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Conserved domains on  [gi|755552302|ref|XP_006521594|]
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EF-hand calcium-binding domain-containing protein 6 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF-hand_11 pfam08976
EF-hand domain; This domain is found predominantly in DJ binding proteins.
 1197-1301 1.51e-69

EF-hand domain; This domain is found predominantly in DJ binding proteins.


:

Pssm-ID: 401068  Cd Length: 105  Bit Score: 228.06  E-value: 1.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  1197 ETAHRDIVARVQKAVASHYHTIVQEFENFDTLKSNTVSRDEFRSICTRHIQILTDEQFDRLWSELPVNAKGRLKYQDFLS 1276
Cdd:pfam08976    1 ATADRDILARLHKAVASHYHAITQEFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDFLS 80

                           90       100
                   ....*....|....*....|....*
gi 755552302  1277 KLSIERVPSPPMAAGDSGESTMAQR 1301
Cdd:pfam08976   81 KFSIERTAAPPMAAGDSGESAMAQR 105
EF-hand_7 pfam13499
EF-hand domain pair;
1474-1535 2.87e-10

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 57.65  E-value: 2.87e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755552302  1474 MRRSFKTYDKNGTGLLSVADFRKVLRQ--YSINLSEEEFFHVLEYYDKSLSSKISYNDFLRAFL 1535
Cdd:pfam13499    4 LKEAFKLLDSDGDGYLDVEELKKLLRKleEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 super family cl33171
centrin; Provisional
 1364-1532 5.56e-07

centrin; Provisional


The actual alignment was detected with superfamily member PTZ00183:

Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 50.84  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1364 LRECKEK-DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFiqscvlllkaketslMRRMRIQN 1442
Cdd:PTZ00183   19 IREAFDLfDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEF---------------LDIMTKKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1443 ADKMKEAGMEtpsfysallriqpkivhcwrpmrRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLS 1522
Cdd:PTZ00183   84 GERDPREEIL-----------------------KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGD 140

                         170
                  ....*....|
gi 755552302 1523 SKISYNDFLR 1532
Cdd:PTZ00183  141 GEISEEEFYR 150
PTZ00184 super family cl33172
calmodulin; Provisional
 122-285 1.23e-05

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.68  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  122 KKVFQILDRNHNQMVTKGDLKRVITAFLIPLTKDQFQDLLAQIPISSLGNVPYLEFLSRFGggidiningikrvnenevd 201
Cdd:PTZ00184   14 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA------------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  202 nrRTVKEVQLTEKIfrnmrsiRKVFQVMDVNNTGLVQPQELRRVLETFCLRMQDGDYEKFLEQYNIDKTTAVDYNAFLKN 281
Cdd:PTZ00184   75 --RKMKDTDSEEEI-------KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKM 145


                  ....
gi 755552302  282 LSVK 285
Cdd:PTZ00184  146 MMSK 149
EF-hand_7 pfam13499
EF-hand domain pair;
898-952 1.28e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 1.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755552302   898 FIETDNEGNGILRRRDIKNSLYGF--DIPLTPREFEKLWQNYDTEGRGYITYQEFLH 952
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_PI-PLC super family cl28895
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 894-1004 3.29e-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.


The actual alignment was detected with superfamily member cd15898:

Pssm-ID: 333715 [Multi-domain]  Cd Length: 137  Bit Score: 42.27  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  894 LSKNFIETDNEGNGILRRRDIKNSLYGFDIPLTPREFEKLWQNYDTEGRGYITYQEF---LHRLGIR---------YSpK 961
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFeelYKSLTERpelepifkkYA-G 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755552302  962 VHRPY--KEDYFNFLghftkpKQVQEEIQELQQIserEKLMNHYE 1004
Cdd:cd15898    81 TNRDYmtLEEFIRFL------REEQGENVSEEEC---EELIEKYE 116
 
Name Accession Description Interval E-value
EF-hand_11 pfam08976
EF-hand domain; This domain is found predominantly in DJ binding proteins.
 1197-1301 1.51e-69

EF-hand domain; This domain is found predominantly in DJ binding proteins.


Pssm-ID: 401068  Cd Length: 105  Bit Score: 228.06  E-value: 1.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  1197 ETAHRDIVARVQKAVASHYHTIVQEFENFDTLKSNTVSRDEFRSICTRHIQILTDEQFDRLWSELPVNAKGRLKYQDFLS 1276
Cdd:pfam08976    1 ATADRDILARLHKAVASHYHAITQEFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDFLS 80

                           90       100
                   ....*....|....*....|....*
gi 755552302  1277 KLSIERVPSPPMAAGDSGESTMAQR 1301
Cdd:pfam08976   81 KFSIERTAAPPMAAGDSGESAMAQR 105
EF-hand_7 pfam13499
EF-hand domain pair;
1474-1535 2.87e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 57.65  E-value: 2.87e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755552302  1474 MRRSFKTYDKNGTGLLSVADFRKVLRQ--YSINLSEEEFFHVLEYYDKSLSSKISYNDFLRAFL 1535
Cdd:pfam13499    4 LKEAFKLLDSDGDGYLDVEELKKLLRKleEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1475-1534 5.09e-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: 48.31  E-value: 5.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1475 RRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLSSKISYNDFLRAF 1534
Cdd:cd00051     3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
 1364-1532 5.56e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 50.84  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1364 LRECKEK-DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFiqscvlllkaketslMRRMRIQN 1442
Cdd:PTZ00183   19 IREAFDLfDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEF---------------LDIMTKKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1443 ADKMKEAGMEtpsfysallriqpkivhcwrpmrRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLS 1522
Cdd:PTZ00183   84 GERDPREEIL-----------------------KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGD 140

                         170
                  ....*....|
gi 755552302 1523 SKISYNDFLR 1532
Cdd:PTZ00183  141 GEISEEEFYR 150
PTZ00184 PTZ00184
calmodulin; Provisional
 122-285 1.23e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.68  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  122 KKVFQILDRNHNQMVTKGDLKRVITAFLIPLTKDQFQDLLAQIPISSLGNVPYLEFLSRFGggidiningikrvnenevd 201
Cdd:PTZ00184   14 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA------------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  202 nrRTVKEVQLTEKIfrnmrsiRKVFQVMDVNNTGLVQPQELRRVLETFCLRMQDGDYEKFLEQYNIDKTTAVDYNAFLKN 281
Cdd:PTZ00184   75 --RKMKDTDSEEEI-------KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKM 145


                  ....
gi 755552302  282 LSVK 285
Cdd:PTZ00184  146 MMSK 149
EF-hand_7 pfam13499
EF-hand domain pair;
118-181 2.06e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 2.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755552302   118 RDDIKKVFQILDRNHNQMVTKGDLKRVITAFL--IPLTKDQFQDLLAQIPISSLGNVPYLEFLSRF 181
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEegEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 222-280 4.55e-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: 42.53  E-value: 4.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755552302  222 IRKVFQVMDVNNTGLVQPQELRRVLETFCLRMQDGDYEKFLEQYNIDKTTAVDYNAFLK 280
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1368-1413 6.95e-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: 42.15  E-value: 6.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755552302 1368 KEKDTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGK 1413
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGK 52
EF-hand_7 pfam13499
EF-hand domain pair;
898-952 1.28e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 1.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755552302   898 FIETDNEGNGILRRRDIKNSLYGF--DIPLTPREFEKLWQNYDTEGRGYITYQEFLH 952
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 894-1004 3.29e-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: 42.27  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  894 LSKNFIETDNEGNGILRRRDIKNSLYGFDIPLTPREFEKLWQNYDTEGRGYITYQEF---LHRLGIR---------YSpK 961
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFeelYKSLTERpelepifkkYA-G 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755552302  962 VHRPY--KEDYFNFLghftkpKQVQEEIQELQQIserEKLMNHYE 1004
Cdd:cd15898    81 TNRDYmtLEEFIRFL------REEQGENVSEEEC---EELIEKYE 116
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 894-1001 1.01e-03

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: 41.16  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  894 LSKNFIETDNEGNGILRRRDIKNSLYGFDIPLTPREFEKLWQNYDT-EGRGYITYQEF------------LHRLGIRYSP 960
Cdd:cd16220     2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTdENQGTLTFEEFcvfykmmslrrdLYLLLLSYSD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755552302  961 KVHRPYKEDYFNFLGHFTKPKQVQEE----IQELQQISEREKLMN 1001
Cdd:cd16220    82 KKDHLTVEELAQFLKVEQKMNNVTTEycldIIKKFEVSEENKEQN 126
EF-hand_7 pfam13499
EF-hand domain pair;
1353-1421 4.86e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 4.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755552302  1353 RKQIQGCWRELlreckekDTDKQGTISAAEFLALVEKFKL--DISREESQQLIVKYDLKNNGKFAYCDFIQ 1421
Cdd:pfam13499    1 EEKLKEAFKLL-------DSDGDGYLDVEELKKLLRKLEEgePLSDEEVEELFKEFDLDKDGRISFEEFLE 64
 
Name Accession Description Interval E-value
EF-hand_11 pfam08976
EF-hand domain; This domain is found predominantly in DJ binding proteins.
 1197-1301 1.51e-69

EF-hand domain; This domain is found predominantly in DJ binding proteins.


Pssm-ID: 401068  Cd Length: 105  Bit Score: 228.06  E-value: 1.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  1197 ETAHRDIVARVQKAVASHYHTIVQEFENFDTLKSNTVSRDEFRSICTRHIQILTDEQFDRLWSELPVNAKGRLKYQDFLS 1276
Cdd:pfam08976    1 ATADRDILARLHKAVASHYHAITQEFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDFLS 80

                           90       100
                   ....*....|....*....|....*
gi 755552302  1277 KLSIERVPSPPMAAGDSGESTMAQR 1301
Cdd:pfam08976   81 KFSIERTAAPPMAAGDSGESAMAQR 105
EF-hand_7 pfam13499
EF-hand domain pair;
1474-1535 2.87e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 57.65  E-value: 2.87e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755552302  1474 MRRSFKTYDKNGTGLLSVADFRKVLRQ--YSINLSEEEFFHVLEYYDKSLSSKISYNDFLRAFL 1535
Cdd:pfam13499    4 LKEAFKLLDSDGDGYLDVEELKKLLRKleEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1475-1534 5.09e-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: 48.31  E-value: 5.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1475 RRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLSSKISYNDFLRAF 1534
Cdd:cd00051     3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
 1364-1532 5.56e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 50.84  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1364 LRECKEK-DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFiqscvlllkaketslMRRMRIQN 1442
Cdd:PTZ00183   19 IREAFDLfDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEF---------------LDIMTKKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1443 ADKMKEAGMEtpsfysallriqpkivhcwrpmrRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLS 1522
Cdd:PTZ00183   84 GERDPREEIL-----------------------KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGD 140

                         170
                  ....*....|
gi 755552302 1523 SKISYNDFLR 1532
Cdd:PTZ00183  141 GEISEEEFYR 150
PTZ00184 PTZ00184
calmodulin; Provisional
 1362-1532 1.36e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.37  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1362 ELLRECKEK----DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFIqscvlllkaketSLMRR 1437
Cdd:PTZ00184    8 EQIAEFKEAfslfDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFL------------TLMAR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1438 mriqnadKMKEAGMEtpsfysallriqpkivhcwRPMRRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYY 1517
Cdd:PTZ00184   76 -------KMKDTDSE-------------------EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREA 129

                         170
                  ....*....|....*
gi 755552302 1518 DKSLSSKISYNDFLR 1532
Cdd:PTZ00184  130 DVDGDGQINYEEFVK 144
PTZ00184 PTZ00184
calmodulin; Provisional
 122-285 1.23e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.68  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  122 KKVFQILDRNHNQMVTKGDLKRVITAFLIPLTKDQFQDLLAQIPISSLGNVPYLEFLSRFGggidiningikrvnenevd 201
Cdd:PTZ00184   14 KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA------------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  202 nrRTVKEVQLTEKIfrnmrsiRKVFQVMDVNNTGLVQPQELRRVLETFCLRMQDGDYEKFLEQYNIDKTTAVDYNAFLKN 281
Cdd:PTZ00184   75 --RKMKDTDSEEEI-------KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKM 145


                  ....
gi 755552302  282 LSVK 285
Cdd:PTZ00184  146 MMSK 149
EF-hand_7 pfam13499
EF-hand domain pair;
118-181 2.06e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 2.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755552302   118 RDDIKKVFQILDRNHNQMVTKGDLKRVITAFL--IPLTKDQFQDLLAQIPISSLGNVPYLEFLSRF 181
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEegEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 222-280 4.55e-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: 42.53  E-value: 4.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755552302  222 IRKVFQVMDVNNTGLVQPQELRRVLETFCLRMQDGDYEKFLEQYNIDKTTAVDYNAFLK 280
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1368-1413 6.95e-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: 42.15  E-value: 6.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755552302 1368 KEKDTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGK 1413
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGK 52
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 1360-1426 7.15e-05

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: 44.83  E-value: 7.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755552302 1360 WRELLREckeKDTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFIQSCVLL 1426
Cdd:cd16180    69 WRRLFRR---FDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTL 132
EF-hand_7 pfam13499
EF-hand domain pair;
898-952 1.28e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 1.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755552302   898 FIETDNEGNGILRRRDIKNSLYGF--DIPLTPREFEKLWQNYDTEGRGYITYQEFLH 952
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 1371-1426 2.81e-04

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 43.02  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755552302 1371 DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFIQSCVLL 1426
Cdd:cd16184    77 DRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRARRSLTLDQFIQVCVQL 132
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 894-1004 3.29e-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: 42.27  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  894 LSKNFIETDNEGNGILRRRDIKNSLYGFDIPLTPREFEKLWQNYDTEGRGYITYQEF---LHRLGIR---------YSpK 961
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFeelYKSLTERpelepifkkYA-G 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755552302  962 VHRPY--KEDYFNFLghftkpKQVQEEIQELQQIserEKLMNHYE 1004
Cdd:cd15898    81 TNRDYmtLEEFIRFL------REEQGENVSEEEC---EELIEKYE 116
EF-hand_11 pfam08976
EF-hand domain; This domain is found predominantly in DJ binding proteins.
 105-181 5.83e-04

EF-hand domain; This domain is found predominantly in DJ binding proteins.


Pssm-ID: 401068  Cd Length: 105  Bit Score: 40.86  E-value: 5.83e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755552302   105 DIERILAQKISSRRDDIKKVFQILDRNHNQMVTKGDLKRVITAFLIPLTKDQFQDLLAQIPISSLGNVPYLEFLSRF 181
Cdd:pfam08976    6 DILARLHKAVASHYHAITQEFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDFLSKF 82
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 1474-1533 7.10e-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: 41.75  E-value: 7.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1474 MRRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLSSKISYNDFLRA 1533
Cdd:cd16180    69 WRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEA 128
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 1371-1426 7.26e-04

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 41.86  E-value: 7.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755552302 1371 DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFIQSCVLL 1426
Cdd:cd16183    77 DRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFIQCCVVL 132
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 894-1001 1.01e-03

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: 41.16  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302  894 LSKNFIETDNEGNGILRRRDIKNSLYGFDIPLTPREFEKLWQNYDT-EGRGYITYQEF------------LHRLGIRYSP 960
Cdd:cd16220     2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTdENQGTLTFEEFcvfykmmslrrdLYLLLLSYSD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755552302  961 KVHRPYKEDYFNFLGHFTKPKQVQEE----IQELQQISEREKLMN 1001
Cdd:cd16220    82 KKDHLTVEELAQFLKVEQKMNNVTTEycldIIKKFEVSEENKEQN 126
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 1371-1536 1.46e-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: 41.05  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1371 DTDKQGTISAAEFLALVEKFKLDISREESQQLIVKYDLKNNGKFAYCDFIQSCVLLLKaketslmrrmriqnadkmkeag 1450
Cdd:cd16185    10 DRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAALHQFLSN---------------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552302 1451 metpsfysallriqpkivhcwrpMRRSFKTYDKNGTGLLSVADFRKVLRQYSINLSEEEFFHVLEYYDKSLSSKISYNDF 1530
Cdd:cd16185    68 -----------------------MQNGFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124


                  ....*...
gi 755552302 1531 LR--AFLQ 1536
Cdd:cd16185   125 IElcIFLA 132
EF-hand_7 pfam13499
EF-hand domain pair;
1353-1421 4.86e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 4.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755552302  1353 RKQIQGCWRELlreckekDTDKQGTISAAEFLALVEKFKL--DISREESQQLIVKYDLKNNGKFAYCDFIQ 1421
Cdd:pfam13499    1 EEKLKEAFKLL-------DSDGDGYLDVEELKKLLRKLEEgePLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EF-hand_7 pfam13499
EF-hand domain pair;
1222-1275 5.86e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 5.86e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755552302  1222 FENFDTLKSNTVSRDEFRSICTRHIQI--LTDEQFDRLWSELPVNAKGRLKYQDFL 1275
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFL 63
 
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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