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Conserved domains on  [gi|1063723298|ref|NP_001329535|]
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calcineurin B-like protein 1 [Arabidopsis thaliana]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 13310055)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to Oryza sativa calcium-binding protein CML23 that is a potential calcium sensor

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 ...
 108-177 1.05e-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: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298 108 KIDFTFRLYDMDCTGYIERQEVKQMLIALLCESEMKladetieiILDKTFEDADVNQDGKIDKLEWSDFV 177
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE--------EIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 super family cl33171
centrin; Provisional
 31-181 2.56e-05

centrin; Provisional


The actual alignment was detected with superfamily member PTZ00183:

Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  31 EVEALFELFKSISSsvvddGLINKEEFQLAL----FKSRKREnifanrIFDMF-DVKR--KGVIDFGDFVRSLNVFHPNA 103
Cdd:PTZ00183   18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEPKKEE------IKQMIaDVDKdgSGKIDFEEFLDIMTKKLGER 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723298 104 SLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALlceSEMKLADETIEIIldktfEDADVNQDGKIDKLEWSDFVNKNP 181
Cdd:PTZ00183   87 DPREEILKAFRLFDDDKTGKISLKNLKRVAKEL---GETITDEELQEMI-----DEADRNGDGEISEEEFYRIMKKTN 156
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 108-177 1.05e-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: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298 108 KIDFTFRLYDMDCTGYIERQEVKQMLIALLCESEMKladetieiILDKTFEDADVNQDGKIDKLEWSDFV 177
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE--------EIDEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-179 4.18e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  49 DGLINKEEFQLALfksrkreNIFANRIFDMFDVKRKGVIDFGDFVRSLnVFHPNASLEDKIDFTFRLYDMDCTGYIERQE 128
Cdd:COG5126    19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063723298 129 VKQMLIALlcesemkladETIEIILDKTFEDADVNQDGKIDKLEWSDFVNK 179
Cdd:COG5126    91 FRRLLTAL----------GVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 31-181 2.56e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  31 EVEALFELFKSISSsvvddGLINKEEFQLAL----FKSRKREnifanrIFDMF-DVKR--KGVIDFGDFVRSLNVFHPNA 103
Cdd:PTZ00183   18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEPKKEE------IKQMIaDVDKdgSGKIDFEEFLDIMTKKLGER 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723298 104 SLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALlceSEMKLADETIEIIldktfEDADVNQDGKIDKLEWSDFVNKNP 181
Cdd:PTZ00183   87 DPREEILKAFRLFDDDKTGKISLKNLKRVAKEL---GETITDEELQEMI-----DEADRNGDGEISEEEFYRIMKKTN 156
PTZ00184 PTZ00184
calmodulin; Provisional
 80-177 4.21e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.06  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  80 DVKRKGVIDFGDFVRSLNVFHPNASLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALlcesEMKLADETIeiilDKTFED 159
Cdd:PTZ00184   57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNL----GEKLTDEEV----DEMIRE 128

                          90
                  ....*....|....*...
gi 1063723298 160 ADVNQDGKIDkleWSDFV 177
Cdd:PTZ00184  129 ADVDGDGQIN---YEEFV 143
EF-hand_7 pfam13499
EF-hand domain pair;
106-172 5.34e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063723298 106 EDKIDFTFRLYDMDCTGYIERQEVKQMLIALlcESEMKLADETIEIIldktFEDADVNQDGKIDKLE 172
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEPLSDEEVEEL----FKEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
74-133 1.51e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063723298  74 RIFDMFDVKRKGVIDFGDFVRSLNVFHPNASL-EDKIDFTFRLYDMDCTGYIERQEVKQML 133
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 50-135 8.42e-03

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: 35.65  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  50 GLINKEEFQLALFKSRKRENI-FANRIFDMFDVKRKGVIDFGDFVRsLNVFHPNASLedkidfTFRLYDMDCTGYIERQE 128
Cdd:cd16185    15 GSIDVNELQKALAGGGLLFSLaTAEKLIRMFDRDGNGTIDFEEFAA-LHQFLSNMQN------GFEQRDTSRSGRLDANE 87


                  ....*..
gi 1063723298 129 VKQMLIA 135
Cdd:cd16185    88 VHEALAA 94
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 108-177 1.05e-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: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298 108 KIDFTFRLYDMDCTGYIERQEVKQMLIALLCESEMKladetieiILDKTFEDADVNQDGKIDKLEWSDFV 177
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE--------EIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 80-179 1.09e-07

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 48.30  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  80 DVKRKGVIDFGDFVRSLNVFHPNASLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALLCESE-MKLADETIEIILdktfE 158
Cdd:cd16252    10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPvAPLSDEEAEAMI----Q 85

                          90       100
                  ....*....|....*....|.
gi 1063723298 159 DADVNQDGKIDKLEWSDFVNK 179
Cdd:cd16252    86 AADTDGDGRIDFQEFSDMVKK 106
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-179 4.18e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  49 DGLINKEEFQLALfksrkreNIFANRIFDMFDVKRKGVIDFGDFVRSLnVFHPNASLEDKIDFTFRLYDMDCTGYIERQE 128
Cdd:COG5126    19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063723298 129 VKQMLIALlcesemkladETIEIILDKTFEDADVNQDGKIDKLEWSDFVNK 179
Cdd:COG5126    91 FRRLLTAL----------GVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 31-181 2.56e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  31 EVEALFELFKSISSsvvddGLINKEEFQLAL----FKSRKREnifanrIFDMF-DVKR--KGVIDFGDFVRSLNVFHPNA 103
Cdd:PTZ00183   18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEPKKEE------IKQMIaDVDKdgSGKIDFEEFLDIMTKKLGER 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723298 104 SLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALlceSEMKLADETIEIIldktfEDADVNQDGKIDKLEWSDFVNKNP 181
Cdd:PTZ00183   87 DPREEILKAFRLFDDDKTGKISLKNLKRVAKEL---GETITDEELQEMI-----DEADRNGDGEISEEEFYRIMKKTN 156
PTZ00184 PTZ00184
calmodulin; Provisional
 80-177 4.21e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.06  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  80 DVKRKGVIDFGDFVRSLNVFHPNASLEDKIDFTFRLYDMDCTGYIERQEVKQMLIALlcesEMKLADETIeiilDKTFED 159
Cdd:PTZ00184   57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNL----GEKLTDEEV----DEMIRE 128

                          90
                  ....*....|....*...
gi 1063723298 160 ADVNQDGKIDkleWSDFV 177
Cdd:PTZ00184  129 ADVDGDGQIN---YEEFV 143
EF-hand_7 pfam13499
EF-hand domain pair;
106-172 5.34e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063723298 106 EDKIDFTFRLYDMDCTGYIERQEVKQMLIALlcESEMKLADETIEIIldktFEDADVNQDGKIDKLE 172
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEPLSDEEVEEL----FKEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
74-133 1.51e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063723298  74 RIFDMFDVKRKGVIDFGDFVRSLNVFHPNASL-EDKIDFTFRLYDMDCTGYIERQEVKQML 133
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 50-177 3.07e-04

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 40.47  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  50 GLINKEE---FQLALFKSRKRENI--------FANRIFDMFDVKRKGVIDFGDFVRSLNV---------FHPNASLEDK- 108
Cdd:cd16179   110 GYIEADElknFLKHLLKEAKRDNDvsedklieYTDTILQLFDRNKDGKLQLSEMARLLPVkenflcrpiFKGAGKLTREd 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723298 109 IDFTFRLYDMDCTGYIERQEVKQMLIAL--LCESEMKLAD--ETIEIILDKtfedADVNQDGKIDKLEWSDFV 177
Cdd:cd16179   190 IDRVFALYDRDNNGTIENEELTGFLKDLleLVQEDYDEQDleEFKEIILRG----WDFNNDGKISRKELTMLL 258
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 99-184 7.98e-04

EF-hand, calcium binding motif, found in secretagogin (SCGN); 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 calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 39.31  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  99 FHPNASLEDKIDFT--FRLYDMDCTGYIERQEVKQMLIALLCESEMKLADETIEIILDKTFEDADVNQDGKIDKLEWSDF 176
Cdd:cd16178    82 FRREEPLDSSVEFMriWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMARI 161


                  ....*...
gi 1063723298 177 VNKNPSLL 184
Cdd:cd16178   162 LALQENFL 169
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 71-168 1.52e-03

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 38.54  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  71 FANRIFDMFDVKRKGVIDFGDFVRSLN-------VFHPNASLEDKIDF--TFRLYDMDCTGYIERQEVKQMLIALLCESE 141
Cdd:cd16179    50 LKEEFMEAYDENQDGRIDIRELAQLLPteenfllLFRRDNPLDSSVEFmkVWREYDKDNSGYIEADELKNFLKHLLKEAK 129

                          90       100
                  ....*....|....*....|....*....
gi 1063723298 142 MKLADETIEII--LDKTFEDADVNQDGKI 168
Cdd:cd16179   130 RDNDVSEDKLIeyTDTILQLFDRNKDGKL 158
EF-hand_5 pfam13202
EF hand;
153-177 7.72e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.06  E-value: 7.72e-03
                          10        20
                  ....*....|....*....|....*
gi 1063723298 153 LDKTFEDADVNQDGKIDKLEWSDFV 177
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 50-135 8.42e-03

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: 35.65  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723298  50 GLINKEEFQLALFKSRKRENI-FANRIFDMFDVKRKGVIDFGDFVRsLNVFHPNASLedkidfTFRLYDMDCTGYIERQE 128
Cdd:cd16185    15 GSIDVNELQKALAGGGLLFSLaTAEKLIRMFDRDGNGTIDFEEFAA-LHQFLSNMQN------GFEQRDTSRSGRLDANE 87


                  ....*..
gi 1063723298 129 VKQMLIA 135
Cdd:cd16185    88 VHEALAA 94
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 112-174 9.05e-03

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 35.97  E-value: 9.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063723298 112 TFRLYDMDCTGYIERQEVKQMLIALLCESEMKLADETIEIILDKTFEDADVNQDGKIDKLEWS 174
Cdd:cd16176    90 TWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMA 152
 
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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