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Conserved domains on  [gi|392921541|ref|NP_001256522|]
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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, ...
170-449 4.67e-39

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: 138.52  E-value: 4.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 170 AFRIAFLMFDEDDNGNIDRDEFMlirsltsslrsttrvqpstasdeedrrescqldaadyhfavsrigadrlftgadsya 249
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFN--------------------------------------------------------- 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 250 vmfTIARMFASKAATLSGTRLVHKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktai 329
Cdd:cd15900   24 ---KVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI--------------- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 330 spvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVG 409
Cdd:cd15900   86 -----------------------------------------------------DDVDTALTFYHLAGASIDRKTFKRAAK 112
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 392921541 410 CTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 449
Cdd:cd15900  113 VVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
140-192 1.19e-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: 37.14  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392921541 140 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
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, ...
170-449 4.67e-39

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: 138.52  E-value: 4.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 170 AFRIAFLMFDEDDNGNIDRDEFMlirsltsslrsttrvqpstasdeedrrescqldaadyhfavsrigadrlftgadsya 249
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFN--------------------------------------------------------- 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 250 vmfTIARMFASKAATLSGTRLVHKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktai 329
Cdd:cd15900   24 ---KVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI--------------- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 330 spvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVG 409
Cdd:cd15900   86 -----------------------------------------------------DDVDTALTFYHLAGASIDRKTFKRAAK 112
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 392921541 410 CTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 449
Cdd:cd15900  113 VVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
349-447 1.33e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 349 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 423
Cdd:COG5126   31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107
                         90       100
                 ....*....|....*....|....
gi 392921541 424 IFRIFDENNDGTLSYPEFLAVMSD 447
Cdd:COG5126  108 LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
412-446 7.57e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 392921541  412 IGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 446
Cdd:pfam13499  33 EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
423-446 1.03e-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: 36.59  E-value: 1.03e-03
                           10        20
                   ....*....|....*....|....
gi 392921541   423 MIFRIFDENNDGTLSYPEFLAVMS 446
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
140-192 1.19e-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: 37.14  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392921541 140 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
Cdd:cd00051    3 REAFRLFDkdGDGTISADELKAALKSLgeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
146-192 4.19e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 392921541 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, ...
170-449 4.67e-39

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: 138.52  E-value: 4.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 170 AFRIAFLMFDEDDNGNIDRDEFMlirsltsslrsttrvqpstasdeedrrescqldaadyhfavsrigadrlftgadsya 249
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFN--------------------------------------------------------- 23
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 250 vmfTIARMFASKAATLSGTRLVHKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktai 329
Cdd:cd15900   24 ---KVQSIIRSQTSVGQRHRDHTNGESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI--------------- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 330 spvdfarlilrysivnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVG 409
Cdd:cd15900   86 -----------------------------------------------------DDVDTALTFYHLAGASIDRKTFKRAAK 112
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 392921541 410 CTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 449
Cdd:cd15900  113 VVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
375-449 1.08e-13

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: 67.93  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392921541 375 FSRFLNNLA----EFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDRL 449
Cdd:cd16175   50 FYRFMDNLQteveDFTIAMRMYTFADRSISQDEFARAVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
264-449 1.92e-11

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: 62.20  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 264 TLSGTRLVHKSEEEVRKQDTTLLLHLFGLRGNATLSFDEFQQFYENLQEELmeiefyefargktaispvdfarlilrysi 343
Cdd:cd16174   37 TQGGTETYQEASDNSDEVNTTLQVHFFGKDGNEKLQYKEFCRFMENLQTEV----------------------------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 344 vnfddyhkylqrvqeksdddepgislsqwatfsrflnnlAEFQSAVRLYVNSNVPVSEPEFARAVGCTIGKELDPVVVSM 423
Cdd:cd16174   88 ---------------------------------------EDFAIAMKMFSEANRPIKLAEFKRAVKVATGQELSDNVLDT 128
                        170       180
                 ....*....|....*....|....*.
gi 392921541 424 IFRIFDENNDGTLSYPEFLAVMSDRL 449
Cdd:cd16174  129 VFKIFDLDGDDCLSHGEFLGVLKNRV 154
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
349-447 1.33e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921541 349 YHKYLQRVQEKSDDDEPG-ISLSQWATF--SRFLNNLAEF-QSAVRLY-VNSNVPVSEPEFARAVGctiGKELDPVVVSM 423
Cdd:COG5126   31 FRRLWATLFSEADTDGDGrISREEFVAGmeSLFEATVEPFaRAAFDLLdTDGDGKISADEFRRLLT---ALGVSEEEADE 107
                         90       100
                 ....*....|....*....|....
gi 392921541 424 IFRIFDENNDGTLSYPEFLAVMSD 447
Cdd:COG5126  108 LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
412-446 7.57e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 392921541  412 IGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 446
Cdd:pfam13499  33 EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
423-446 1.03e-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: 36.59  E-value: 1.03e-03
                           10        20
                   ....*....|....*....|....
gi 392921541   423 MIFRIFDENNDGTLSYPEFLAVMS 446
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
140-192 1.19e-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: 37.14  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392921541 140 KHFFRTMD--QSGIISYSEYIFLLTLL--TKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
Cdd:cd00051    3 REAFRLFDkdGDGTISADELKAALKSLgeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
384-446 2.24e-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: 2.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921541 384 EFQSAVRLY-VNSNVPVSEPEFARAVGCtIGKELDPVVVSMIFRIFDENNDGTLSYPEFLAVMS 446
Cdd:cd00051    1 ELREAFRLFdKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
421-447 2.27e-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: 2.27e-03
                          10        20
                  ....*....|....*....|....*..
gi 392921541  421 VSMIFRIFDENNDGTLSYPEFLAVMSD 447
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EF-hand_8 pfam13833
EF-hand domain pair;
414-448 2.82e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 2.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 392921541  414 KELDPVVVSMIFRIFDENNDGTLSYPEFLAVMSDR 448
Cdd:pfam13833  20 KDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
146-192 4.19e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 392921541 146 MDQSGIISYSEYIFLLTLLTKSKAAFRIAFLMFDEDDNGNIDRDEFM 192
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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