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Conserved domains on  [gi|1734336587|ref|NP_001360535|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11656625)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
172-432 1.32e-38

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: 136.97  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 172 AFRIAFLMFDEDDNGNIDRDEFMLIRSLTSSlrsttrvQPSTASDEEDRrescqldaadyhfavsrigadrlftgadsya 251
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRS-------QTSVGQRHRDH------------------------------- 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 252 vmfTKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysivnfdd 331
Cdd:cd15900    43 ---TNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI---------------------------------- 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 332 yhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIF 411
Cdd:cd15900    86 ----------------------------------DDVDTALTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIF 131
                         250       260
                  ....*....|....*....|.
gi 1734336587 412 DENNDGTLSYPEFLAVMSDRL 432
Cdd:cd15900   132 DEDGDGILSHKEFISVMKDRL 152
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
142-194 1.40e-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.


The actual alignment was detected with superfamily member cd00051:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734336587 142 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 194
Cdd:cd00051     3 REAFRLFDkdGDGTISADELKAALKSLgeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
 
Name Accession Description Interval E-value
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
172-432 1.32e-38

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: 136.97  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 172 AFRIAFLMFDEDDNGNIDRDEFMLIRSLTSSlrsttrvQPSTASDEEDRrescqldaadyhfavsrigadrlftgadsya 251
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRS-------QTSVGQRHRDH------------------------------- 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 252 vmfTKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysivnfdd 331
Cdd:cd15900    43 ---TNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI---------------------------------- 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 332 yhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIF 411
Cdd:cd15900    86 ----------------------------------DDVDTALTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIF 131
                         250       260
                  ....*....|....*....|.
gi 1734336587 412 DENNDGTLSYPEFLAVMSDRL 432
Cdd:cd15900   132 DEDGDGILSHKEFISVMKDRL 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
332-430 1.30e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 332 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 406
Cdd:COG5126    31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107
                          90       100
                  ....*....|....*....|....
gi 1734336587 407 IFRIFDENNDGTLSYPEFLAVMSD 430
Cdd:COG5126   108 LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
395-429 8.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 8.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1734336587 395 IGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 429
Cdd:pfam13499  33 EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
406-429 1.06e-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: 36.20  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....
gi 1734336587  406 MIFRIFDENNDGTLSYPEFLAVMS 429
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
142-194 1.40e-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: 36.76  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734336587 142 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 194
Cdd:cd00051     3 REAFRLFDkdGDGTISADELKAALKSLgeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
148-194 4.06e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1734336587 148 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 194
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, ...
172-432 1.32e-38

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: 136.97  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 172 AFRIAFLMFDEDDNGNIDRDEFMLIRSLTSSlrsttrvQPSTASDEEDRrescqldaadyhfavsrigadrlftgadsya 251
Cdd:cd15900     1 HFEIAFKMFDLDGDGELDKEEFNKVQSIIRS-------QTSVGQRHRDH------------------------------- 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 252 vmfTKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysivnfdd 331
Cdd:cd15900    43 ---TNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI---------------------------------- 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 332 yhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIF 411
Cdd:cd15900    86 ----------------------------------DDVDTALTFYHLAGASIDRKTFKRAAKVVAGVELSDHVVDVVFTIF 131
                         250       260
                  ....*....|....*....|.
gi 1734336587 412 DENNDGTLSYPEFLAVMSDRL 432
Cdd:cd15900   132 DEDGDGILSHKEFISVMKDRL 152
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
173-432 3.44e-14

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: 69.08  E-value: 3.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 173 FRIAFLMFDEDDNGNIDRDEFMLIRSLTSslrsttrvqpstasdeedrrescqldaadyhfavsrigadrlftgadsyav 252
Cdd:cd16175     2 FRIAFNMFDTDGNEMVDKKEFLVLQEIFR--------------------------------------------------- 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 253 mftkseeevrkqdtTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysivnfddy 332
Cdd:cd16175    31 --------------TLLVHFFGKKGKAELNFEDFYRFMDNLQTEV----------------------------------- 61
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 333 hkylqrvqeksdDDepgislsqwatfsrflnnlaeFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFD 412
Cdd:cd16175    62 ------------ED---------------------FTIAMRMYTFADRSISQDEFARAVKVCTGLKLSPHLVNTVFKIFD 108
                         250       260
                  ....*....|....*....|
gi 1734336587 413 ENNDGTLSYPEFLAVMSDRL 432
Cdd:cd16175   109 VDGDGQLSYKEFIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
173-432 1.53e-12

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: 65.28  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 173 FRIAFLMFDEDDNGNIDRDEFMLIRSLTSSLRSTTRvQPSTASDEEDRRESCQLDaadyhfavsrigadrlftgadsyav 252
Cdd:cd16174     2 FHIAFKMLDTDGNEQVEKREFFKLQKIIGKKDDLMT-QGGTETYQEASDNSDEVN------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 253 mftkseeevrkqdTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysivnfddy 332
Cdd:cd16174    56 -------------TTLQVHFFGKDGNEKLQYKEFCRFMENLQTEV----------------------------------- 87
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 333 hkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFD 412
Cdd:cd16174    88 ---------------------------------EDFAIAMKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDTVFKIFD 134
                         250       260
                  ....*....|....*....|
gi 1734336587 413 ENNDGTLSYPEFLAVMSDRL 432
Cdd:cd16174   135 LDGDDCLSHGEFLGVLKNRV 154
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
332-430 1.30e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734336587 332 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 406
Cdd:COG5126    31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107
                          90       100
                  ....*....|....*....|....
gi 1734336587 407 IFRIFDENNDGTLSYPEFLAVMSD 430
Cdd:COG5126   108 LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
395-429 8.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 8.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1734336587 395 IGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 429
Cdd:pfam13499  33 EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
406-429 1.06e-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: 36.20  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....
gi 1734336587  406 MIFRIFDENNDGTLSYPEFLAVMS 429
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
142-194 1.40e-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: 36.76  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734336587 142 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 194
Cdd:cd00051     3 REAFRLFDkdGDGTISADELKAALKSLgeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
404-430 2.47e-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: 35.45  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|....*..
gi 1734336587 404 VSMIFRIFDENNDGTLSYPEFLAVMSD 430
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
367-429 2.50e-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: 36.37  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734336587 367 EFQSAVRLY-VNSNVPVSEPEFARAVGCtIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 429
Cdd:cd00051     1 ELREAFRLFdKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_8 pfam13833
EF-hand domain pair;
404-431 2.96e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....*...
gi 1734336587 404 VSMIFRIFDENNDGTLSYPEFLAVMSDR 431
Cdd:pfam13833  27 VDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
148-194 4.06e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1734336587 148 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 194
Cdd:COG5126    80 TDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
 
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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