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Conserved domains on  [gi|1025812257|ref|NP_001311388|]
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myosin regulatory light chain 11 [Homo sapiens]

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
 21-157 2.11e-18

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 77.11  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  21 MFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRlNVKNEELDAMMKE----ASGPINFTVFLTMFGEKLKGADP 96
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025812257  97 EDVITGAFKVLDPEGKGTIKKKFLEELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNIC 157
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 21-157 2.11e-18

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 77.11  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  21 MFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRlNVKNEELDAMMKE----ASGPINFTVFLTMFGEKLKGADP 96
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025812257  97 EDVITGAFKVLDPEGKGTIKKKFLEELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNIC 157
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
25-153 2.23e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  25 TQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVknEELDAmmkEASGPINFTVFLTMFgEKLKGADPEDVITGAF 104
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLF--SEADT---DGDGRISREEFVAGM-ESLFEATVEPFARAAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1025812257 105 KVLDPEGKGTIKKKFLEELLTTQcdRFSQEEIKNMWAAFPPDVGGNVDY 153
Cdd:COG5126    76 DLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISF 122
EF-hand_6 pfam13405
EF-hand domain;
29-58 4.13e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 4.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1025812257  29 EFKEAFTVIDQNRDGIIDKEDLRDTFAAMG 58
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 27-123 4.44e-04

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: 38.95  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  27 IQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMG-RLNvkNEELDAMMK---EASGPINFTVFLTMFgEKLKGadpedvITG 102
Cdd:cd15897    69 IKAWQEIFRTYDTDGSGTIDSNELRQALSGAGyRLS--EQTYDIIIRrydRGRGNIDFDDFIQCC-VRLQR------LTD 139

                          90       100
                  ....*....|....*....|.
gi 1025812257 103 AFKVLDPEGKGTIKKKFLEEL 123
Cdd:cd15897   140 AFRRYDKDQDGQIQVNYDEFL 160
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 29-57 1.20e-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: 34.66  E-value: 1.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 1025812257   29 EFKEAFTVIDQNRDGIIDKEDLRDTFAAM 57
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 21-157 2.11e-18

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 77.11  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  21 MFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRlNVKNEELDAMMKE----ASGPINFTVFLTMFGEKLKGADP 96
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025812257  97 EDVITGAFKVLDPEGKGTIKKKFLEELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNIC 157
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
PTZ00183 PTZ00183
centrin; Provisional
 26-139 1.08e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 62.01  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  26 QIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGrLNVKNEELDAMM----KEASGPINFTVFLTMFGEKLKGADPEDVIT 101
Cdd:PTZ00183   15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEIL 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1025812257 102 GAFKVLDPEGKGTIKKKFLEELLTTQCDRFSQEEIKNM 139
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEM 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
25-153 2.23e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  25 TQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVknEELDAmmkEASGPINFTVFLTMFgEKLKGADPEDVITGAF 104
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLF--SEADT---DGDGRISREEFVAGM-ESLFEATVEPFARAAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1025812257 105 KVLDPEGKGTIKKKFLEELLTTQcdRFSQEEIKNMWAAFPPDVGGNVDY 153
Cdd:COG5126    76 DLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISF 122
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
20-89 1.45e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025812257  20 SMFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRdtfAAMGRLNVKNEELDAMMKEA----SGPINFTVFLTMFGE 89
Cdd:COG5126    61 SLFEATVEPFARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARLdtdgDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
29-58 4.13e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 4.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1025812257  29 EFKEAFTVIDQNRDGIIDKEDLRDTFAAMG 58
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 27-123 4.44e-04

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: 38.95  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025812257  27 IQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMG-RLNvkNEELDAMMK---EASGPINFTVFLTMFgEKLKGadpedvITG 102
Cdd:cd15897    69 IKAWQEIFRTYDTDGSGTIDSNELRQALSGAGyRLS--EQTYDIIIRrydRGRGNIDFDDFIQCC-VRLQR------LTD 139

                          90       100
                  ....*....|....*....|.
gi 1025812257 103 AFKVLDPEGKGTIKKKFLEEL 123
Cdd:cd15897   140 AFRRYDKDQDGQIQVNYDEFL 160
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 29-57 1.20e-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: 34.66  E-value: 1.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 1025812257   29 EFKEAFTVIDQNRDGIIDKEDLRDTFAAM 57
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_7 pfam13499
EF-hand domain pair;
27-87 1.34e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 1.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025812257  27 IQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGR-LNVKNEELDAMMKEA----SGPINFTVFLTMF 87
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFdldkDGRISFEEFLELY 66
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 29-57 4.51e-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: 33.14  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|....*....
gi 1025812257  29 EFKEAFTVIDQNRDGIIDKEDLRDTFAAM 57
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_8 pfam13833
EF-hand domain pair;
42-87 4.88e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 33.83  E-value: 4.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1025812257  42 DGIIDKEDLRDTFAAMGRLNVKNEELDAMMKEA----SGPINFTVFLTMF 87
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 28-96 5.12e-03

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: 33.86  E-value: 5.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025812257  28 QEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGrLNVKNEELDAMmkeaSGPINFTVFLTMFGEKLKGADP 96
Cdd:cd22949     3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
 
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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