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Conserved domains on  [gi|392921535|ref|NP_001256519|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

Protein Classification

calcium uptake protein( domain architecture ID 11610295)

mitochondrial calcium uptake protein (MICU) may act as a key regulator of mitochondrial calcium uniporter (MCU)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 170-370 1.10e-40

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


:

Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 141.21  E-value: 1.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 170 AFRIAFLMFDEDDNGNIDRDEFML-------------------KSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYEN 230
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNKvqsiirsqtsvgqrhrdhtNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 231 LQEELmeiefyefargktaispvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAV 310
Cdd:cd15900   81 LQEEI--------------------------------------------------------------------DDVDTAL 92

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 311 RLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 370
Cdd:cd15900   93 TFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
146-192 2.90e-03

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 392921535 146 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
Cdd:COG5126   80 TDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 170-370 1.10e-40

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 141.21  E-value: 1.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 170 AFRIAFLMFDEDDNGNIDRDEFML-------------------KSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYEN 230
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNKvqsiirsqtsvgqrhrdhtNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 231 LQEELmeiefyefargktaispvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAV 310
Cdd:cd15900   81 LQEEI--------------------------------------------------------------------DDVDTAL 92

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 311 RLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 370
Cdd:cd15900   93 TFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
270-368 7.55e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 270 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 344
Cdd:COG5126   31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107

                         90       100
                 ....*....|....*....|....
gi 392921535 345 IFRIFDENNDGTLSYPEFLAVMSD 368
Cdd:COG5126  108 LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
168-228 4.49e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 4.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392921535  168 KAAFRIAFLMFDEDDNGNIDRDEFM-----LKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFY 228
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKkllrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 344-367 1.28e-03

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: 35.82  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....
gi 392921535   344 MIFRIFDENNDGTLSYPEFLAVMS 367
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
146-192 2.90e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 392921535 146 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
Cdd:COG5126   80 TDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 170-370 1.10e-40

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 141.21  E-value: 1.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 170 AFRIAFLMFDEDDNGNIDRDEFML-------------------KSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYEN 230
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNKvqsiirsqtsvgqrhrdhtNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 231 LQEELmeiefyefargktaispvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAV 310
Cdd:cd15900   81 LQEEI--------------------------------------------------------------------DDVDTAL 92

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 311 RLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 370
Cdd:cd15900   93 TFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
 171-370 5.09e-21

EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and similar proteins; MICU3, also termed EF-hand domain-containing family member A2 (EFHA2), is a paralog of MICU1 and notably found in the central nervous system (CNS) and skeletal muscle. At present, the precise molecular function of MICU3 remains unclear. It likely has a role in mitochondrial calcium handling. MICU3 contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320083 [Multi-domain]  Cd Length: 128  Bit Score: 87.96  E-value: 5.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 171 FRIAFLMFDEDDNGNIDRDEFMLkseeeVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktai 250
Cdd:cd16175    2 FRIAFNMFDTDGNEMVDKKEFLV-----LQEIFRTLLVHFFGKKGKAELNFEDFYRFMDNLQTEV--------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 251 spvdfarlilrysivnfddyhkylqrvqeksdDDepgislsqwatfsrflnnlaeFQSAVRLYVNSNVPVSEPEFARAVG 330
Cdd:cd16175   62 --------------------------------ED---------------------FTIAMRMYTFADRSISQDEFARAVK 88

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392921535 331 CTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 370
Cdd:cd16175   89 VCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
 171-370 1.20e-14

EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and similar proteins; MICU2, also termed EF-hand domain-containing family member A1 (EFHA1), is a mitochondrial-localized paralog of MICU1. MICU2 and its paralog, MICU1, are physically associated within the mitochondrial calcium uniporter (MCU) complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. At present, the precise molecular function of MICU2 remains unclear. It may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU2 contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320082 [Multi-domain]  Cd Length: 154  Bit Score: 71.05  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 171 FRIAFLMFDEDDNGNIDRDEF------------MLKSEEEVRKQ---------DTTLLLHLFGLRGNATLSFDEFQQFYE 229
Cdd:cd16174    2 FHIAFKMLDTDGNEQVEKREFfklqkiigkkddLMTQGGTETYQeasdnsdevNTTLQVHFFGKDGNEKLQYKEFCRFME 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 230 NLQEELmeiefyefargktaispvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSA 309
Cdd:cd16174   82 NLQTEV--------------------------------------------------------------------EDFAIA 93

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921535 310 VRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 370
Cdd:cd16174   94 MKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFDLDGDDCLSHGEFLGVLKNRV 154
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
270-368 7.55e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 270 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 344
Cdd:COG5126   31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107

                         90       100
                 ....*....|....*....|....
gi 392921535 345 IFRIFDENNDGTLSYPEFLAVMSD 368
Cdd:COG5126  108 LFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 171-227 4.30e-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: 40.99  E-value: 4.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 171 FRIAFLMFDEDDNGNIDRDEF---MLKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQF 227
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELkaaLKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
168-228 4.49e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 4.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392921535  168 KAAFRIAFLMFDEDDNGNIDRDEFM-----LKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFY 228
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKkllrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EF-hand_7 pfam13499
EF-hand domain pair;
333-367 1.01e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 392921535  333 IGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 367
Cdd:pfam13499  33 EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 344-367 1.28e-03

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: 35.82  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....
gi 392921535   344 MIFRIFDENNDGTLSYPEFLAVMS 367
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 171-257 2.78e-03

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: 37.65  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 171 FRIAFLMFDEDDNGNIDRDEF--MLK------SEEEVRKqdttlLLHLFGLRGNATLSFDEFQQFYENL--QEELMEIeF 240
Cdd:cd15898    2 LRRQWIKADKDGDGKLSLKEIkkLLKrlnirvSEKELKK-----LFKEVDTNGDGTLTFDEFEELYKSLteRPELEPI-F 75

                         90
                 ....*....|....*...
gi 392921535 241 YEFA-RGKTAISPVDFAR 257
Cdd:cd15898   76 KKYAgTNRDYMTLEEFIR 93
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 342-368 2.79e-03

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: 35.07  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*..
gi 392921535  342 VSMIFRIFDENNDGTLSYPEFLAVMSD 368
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
146-192 2.90e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 392921535 146 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
Cdd:COG5126   80 TDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
EF-hand_8 pfam13833
EF-hand domain pair;
342-369 2.90e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|....*...
gi 392921535  342 VSMIFRIFDENNDGTLSYPEFLAVMSDR 369
Cdd:pfam13833  27 VDILFREFDTDGDGYISFDEFCVLLERR 54
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 305-367 3.07e-03

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: 35.99  E-value: 3.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921535 305 EFQSAVRLY-VNSNVPVSEPEFARAVGCtIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 367
Cdd:cd00051    1 ELREAFRLFdKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
135-227 3.65e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921535 135 FRSGGKHFFRTM------DQSGIISYSEYI-FLLTLLTKSKAAF-RIAFLMFDEDDNGNIDRDEFM-LKSEEEVRKQDTT 205
Cdd:COG5126   27 FEALFRRLWATLfseadtDGDGRISREEFVaGMESLFEATVEPFaRAAFDLLDTDGDGKISADEFRrLLTALGVSEEEAD 106

                         90       100
                 ....*....|....*....|..
gi 392921535 206 LLLHLFGLRGNATLSFDEFQQF 227
Cdd:COG5126  107 ELFARLDTDGDGKISFEEFVAA 128
 
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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