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Conserved domains on  [gi|17556408|ref|NP_497601|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

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 ...
 115-181 3.55e-15

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: 66.80  E-value: 3.55e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556408 115 KLRFAFTMYDLNKSGTITKDEFQDILAMMiGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEM----IREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-183 2.06e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408  49 FLTKGDFQSIAelkqnplgDRIIDAFFADAEVLERRKVYFKDFVKVLSHFRPinknkphpwNSREAKLRFAFTMYDLNKS 128
Cdd:COG5126  21 VLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGMESLFE---------ATVEPFARAAFDLLDTDGD 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17556408 129 GTITKDEFQdilAMMIGVGVPKDQvnsiADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:COG5126  84 GKISADEFR---RLLTALGVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-181 3.55e-15

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: 66.80  E-value: 3.55e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556408 115 KLRFAFTMYDLNKSGTITKDEFQDILAMMiGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEM----IREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-183 2.06e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408  49 FLTKGDFQSIAelkqnplgDRIIDAFFADAEVLERRKVYFKDFVKVLSHFRPinknkphpwNSREAKLRFAFTMYDLNKS 128
Cdd:COG5126  21 VLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGMESLFE---------ATVEPFARAAFDLLDTDGD 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17556408 129 GTITKDEFQdilAMMIGVGVPKDQvnsiADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:COG5126  84 GKISADEFR---RLLTALGVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
113-181 4.96e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.96e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408   113 EAKLRFAFTMYDLNKSGTITKDEFQDILAM-MIGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
112-183 5.24e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 5.24e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 112 REAKLRFAFTMYDLNKSGTITKDEFQdilAMMIGvgvpkdqvnsIADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFE---ALFRR----------LWATLFSEADTDGDGRISREEFVAGMES 61
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 158-184 2.43e-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: 39.67  E-value: 2.43e-05
                           10        20
                   ....*....|....*....|....*..
gi 17556408    158 DRTMREADRDGDGFITFQEFCNAMEKT 184
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00183 PTZ00183
centrin; Provisional
 75-184 2.46e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408   75 FADAEVLERRKVYFKDFVKVLShfrpinkNKPHPWNSREAKLRfAFTMYDLNKSGTITKDEFQDIlAMMIGVGVPKDQVN 154
Cdd:PTZ00183  59 IADVDKDGSGKIDFEEFLDIMT-------KKLGERDPREEILK-AFRLFDDDKTGKISLKNLKRV-AKELGETITDEELQ 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 17556408  155 SIADrtmrEADRDGDGFITFQEFCNAMEKT 184
Cdd:PTZ00183 130 EMID----EADRNGDGEISEEEFYRIMKKT 155
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-181 3.55e-15

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: 66.80  E-value: 3.55e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556408 115 KLRFAFTMYDLNKSGTITKDEFQDILAMMiGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEM----IREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-183 2.06e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.73  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408  49 FLTKGDFQSIAelkqnplgDRIIDAFFADAEVLERRKVYFKDFVKVLSHFRPinknkphpwNSREAKLRFAFTMYDLNKS 128
Cdd:COG5126  21 VLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGMESLFE---------ATVEPFARAAFDLLDTDGD 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17556408 129 GTITKDEFQdilAMMIGVGVPKDQvnsiADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:COG5126  84 GKISADEFR---RLLTALGVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
113-181 4.96e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.96e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408   113 EAKLRFAFTMYDLNKSGTITKDEFQDILAM-MIGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLELY 66
EF-hand_8 pfam13833
EF-hand domain pair;
127-183 2.30e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 45.77  E-value: 2.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17556408   127 KSGTITKDEFQDILAMMIGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAMEK 183
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDIL----FREFDTDGDGYISFDEFCVLLER 53
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
112-183 5.24e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 5.24e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 112 REAKLRFAFTMYDLNKSGTITKDEFQdilAMMIGvgvpkdqvnsIADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFE---ALFRR----------LWATLFSEADTDGDGRISREEFVAGMES 61
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 112-183 1.73e-05

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: 42.13  E-value: 1.73e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 112 REAKLRFAFTMYDLNKSGTITKDEFQDILAMMIGVGVPKDQVNSIADRTMREADRDGDGFITFQEFCNAMEK 183
Cdd:cd16252  35 QEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVAPLSDEEAEAMIQAADTDGDGRIDFQEFSDMVKK 106
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 158-184 2.43e-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: 39.67  E-value: 2.43e-05
                           10        20
                   ....*....|....*....|....*..
gi 17556408    158 DRTMREADRDGDGFITFQEFCNAMEKT 184
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00183 PTZ00183
centrin; Provisional
 75-184 2.46e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408   75 FADAEVLERRKVYFKDFVKVLShfrpinkNKPHPWNSREAKLRfAFTMYDLNKSGTITKDEFQDIlAMMIGVGVPKDQVN 154
Cdd:PTZ00183  59 IADVDKDGSGKIDFEEFLDIMT-------KKLGERDPREEILK-AFRLFDDDKTGKISLKNLKRV-AKELGETITDEELQ 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 17556408  155 SIADrtmrEADRDGDGFITFQEFCNAMEKT 184
Cdd:PTZ00183 130 EMID----EADRNGDGEISEEEFYRIMKKT 155
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 158-184 3.55e-05

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: 39.31  E-value: 3.55e-05
                          10        20
                  ....*....|....*....|....*..
gi 17556408   158 DRTMREADRDGDGFITFQEFCNAMEKT 184
Cdd:pfam00036   3 KEIFRLFDKDGDGKIDFEEFKELLKKL 29
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 120-191 3.59e-05

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 40.28  E-value: 3.59e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 120 FTMYDLNKSGTITKDEFQDILaMMIGVgvPKDQVNSIADrtmrEADRDGDGFITFQEFCNAMEktDIEQKMS 191
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPFL-GKSGL--PRSVLAQIWD----LADTDKDGKLDKEEFAIAMH--LIALALN 67
PTZ00184 PTZ00184
calmodulin; Provisional
 113-181 6.03e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 6.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556408  113 EAKLRFAFTMYDLNKSGTITKDEFQDILAMMiGVGVPKDQVnsiaDRTMREADRDGDGFITFQEFCNAM 181
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEEV----DEMIREADVDGDGQINYEEFVKMM 146
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 112-177 1.83e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 41.15  E-value: 1.83e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17556408 112 REAKLRFAFTmyDLNKSGTITKDEF---------QDILAMMIgvgvpkdqvnsiaDRTMREADRDGDGFITFQEF 177
Cdd:cd16227 122 EDDKEMFEAA--DLNKDGKLDKTEFsafqhpeeyPHMHPVLI-------------EQTLRDKDKDNDGFISFQEF 181
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 115-143 3.30e-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: 36.59  E-value: 3.30e-04
                           10        20
                   ....*....|....*....|....*....
gi 17556408    115 KLRFAFTMYDLNKSGTITKDEFQDILAMM 143
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 115-143 3.93e-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: 3.93e-04
                          10        20
                  ....*....|....*....|....*....
gi 17556408   115 KLRFAFTMYDLNKSGTITKDEFQDILAMM 143
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 115-181 5.53e-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: 5.53e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556408 115 KLRFAFTMYDLNKSGTITkdeFQDILAMM--IGVGVPKDQVNSIadrtMREADRDGDGFITFQEFCNAM 181
Cdd:cd15898   1 WLRRQWIKADKDGDGKLS---LKEIKKLLkrLNIRVSEKELKKL----FKEVDTNGDGTLTFDEFEELY 62
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 115-179 6.35e-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: 6.35e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556408 115 KLRFAFTMYDLNKSGTITKDEFQdiLAMMIGVGVPKDqvnsiaDRT----MREADRDGDGFITFQEFCN 179
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQ--RALSNGDWTPFS------IETvrlmINMFDRDRSGTINFDEFVG 61
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 124-181 1.12e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17556408    124 DLNKSGTITKDEFQDILAMMigvGVPKDQVNSIADRtmreADRDGDGFITFQEFCNAM 181
Cdd:smart00027  20 DKNQDGTVTGAQAKPILLKS---GLPQTLLAKIWNL----ADIDNDGELDKDEFALAM 70
EF-hand_6 pfam13405
EF-hand domain;
115-143 1.36e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 17556408   115 KLRFAFTMYDLNKSGTITKDEFQDILAMM 143
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 113-188 1.44e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 38.45  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556408 113 EAKLRFA--FTMYDLNKSGTITKDEFQD-ILAMMIGVGvpkdqvNSIADRTMREADRDGDGFITFQEFCN---AMEKTDI 186
Cdd:cd16227  33 EAKRRLAvlAKKMDLNDDGFIDRKELKAwILRSFKMLD------EEEANERFEEADEDGDGKVTWEEYLAdsfGYDDEDN 106


                ..
gi 17556408 187 EQ 188
Cdd:cd16227 107 EE 108
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 161-193 2.19e-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: 35.40  E-value: 2.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17556408 161 MREA----DRDGDGFITFQEFCNAM----------EKTDIEQKMSFR 193
Cdd:cd22949   5 FREAfilfDRDGDGELTMYEAVLAMrscgipltndEKDALPASMNWD 51
PTZ00183 PTZ00183
centrin; Provisional
 113-183 2.22e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 36.98  E-value: 2.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17556408  113 EAKLRFAFTMYDLNKSGTITKDEFQdiLAMM-IGVGVPKDQV-NSIADrtmreADRDGDGFITFQEFCNAMEK 183
Cdd:PTZ00183  16 KKEIREAFDLFDTDGSGTIDPKELK--VAMRsLGFEPKKEEIkQMIAD-----VDKDGSGKIDFEEFLDIMTK 81
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 116-177 2.39e-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: 37.19  E-value: 2.39e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 116 LRFAFTMYDLNKSGTITKDEFQDILAMMiGVGVPKDQvnsiADRTMREADRDGDGFITFQEF 177
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQKALAGG-GLLFSLAT----AEKLIRMFDRDGNGTIDFEEF 58
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 122-181 4.54e-03

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: 36.35  E-value: 4.54e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17556408 122 MYDLNKSGTITKDEFQDILammigvgvpkdqvNSIAD--RTMREADRDGDGFITFQEFCNAM 181
Cdd:cd16180  45 MFDRDRSGTINFDEFVGLW-------------KYIQDwrRLFRRFDRDRSGSIDFNELQNAL 93
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 113-177 5.20e-03

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


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 35.20  E-value: 5.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17556408 113 EAKLRFAFTMYDLNKSGTITKDEFQDILAmmigvGVPKDQVNSIADRT---MREADRDGDGFITFQEF 177
Cdd:cd16251  33 EDQIKKVFQILDKDKSGFIEEEELKYILK-----GFSIAGRDLTDEETkalLAAGDTDGDGKIGVEEF 95
 
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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