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Conserved domains on  [gi|19074158|ref|NP_584764|]
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Ca2+-binding protein [Encephalitozoon cuniculi GB-M1]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-168 3.13e-09

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158  41 GCMTLKDLEAMFRSFFpfgsptnfsRRLFETINISQTETVDFHELLIAYSILVKGSDHEKLRWMFRFYDKDNDGVVSKEE 120
Cdd:COG5126  20 GVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19074158 121 MVEVvqcladMTSHTLDisidaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:COG5126  91 FRRL------LTALGVS-----EEEADELFARLDTDGdGKISFEEFVAA 128
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-168 3.13e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158  41 GCMTLKDLEAMFRSFFpfgsptnfsRRLFETINISQTETVDFHELLIAYSILVKGSDHEKLRWMFRFYDKDNDGVVSKEE 120
Cdd:COG5126  20 GVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19074158 121 MVEVvqcladMTSHTLDisidaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:COG5126  91 FRRL------LTALGVS-----EEEADELFARLDTDGdGKISFEEFVAA 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-168 2.24e-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: 48.70  E-value: 2.24e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158 100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCLADMTShtldisidaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS---------EEEIDEMIREVDKDGdGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
99-168 8.63e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 8.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19074158    99 EKLRWMFRFYDKDNDGVVSKEEMVEVVQCLAdmtshtLDISIDaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE------EGEPLS-DEEVEELFKEFDLDKdGRISFEEFLEL 65
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 9.61e-05

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: 38.13  E-value: 9.61e-05
                           10        20
                   ....*....|....*....|....*....
gi 19074158    100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCL 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
41-168 3.13e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158  41 GCMTLKDLEAMFRSFFpfgsptnfsRRLFETINISQTETVDFHELLIAYSILVKGSDHEKLRWMFRFYDKDNDGVVSKEE 120
Cdd:COG5126  20 GVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19074158 121 MVEVvqcladMTSHTLDisidaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:COG5126  91 FRRL------LTALGVS-----EEEADELFARLDTDGdGKISFEEFVAA 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-168 2.24e-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: 48.70  E-value: 2.24e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158 100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCLADMTShtldisidaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLS---------EEEIDEMIREVDKDGdGKIDFEEFLEL 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 66-126 4.39e-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: 45.23  E-value: 4.39e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19074158  66 RRLFETINISQTETVDFHELLIAYSILVKGSDHEKLRWMFRFYDKDNDGVVSKEEMVEVVQ 126
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
99-168 8.63e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 8.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19074158    99 EKLRWMFRFYDKDNDGVVSKEEMVEVVQCLAdmtshtLDISIDaEGIVSEIFASVESDR-GFLTFEDFKTL 168
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE------EGEPLS-DEEVEELFKEFDLDKdGRISFEEFLEL 65
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 9.61e-05

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: 38.13  E-value: 9.61e-05
                           10        20
                   ....*....|....*....|....*....
gi 19074158    100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCL 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 100-128 3.49e-04

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: 36.61  E-value: 3.49e-04
                          10        20
                  ....*....|....*....|....*....
gi 19074158   100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCL 128
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 103-184 6.30e-04

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 38.47  E-value: 6.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19074158 103 WM---FRFYDKDNDGVVSKEEMVEVVqcladmtsHTLDISIDAEGiVSEIFASVESD--RGFLTFEDF----KTLSIRSE 173
Cdd:cd16220   1 WVkqtFEEADKNGDGLLNIEEIYQLM--------HKLNVNLPRRK-VRQMFQEADTDenQGTLTFEEFcvfyKMMSLRRD 71

                        90
                ....*....|.
gi 19074158 174 kLFKMLVPFSD 184
Cdd:cd16220  72 -LYLLLLSYSD 81
EF-hand_6 pfam13405
EF-hand domain;
100-128 2.49e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.07  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 19074158   100 KLRWMFRFYDKDNDGVVSKEEMVEVVQCL 128
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EF-hand_8 pfam13833
EF-hand domain pair;
76-126 5.67e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 33.83  E-value: 5.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 19074158    76 QTETVDFHELLIAYSILVKG--SDHEkLRWMFRFYDKDNDGVVSKEEMVEVVQ 126
Cdd:pfam13833   1 EKGVITREELKRALALLGLKdlSEDE-VDILFREFDTDGDGYISFDEFCVLLE 52
 
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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