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Conserved domains on  [gi|146229342|ref|NP_067624|]
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myosin regulatory light chain 10 isoform 1 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

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
PTZ00184 super family cl33172
calmodulin; Provisional
 1-137 6.06e-22

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 85.20  E-value: 6.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   1 MFDQSQIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDP 76
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 146229342  77 EETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 137
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-137 6.06e-22

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 85.20  E-value: 6.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   1 MFDQSQIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDP 76
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 146229342  77 EETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 137
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-126 1.90e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.40  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   6 QIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRinvknEELEAMVKEAPGPINFTVFLTMFgEKLKGTDPEETILHAFK 85
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 146229342  86 VFDTEGKGFVKADFIKEklMTQADRFSEEEVKQMFAAFPPD 126
Cdd:COG5126   77 LLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTD 115
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 8-76 4.54e-05

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 39.25  E-value: 4.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146229342   8 QEFKEAFTIMDQNRDGFIDKEDLRDTFAALGrINVKNEELEAMvkeaPGPINFTVFLTMFGEKLKGTDP 76
Cdd:cd22949    3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EF-hand_6 pfam13405
EF-hand domain;
9-38 3.20e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 3.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 146229342    9 EFKEAFTIMDQNRDGFIDKEDLRDTFAALG 38
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 9-37 3.93e-04

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: 3.93e-04
                           10        20
                   ....*....|....*....|....*....
gi 146229342     9 EFKEAFTIMDQNRDGFIDKEDLRDTFAAL 37
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-137 6.06e-22

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 85.20  E-value: 6.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   1 MFDQSQIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDP 76
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 146229342  77 EETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 137
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
PTZ00183 PTZ00183
centrin; Provisional
 2-119 5.97e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 59.70  E-value: 5.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   2 FDQSQIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGrINVKNEELEAMV----KEAPGPINFTVFLTMFGEKLKGTDPE 77
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPR 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 146229342  78 ETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQM 119
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEM 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-126 1.90e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.40  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   6 QIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRinvknEELEAMVKEAPGPINFTVFLTMFgEKLKGTDPEETILHAFK 85
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 146229342  86 VFDTEGKGFVKADFIKEklMTQADRFSEEEVKQMFAAFPPD 126
Cdd:COG5126   77 LLDTDGDGKISADEFRR--LLTALGVSEEEADELFARLDTD 115
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 8-76 4.54e-05

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 39.25  E-value: 4.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146229342   8 QEFKEAFTIMDQNRDGFIDKEDLRDTFAALGrINVKNEELEAMvkeaPGPINFTVFLTMFGEKLKGTDP 76
Cdd:cd22949    3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 9-54 6.15e-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: 38.68  E-value: 6.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 146229342   9 EFKEAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKEA 54
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREV 45
EF-hand_6 pfam13405
EF-hand domain;
9-38 3.20e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 3.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 146229342    9 EFKEAFTIMDQNRDGFIDKEDLRDTFAALG 38
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 9-37 3.93e-04

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: 3.93e-04
                           10        20
                   ....*....|....*....|....*....
gi 146229342     9 EFKEAFTIMDQNRDGFIDKEDLRDTFAAL 37
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-54 6.73e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 6.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 146229342   1 MFDQSQIQEFKEAFTIMDQNRDGFIDKEDLRdtfAALGRINVKNEELEAMVKEA 54
Cdd:COG5126   62 LFEATVEPFARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARL 112
EF-hand_7 pfam13499
EF-hand domain pair;
7-67 9.04e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 9.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146229342    7 IQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGR-INVKNEELEAMVKEAP----GPINFTVFLTMF 67
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 9-137 1.09e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.19  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146229342   9 EFKEAFTIMDQNRDGFIDKEDLRdTFAALGRINVKNEELEAMVK----EAPGPINFTVFLTM--FGEKLKGtdpeetilh 82
Cdd:cd16185    1 ELRQWFRAVDRDRSGSIDVNELQ-KALAGGGLLFSLATAEKLIRmfdrDGNGTIDFEEFAALhqFLSNMQN--------- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 146229342  83 AFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNL---DYRNLC 137
Cdd:cd16185   71 GFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLgfdDYIELC 128
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 9-37 2.38e-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: 33.91  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|....*....
gi 146229342    9 EFKEAFTIMDQNRDGFIDKEDLRDTFAAL 37
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
PTZ00183 PTZ00183
centrin; Provisional
 75-141 9.71e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 34.66  E-value: 9.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146229342  75 DPEETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLCYVIT 141
Cdd:PTZ00183  14 DQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMT 80
 
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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