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Conserved domains on  [gi|115763|sp|P10463|]
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RecName: Full=Calcyphosin; AltName: Full=Calcyphosine; AltName: Full=Protein 5; AltName: Full=Thyroid protein p24; Short=TPP

Protein Classification

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

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
56-162 4.75e-10

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 4.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    56 VLDTAEAEGVCRRW--------DRDGSGTLDLEEFLRALRPPMSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRTh 127
Cdd:COG5126  21 VLERDDFEALFRRLwatlfseaDTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG- 99

                        90       100       110
                ....*....|....*....|....*....|....*
gi 115763   128 pkvqsgewTEEEVLRRFLDNFDSSeKDGQVTLAEF 162
Cdd:COG5126 100 --------VSEEEADELFARLDTD-GDGKISFEEF 125
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
56-162 4.75e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 4.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    56 VLDTAEAEGVCRRW--------DRDGSGTLDLEEFLRALRPPMSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRTh 127
Cdd:COG5126  21 VLERDDFEALFRRLwatlfseaDTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG- 99

                        90       100       110
                ....*....|....*....|....*....|....*
gi 115763   128 pkvqsgewTEEEVLRRFLDNFDSSeKDGQVTLAEF 162
Cdd:COG5126 100 --------VSEEEADELFARLDTD-GDGKISFEEF 125
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 45-165 1.20e-07

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: 48.43  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    45 ELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRALRPPMSQAReavIAAAFAKLDRSGDGVVTVDD----LRg 120
Cdd:cd15898  21 EIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPE---LEPIFKKYAGTNRDYMTLEEfirfLR- 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 115763   121 vysgrthpKVQSGEWTEEEVLRRFlDNFDSSEKDGQVTLAEFQDY 165
Cdd:cd15898  97 --------EEQGENVSEEECEELI-EKYEPERENRQLSFEGFTNF 132
EF-hand_7 pfam13499
EF-hand domain pair;
95-167 4.84e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.32  E-value: 4.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115763      95 EAVIAAAFAKLDRSGDGVVTVDDLRGVYSgrthpKVQSGEWTEEEVLRRFLDNFDSSeKDGQVTLAEFQDYYS 167
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLR-----KLEEGEPLSDEEVEELFKEFDLD-KDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 51-162 3.02e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.14  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763     51 AELGLVLDT-------AEAEGVCRRWDRDGSGTLDLEEFLRALRPPMSQA-REAVIAAAFAKLDRSGDGVVTVDDLRgvy 122
Cdd:PTZ00184  31 KELGTVMRSlgqnpteAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELR--- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115763    123 sgrtHPKVQSGEWTEEEVLRRFLDNFDsSEKDGQVTLAEF 162
Cdd:PTZ00184 108 ----HVMTNLGEKLTDEEVDEMIREAD-VDGDGQINYEEF 142
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
70-163 4.93e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.36  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763     70 DRDGSGTLDLEEFLRALRPP---MSQAREAVIAAA-FAKLDRSGDGVVTVDDLRGVYSGrthpkvqSGEWTEEEVLRRFL 145
Cdd:NF041410  73 DSDGDGSLSSDELAAAAPPPpppPDQAPSTELADDlLSALDTDGDGSISSDELSAGLTS-------AGSSADSSQLFSAL 145

                         90
                 ....*....|....*...
gi 115763    146 DnfdsSEKDGQVTLAEFQ 163
Cdd:NF041410 146 D----SDGDGSVSSDELA 159
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
56-162 4.75e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 4.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    56 VLDTAEAEGVCRRW--------DRDGSGTLDLEEFLRALRPPMSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRTh 127
Cdd:COG5126  21 VLERDDFEALFRRLwatlfseaDTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG- 99

                        90       100       110
                ....*....|....*....|....*....|....*
gi 115763   128 pkvqsgewTEEEVLRRFLDNFDSSeKDGQVTLAEF 162
Cdd:COG5126 100 --------VSEEEADELFARLDTD-GDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
68-188 1.22e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 51.33  E-value: 1.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    68 RWDRDGSGTLDLEEFlralrppmSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGRTHPKVqsgewteEEVLRRFLDN 147
Cdd:COG5126  13 LLDADGDGVLERDDF--------EALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-------EPFARAAFDL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 115763   148 FDSSeKDGQVTLAEFQDYYSGVS----------ASMDTD-------EEFVAMMTSAWQ 188
Cdd:COG5126  78 LDTD-GDGKISADEFRRLLTALGvseeeadelfARLDTDgdgkisfEEFVAAVRDYYT 134
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
45-119 4.96e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 4.96e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115763    45 ELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRALRppMSQAREAVIAAAFAKLDRSGDGVVTVDDLR 119
Cdd:COG5126  54 EFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFV 126
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 45-165 1.20e-07

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: 48.43  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    45 ELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRALRPPMSQAReavIAAAFAKLDRSGDGVVTVDD----LRg 120
Cdd:cd15898  21 EIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPE---LEPIFKKYAGTNRDYMTLEEfirfLR- 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 115763   121 vysgrthpKVQSGEWTEEEVLRRFlDNFDSSEKDGQVTLAEFQDY 165
Cdd:cd15898  97 --------EEQGENVSEEECEELI-EKYEPERENRQLSFEGFTNF 132
EF-hand_7 pfam13499
EF-hand domain pair;
95-167 4.84e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.32  E-value: 4.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115763      95 EAVIAAAFAKLDRSGDGVVTVDDLRGVYSgrthpKVQSGEWTEEEVLRRFLDNFDSSeKDGQVTLAEFQDYYS 167
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLR-----KLEEGEPLSDEEVEELFKEFDLD-KDGRISFEEFLELYS 67
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 67-165 1.03e-06

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 47.44  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    67 RRW---DRDGSGTLDLEEFLRALRPPMS-QAREAVIAAAFAKLDRSGDGVVTVDDLRGVYSGrTHPKVQSGEWTEEEVlR 142
Cdd:cd15899 127 KRFeaaDQDGDLILTLEEFLAFLHPEESpYMLDFVIKETLEDLDKNGDGFISLEEFISDPYS-ADENEEEPEWVKVEK-E 204

                        90       100
                ....*....|....*....|...
gi 115763   143 RFLDNFDsSEKDGQVTLAEFQDY 165
Cdd:cd15899 205 RFVELRD-KDKDGKLDGEELLSW 226
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 67-166 1.61e-06

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 46.81  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    67 RRW---DRDGSGTLDLEEFLRALRPP----MsqaREAVIAAAFAKLDRSGDGVVTVDDLRG-VYSGRTHPKVqsGEW--T 136
Cdd:cd16226 123 RRWkaaDQDGDGKLTKEEFTAFLHPEefphM---RDIVVQETLEDIDKNKDGFISLEEYIGdMYRDDDEEED--PDWvkS 197

                        90       100       110
                ....*....|....*....|....*....|
gi 115763   137 EEEVLRRFLDnfdsSEKDGQVTLAEFQDYY 166
Cdd:cd16226 198 EREQFKEFRD----KNKDGKMDREEVKDWI 223
PTZ00184 PTZ00184
calmodulin; Provisional
 51-162 3.02e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.14  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763     51 AELGLVLDT-------AEAEGVCRRWDRDGSGTLDLEEFLRALRPPMSQA-REAVIAAAFAKLDRSGDGVVTVDDLRgvy 122
Cdd:PTZ00184  31 KELGTVMRSlgqnpteAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELR--- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115763    123 sgrtHPKVQSGEWTEEEVLRRFLDNFDsSEKDGQVTLAEF 162
Cdd:PTZ00184 108 ----HVMTNLGEKLTDEEVDEMIREAD-VDGDGQINYEEF 142
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 45-119 6.95e-06

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: 44.13  E-value: 6.95e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115763    45 ELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLrALRPPMSQAReaviaAAFAKLDRSGDGVVTVDDLR 119
Cdd:cd16185  21 ELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFA-ALHQFLSNMQ-----NGFEQRDTSRSGRLDANEVH 89
EF-hand_7 pfam13499
EF-hand domain pair;
70-123 1.52e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115763      70 DRDGSGTLDLEEFLRALRPPMSQA--REAVIAAAFAKLDRSGDGVVTVDDLRGVYS 123
Cdd:pfam13499  12 DSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 67-161 3.20e-05

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 43.04  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    67 RRWDRDGSGTLDLEEFLRALRPP-MSQAREAVIAAAFAKLDRSGDGVVTVDD-LRGVYSGRthPKVQSGEWTEEEvlRRF 144
Cdd:cd16230 130 RVADQDGDSMATREELTAFLHPEeFPHMRDIVVAETLEDLDKNKDGYVQVEEyIADLYSGE--PGEEEPAWVQTE--RQQ 205

                        90
                ....*....|....*..
gi 115763   145 LDNFDSSEKDGQVTLAE 161
Cdd:cd16230 206 FRQFRDLNKDGRLDGSE 222
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 45-87 3.70e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.84  E-value: 3.70e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 115763    45 ELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRALR 87
Cdd:cd00051  21 ELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
70-163 4.93e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.36  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763     70 DRDGSGTLDLEEFLRALRPP---MSQAREAVIAAA-FAKLDRSGDGVVTVDDLRGVYSGrthpkvqSGEWTEEEVLRRFL 145
Cdd:NF041410  73 DSDGDGSLSSDELAAAAPPPpppPDQAPSTELADDlLSALDTDGDGSISSDELSAGLTS-------AGSSADSSQLFSAL 145

                         90
                 ....*....|....*...
gi 115763    146 DnfdsSEKDGQVTLAEFQ 163
Cdd:NF041410 146 D----SDGDGSVSSDELA 159
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-164 2.78e-04

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: 37.53  E-value: 2.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115763   100 AAFAKLDRSGDGVVTVDDLRGVysgrthPKVQSGEWTEEEVlRRFLDNFDsSEKDGQVTLAEFQD 164
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAA------LKSLGEGLSEEEI-DEMIREVD-KDGDGKIDFEEFLE 60
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 70-163 3.54e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 40.11  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    70 DRDGSGTLDLEEFLRALRPP-MSQAREAVIAAAFAKLDRSGDGVVTVDDLRGVYsgRTHPKV-QSGEWTEEEVLrRFLDN 147
Cdd:cd16224 134 NTDGGPGLNLTEFIAFEHPEeVDYMTEFVIQEALEEHDKDGDGFISLEEFLGDY--RKDPTAnEDPEWIIVEKD-RFVND 210

                        90
                ....*....|....*.
gi 115763   148 FDsSEKDGQVTLAEFQ 163
Cdd:cd16224 211 YD-KDNDGKLDPQELL 225
PTZ00183 PTZ00183
centrin; Provisional
 70-162 7.93e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.13  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763     70 DRDGSGTLDLEEFLRALRPPMSQ--AREAvIAAAFAKLDRSGDGVVTVDDLRGVYSgrthpkvQSGEWTEEEVLRRFLDN 147
Cdd:PTZ00183  63 DKDGSGKIDFEEFLDIMTKKLGErdPREE-ILKAFRLFDDDKTGKISLKNLKRVAK-------ELGETITDEELQEMIDE 134

                         90
                 ....*....|....*
gi 115763    148 FDsSEKDGQVTLAEF 162
Cdd:PTZ00183 135 AD-RNGDGEISEEEF 148
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 45-165 1.10e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 38.43  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115763    45 ELQRGLAELGLVLDTAEA-EGVCRRW---DRDGSGTLDLEEFLRALRPpmSQAREAVIAAAFA---KLDRSGDGVVTVDD 117
Cdd:cd16225 112 EKIKNNEELKLDEDDKEVlDRYKDRWsqaDEPEDGLLDVEEFLSFRHP--EHSRGMLKNMVKEilhDLDQDGDEKLTLDE 189

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 115763   118 LRGVYSGrTHPKVQSGEWTEEEVLRR--FLDNFDSSeKDGQVTLAEFQDY 165
Cdd:cd16225 190 FVSLPPG-TVEEQQAEDDDEWKKERKkeFEEVIDLN-HDGKVTKEELEEY 237
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 40-116 3.23e-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: 36.42  E-value: 3.23e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115763    40 SLDSRELQRGLAELGLVLDTAEAEGVCRRWDRDGSGTLDLEEFLRaLRPPMSQAReaviaAAFAKLDRSGDGVVTVD 116
Cdd:cd16185  82 RLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIE-LCIFLASAR-----NLFQAFDRQRTGRVTLD 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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