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Conserved domains on  [gi|442619983|ref|NP_001262743|]
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mitochondrial calcium uptake 3, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_MICU super family cl28896
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
191-473 9.39e-51

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.


The actual alignment was detected with superfamily member cd16175:

Pssm-ID: 333716 [Multi-domain]  Cd Length: 128  Bit Score: 169.23  E-value: 9.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 191 GFRIAFNMFDTDGNQRVDKDEFLVIISILAgalkdtqnvdpqtkrilsrlvsydeqsqmtkpmavpqakrgimerifsga 270
Cdd:cd16175    1 GFRIAFNMFDTDGNEMVDKKEFLVLQEIFR-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 271 wkekhgeqepeeelatptplenyvndgeglqrrhmvatTLQLHFFGKRGTGVINYDNFYRFMDNLQTEVlelefhefskg 350
Cdd:cd16175   31 --------------------------------------TLLVHFFGKKGKAELNFEDFYRFMDNLQTEV----------- 61
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 351 nsviseldfakillrytylatdeydvflerllervkdekgisfhdfrdfchflnnlDDFTIAMRMYTLADRAISKDEFSR 430
Cdd:cd16175   62 --------------------------------------------------------EDFTIAMRMYTFADRSISQDEFAR 85
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442619983 431 AVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd16175   86 AVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
 
Name Accession Description Interval E-value
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
191-473 9.39e-51

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: 169.23  E-value: 9.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 191 GFRIAFNMFDTDGNQRVDKDEFLVIISILAgalkdtqnvdpqtkrilsrlvsydeqsqmtkpmavpqakrgimerifsga 270
Cdd:cd16175    1 GFRIAFNMFDTDGNEMVDKKEFLVLQEIFR-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 271 wkekhgeqepeeelatptplenyvndgeglqrrhmvatTLQLHFFGKRGTGVINYDNFYRFMDNLQTEVlelefhefskg 350
Cdd:cd16175   31 --------------------------------------TLLVHFFGKKGKAELNFEDFYRFMDNLQTEV----------- 61
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 351 nsviseldfakillrytylatdeydvflerllervkdekgisfhdfrdfchflnnlDDFTIAMRMYTLADRAISKDEFSR 430
Cdd:cd16175   62 --------------------------------------------------------EDFTIAMRMYTFADRSISQDEFAR 85
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442619983 431 AVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd16175   86 AVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
335-471 5.60e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 335 LQTEVLELEFHEF-SKGNSVISELDFAKILLRYTYLATDEYDVflerllerVKDEKgISFHDFRDFCHFLNNLDDFTIAM 413
Cdd:COG5126    2 LQRRKLDRRFDLLdADGDGVLERDDFEALFRRLWATLFSEADT--------DGDGR-ISREEFVAGMESLFEATVEPFAR 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619983 414 RMYTLADR----AISKDEFSRAVkicTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKD 471
Cdd:COG5126   73 AAFDLLDTdgdgKISADEFRRLL---TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
420-470 5.63e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 5.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442619983  420 DRAISKDEFSRAV-KICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMK 470
Cdd:pfam13499  16 DGYLDVEELKKLLrKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
445-470 1.89e-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: 1.89e-03
                           10        20
                   ....*....|....*....|....*.
gi 442619983   445 IDTVFAIFDADGDGLLSYKEFIAIMK 470
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
EFh_MICU3 cd16175
EF-hand, calcium binding motif, found in calcium uptake protein 3, mitochondrial (MICU3) and ...
191-473 9.39e-51

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: 169.23  E-value: 9.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 191 GFRIAFNMFDTDGNQRVDKDEFLVIISILAgalkdtqnvdpqtkrilsrlvsydeqsqmtkpmavpqakrgimerifsga 270
Cdd:cd16175    1 GFRIAFNMFDTDGNEMVDKKEFLVLQEIFR-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 271 wkekhgeqepeeelatptplenyvndgeglqrrhmvatTLQLHFFGKRGTGVINYDNFYRFMDNLQTEVlelefhefskg 350
Cdd:cd16175   31 --------------------------------------TLLVHFFGKKGKAELNFEDFYRFMDNLQTEV----------- 61
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 351 nsviseldfakillrytylatdeydvflerllervkdekgisfhdfrdfchflnnlDDFTIAMRMYTLADRAISKDEFSR 430
Cdd:cd16175   62 --------------------------------------------------------EDFTIAMRMYTFADRSISQDEFAR 85
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442619983 431 AVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd16175   86 AVKVCTGLKLSPHLVNTVFKIFDVDGDGQLSYKEFIGIMKDRL 128
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
191-473 1.85e-42

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: 148.15  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 191 GFRIAFNMFDTDGNQRVDKDEFLViisilagalkdtqnvdpqtkrilsrlvsydeqsqmtkpmavpqakrgiMERIFSGA 270
Cdd:cd15900    1 HFEIAFKMFDLDGDGELDKEEFNK------------------------------------------------VQSIIRSQ 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 271 WKEKHGEQEPEEelatptplenyvndgeGLQRRHMVATTLQLHFFGKRGTGVINYDNFYRFMDNLQTEVlelefhefskg 350
Cdd:cd15900   33 TSVGQRHRDHTN----------------GESTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENLQEEI----------- 85
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 351 nsviseldfakillrytylatdeydvflerllervkdekgisfhdfrdfchflnnlDDFTIAMRMYTLADRAISKDEFSR 430
Cdd:cd15900   86 --------------------------------------------------------DDVDTALTFYHLAGASIDRKTFKR 109
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442619983 431 AVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd15900  110 AAKVVAGVELSDHVVDVVFTIFDEDGDGILSHKEFISVMKDRL 152
EFh_MICU2 cd16174
EF-hand, calcium binding motif, found in calcium uptake protein 2, mitochondrial (MICU2) and ...
191-473 9.01e-28

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: 108.42  E-value: 9.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 191 GFRIAFNMFDTDGNQRVDKDEFLviisilagalkdtqnvdpQTKRILSRlvsydEQSQMTKPMAVPQakrgimerifsga 270
Cdd:cd16174    1 GFHIAFKMLDTDGNEQVEKREFF------------------KLQKIIGK-----KDDLMTQGGTETY------------- 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 271 wkekhgeQEPEEElatptplENYVNdgeglqrrhmvaTTLQLHFFGKRGTGVINYDNFYRFMDNLQTEVlelefhefskg 350
Cdd:cd16174   45 -------QEASDN-------SDEVN------------TTLQVHFFGKDGNEKLQYKEFCRFMENLQTEV----------- 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 351 nsviseldfakillrytylatdeydvflerllervkdekgisfhdfrdfchflnnlDDFTIAMRMYTLADRAISKDEFSR 430
Cdd:cd16174   88 --------------------------------------------------------EDFAIAMKMFSEANRPIKLAEFKR 111
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442619983 431 AVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd16174  112 AVKVATGQELSDNVLDTVFKIFDLDGDDCLSHGEFLGVLKNRV 154
EFh_MICU1 cd16173
EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and ...
404-473 4.78e-09

EF-hand, calcium binding motif, found in calcium uptake protein 1, mitochondrial (MICU1) and similar proteins; MICU1, also termed atopy-related autoantigen CALC (ara CALC), or calcium-binding atopy-related autoantigen 1 (CBARA1), or Hom s 4, or EFHA3, 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 its paralog, MICU2, are physically associated within the uniporter complex and are co-expressed across all tissues. They may operate together with MCU to regulate the channel. The mutations in MICU1 are associated with neuromuscular abnormalities in children. MICU1 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: 320081 [Multi-domain]  Cd Length: 153  Bit Score: 55.41  E-value: 4.78e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 404 NNLDDFTIAMRMYTLADRAISKDEFSRAVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDRL 473
Cdd:cd16173   84 HDVNDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVAIMKQRL 153
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
335-471 5.60e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619983 335 LQTEVLELEFHEF-SKGNSVISELDFAKILLRYTYLATDEYDVflerllerVKDEKgISFHDFRDFCHFLNNLDDFTIAM 413
Cdd:COG5126    2 LQRRKLDRRFDLLdADGDGVLERDDFEALFRRLWATLFSEADT--------DGDGR-ISREEFVAGMESLFEATVEPFAR 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619983 414 RMYTLADR----AISKDEFSRAVkicTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKD 471
Cdd:COG5126   73 AAFDLLDTdgdgKISADEFRRLL---TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
420-470 5.63e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 5.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442619983  420 DRAISKDEFSRAV-KICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMK 470
Cdd:pfam13499  16 DGYLDVEELKKLLrKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
420-470 5.22e-06

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: 44.08  E-value: 5.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442619983 420 DRAISKDEFSRAVKiCTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMK 470
Cdd:cd00051   14 DGTISADELKAALK-SLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_8 pfam13833
EF-hand domain pair;
423-472 8.00e-06

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 43.07  E-value: 8.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442619983  423 ISKDEFSRAVKICTGYKLSPHLIDTVFAIFDADGDGLLSYKEFIAIMKDR 472
Cdd:pfam13833   5 ITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
445-471 4.65e-04

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: 37.38  E-value: 4.65e-04
                          10        20
                  ....*....|....*....|....*..
gi 442619983  445 IDTVFAIFDADGDGLLSYKEFIAIMKD 471
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
445-470 1.89e-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: 1.89e-03
                           10        20
                   ....*....|....*....|....*.
gi 442619983   445 IDTVFAIFDADGDGLLSYKEFIAIMK 470
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
448-470 2.45e-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: 2.45e-03
                         10        20
                 ....*....|....*....|...
gi 442619983 448 VFAIFDADGDGLLSYKEFIAIMK 470
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALK 27
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
195-219 7.93e-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: 33.89  E-value: 7.93e-03
                           10        20
                   ....*....|....*....|....*
gi 442619983   195 AFNMFDTDGNQRVDKDEFLVIISIL 219
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDLLKAL 29
 
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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