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Conserved domains on  [gi|114326499|ref|NP_075017|]
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myosin regulatory light chain 2, atrial isoform [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
 28-168 5.21e-23

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 89.05  E-value: 5.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  28 MFEQAQIQEFKEAFSCIDQNRDGIICKSDLKETYSQLGRvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326499 104 EEAILSAFRMFDPSGQGVVNKEEFKQLLMTQADKFSPAEVEQLFALTPMDLAGNIDYKSLCYIIT 168
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 28-168 5.21e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 89.05  E-value: 5.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  28 MFEQAQIQEFKEAFSCIDQNRDGIICKSDLKETYSQLGRvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326499 104 EEAILSAFRMFDPSGQGVVNKEEFKQLLMTQADKFSPAEVEQLFALTPMDLAGNIDYKSLCYIIT 168
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
33-157 1.27e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  33 QIQEFKEAFSCIDQNRDGIICKSDLketysQLGRVSVPEEELDAMLQEGKGPINFTVFLTlFGEKLNGTDPEEAILSAFR 112
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDF-----EALFRRLWATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 114326499 113 MFDPSGQGVVNKEEFKQLLmtQADKFSPAEVEQLFALtpMDLAGN 157
Cdd:COG5126   77 LLDTDGDGKISADEFRRLL--TALGVSEEEADELFAR--LDTDGD 117
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 36-132 2.07e-04

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: 37.91  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  36 EFKEAFSCIDQNRDGIICKSDLKETYSQLGRvSVPEEELDAMlqegkgpinftvfltlfgeklngtdpeeailsaFRMFD 115
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEM---------------------------------IREVD 46

                         90
                 ....*....|....*..
gi 114326499 116 PSGQGVVNKEEFKQLLM 132
Cdd:cd00051   47 KDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
104-168 2.82e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114326499  104 EEAILSAFRMFDPSGQGVVNKEEFKQLLMT--QADKFSPAEVEQLFALtpMDLAGN--IDYKSLCYIIT 168
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKleEGEPLSDEEVEELFKE--FDLDKDgrISFEEFLELYS 67
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 28-168 5.21e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 89.05  E-value: 5.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  28 MFEQAQIQEFKEAFSCIDQNRDGIICKSDLKETYSQLGRvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326499 104 EEAILSAFRMFDPSGQGVVNKEEFKQLLMTQADKFSPAEVEQLFALTPMDLAGNIDYKSLCYIIT 168
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00183 PTZ00183
centrin; Provisional
 33-120 3.36e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 55.85  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  33 QIQEFKEAFSCIDQNRDGIICKSDLKETYSQLGrVSVPEEELDAMLQ----EGKGPINFTVFLTLFGEKLNGTDPEEAIL 108
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIAdvdkDGSGKIDFEEFLDIMTKKLGERDPREEIL 93

                         90
                 ....*....|..
gi 114326499 109 SAFRMFDPSGQG 120
Cdd:PTZ00183  94 KAFRLFDDDKTG 105
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
33-157 1.27e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  33 QIQEFKEAFSCIDQNRDGIICKSDLketysQLGRVSVPEEELDAMLQEGKGPINFTVFLTlFGEKLNGTDPEEAILSAFR 112
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDF-----EALFRRLWATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 114326499 113 MFDPSGQGVVNKEEFKQLLmtQADKFSPAEVEQLFALtpMDLAGN 157
Cdd:COG5126   77 LLDTDGDGKISADEFRRLL--TALGVSEEEADELFAR--LDTDGD 117
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 36-132 2.07e-04

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: 37.91  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  36 EFKEAFSCIDQNRDGIICKSDLKETYSQLGRvSVPEEELDAMlqegkgpinftvfltlfgeklngtdpeeailsaFRMFD 115
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEM---------------------------------IREVD 46

                         90
                 ....*....|....*..
gi 114326499 116 PSGQGVVNKEEFKQLLM 132
Cdd:cd00051   47 KDGDGKIDFEEFLELMA 63
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 35-103 2.17e-04

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: 37.71  E-value: 2.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114326499  35 QEFKEAFSCIDQNRDGIICKSDLKETYSQLGrVSVPEEELDAMlqegKGPINFTVFLTLFGEKLNGTDP 103
Cdd:cd22949    3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EF-hand_7 pfam13499
EF-hand domain pair;
104-168 2.82e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114326499  104 EEAILSAFRMFDPSGQGVVNKEEFKQLLMT--QADKFSPAEVEQLFALtpMDLAGN--IDYKSLCYIIT 168
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKleEGEPLSDEEVEELFKE--FDLDKDgrISFEEFLELYS 67
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 34-132 1.03e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 37.80  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  34 IQEFKEAFSCIDQNRDGIICKSDLKETYSQLG-RVSvpEEELDAMLQ---EGKGPINFTVFLTLFgEKLngtdpeEAILS 109
Cdd:cd15897   69 IKAWQEIFRTYDTDGSGTIDSNELRQALSGAGyRLS--EQTYDIIIRrydRGRGNIDFDDFIQCC-VRL------QRLTD 139

                         90       100
                 ....*....|....*....|....*
gi 114326499 110 AFRMFDPSGQGV--VNKEEFKQLLM 132
Cdd:cd15897  140 AFRRYDKDQDGQiqVNYDEFLQGTM 164
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 110-168 1.22e-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: 35.60  E-value: 1.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114326499 110 AFRMFDPSGQGVVNKEEFKQLLMTQADKFSPAEVEQLFALtpMDLAGN--IDYKSLCYIIT 168
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIRE--VDKDGDgkIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-132 1.45e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499  27 SMFEQAQIQEFKEAFSCIDQNRDGIICKSDLKETYSQLGrvsVPEEELDAMlqegkgpinftvfltlfgeklngtdpeea 106
Cdd:COG5126   61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG---VSEEEADEL----------------------------- 108

                         90       100
                 ....*....|....*....|....*.
gi 114326499 107 ilsaFRMFDPSGQGVVNKEEFKQLLM 132
Cdd:COG5126  109 ----FARLDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
34-132 1.82e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.31  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326499   34 IQEFKEAFSCIDQNRDGIICKSDLKETYSQLGRvsvpeeeldamlqegkgpinftvfltlfGEKLngtdPEEAILSAFRM 113
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE----------------------------GEPL----SDEEVEELFKE 48

                          90
                  ....*....|....*....
gi 114326499  114 FDPSGQGVVNKEEFKQLLM 132
Cdd:pfam13499  49 FDLDKDGRISFEEFLELYS 67
 
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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