVAVVmLFGYKPSKIEADSVMSSI--NPNTSGIVLGEFLNIIRkkkeaqlYRNEIRHIFT 101
Cdd:cd16180    3 RRIFQAVDRDRSGRISAKELQRALS-NGDWTPFSIETVRLMINMfdRDRSGTINFDEFVGLWK-------YIQDWRRLFR 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 512949370 102 AFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAM 156
Cdd:cd16180   75 RFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEAC 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 25-84 4.93e-05

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: 39.45  E-value: 4.93e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512949370  25 EVFKACDEDNKGYLSREDFKvAVVMLFGYKPSKIEADSVMSSINPNTSGIV-LGEFLNIIR 84
Cdd:cd00051    4 EAFRLFDKDGDGTISADELK-AALKSLGEGLSEEEIDEMIREVDKDGDGKIdFEEFLELMA 63
EF-hand_8 pfam13833
EF-hand domain pair;
108-158 9.31e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.45  E-value: 9.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 512949370  108 RGYLTLEDFKKAFSQV-APRLPERTVLEVFREVDRDSDGHVSFRDFEYAMKH 158
Cdd:pfam13833   2 KGVITREELKRALALLgLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 21-152 2.73e-04

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: 39.12  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  21 RKWvevFKACDEDNKGYLSREDFKVAVV---MLFGYKpskiEADSVMSSINPNTSGIV-LGEFlniirkkkeAQLYR--N 94
Cdd:cd16185    3 RQW---FRAVDRDRSGSIDVNELQKALAgggLLFSLA----TAEKLIRMFDRDGNGTIdFEEF---------AALHQflS 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 512949370  95 EIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDF 152
Cdd:cd16185   67 NMQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
EF-hand_7 pfam13499
EF-hand domain pair;
25-84 2.93e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 2.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512949370   25 EVFKACDEDNKGYLSREDFKVAVVMLF-GYKPSKIEADSVMSSINPNTSGIV-LGEFLNIIR 84
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRIsFEEFLELYS 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 96-157 3.56e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 38.42  E-value: 3.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512949370  96 IRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:cd15898    2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYK 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
91-157 7.13e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  91 LYRNEIRHIFTAFDVHYRGYLTLEDFKKAFSQ----------------------------VAPRLPERTVLEVFREVDRD 142
Cdd:COG5126    2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRlwatlfseadtdgdgrisreefvagmesLFEATVEPFARAAFDLLDTD 81

                         90
                 ....*....|....*
gi 512949370 143 SDGHVSFRDFEYAMK 157
Cdd:COG5126   82 GDGKISADEFRRLLT 96
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 132-158 1.42e-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: 1.42e-03
                          10        20
                  ....*....|....*....|....*..
gi 512949370  132 VLEVFREVDRDSDGHVSFRDFEYAMKH 158
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 25-116 1.49e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 36.88  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  25 EVFKACDEDNKGYLSREDFkvavVMLFGYKPSKIEADSVMSSI-NPNTSGIVLGEFLNIIRKKKEAQLYRNEIRHIFTAF 103
Cdd:cd15898   40 KLFKEVDTNGDGTLTFDEF----EELYKSLTERPELEPIFKKYaGTNRDYMTLEEFIRFLREEQGENVSEEECEELIEKY 115

                         90
                 ....*....|....
gi 512949370 104 DVH-YRGYLTLEDF 116
Cdd:cd15898  116 EPErENRQLSFEGF 129
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 25-116 4.43e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 35.69  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  25 EVFKACDEDNKGYLSREDFKvAVVMLFGYKPskiEADSVMSSI-NPNTSGIVLGEFLNIIRKKKEAQLYRNEIRHIFTAF 103
Cdd:cd16207   42 ELFDKADTDKKGYLNFEEFQ-EFVKLLKRRK---DIKAIFKQLtKPGSDGLTLEEFLKFLRDVQKEDVDRETWEKIFEKF 117

                         90
                 ....*....|....*..
gi 512949370 104 ----DVHYRGYLTLEDF 116
Cdd:cd16207  118 arriDDSDSLTMTLEGF 134
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 132-157 4.46e-03

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: 33.12  E-value: 4.46e-03
                           10        20
                   ....*....|....*....|....*.
gi 512949370   132 VLEVFREVDRDSDGHVSFRDFEYAMK 157
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
PTZ00183 PTZ00183
centrin; Provisional
 93-152 4.77e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 35.82  E-value: 4.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 512949370  93 RNEIRHIFTAFDVHYRGYLTLEDFKKAFSQVAPRLPERTVLEVFREVDRDSDGHVSFRDF 152
Cdd:PTZ00183  16 KKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEF 75
 
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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