NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|94981553|ref|NP_000423|]
View 

myosin regulatory light chain 2, ventricular/cardiac muscle isoform isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 20-160 8.24e-25

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 93.29  E-value: 8.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553   20 MFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvNVKNEEIDEMIKE----APGPINFTVFLTMFGEKLKGADP 95
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94981553   96 EETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIIT 160
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 20-160 8.24e-25

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 93.29  E-value: 8.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553   20 MFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvNVKNEEIDEMIKE----APGPINFTVFLTMFGEKLKGADP 95
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94981553   96 EETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIIT 160
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-161 1.14e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553  24 TQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvnvknEEIDEMIKEAPGPINFTVFLTMFgEKLKGADPEETILNAF 103
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAF 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 94981553 104 KVFDPEGKGVLKADYVREMLTtqAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITH 161
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 28-73 1.07e-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: 43.69  E-value: 1.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 94981553  28 EFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvNVKNEEIDEMIKEA 73
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREV 45
EF-hand_7 pfam13499
EF-hand domain pair;
26-86 5.22e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 5.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94981553    26 IQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGR-VNVKNEEIDEMIKEAP----GPINFTVFLTMF 86
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 28-56 5.22e-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: 5.22e-04
                           10        20
                   ....*....|....*....|....*....
gi 94981553     28 EFKEAFTIMDQNRDGFIDKNDLRDTFAAL 56
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 20-160 8.24e-25

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 93.29  E-value: 8.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553   20 MFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvNVKNEEIDEMIKE----APGPINFTVFLTMFGEKLKGADP 95
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94981553   96 EETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIIT 160
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00183 PTZ00183
centrin; Provisional
 25-138 4.35e-14

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 65.87  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553   25 QIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGrVNVKNEEIDEMI----KEAPGPINFTVFLTMFGEKLKGADPEETIL 100
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEIL 93

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 94981553  101 NAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQM 138
Cdd:PTZ00183  94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEM 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-161 1.14e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94981553  24 TQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvnvknEEIDEMIKEAPGPINFTVFLTMFgEKLKGADPEETILNAF 103
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAF 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 94981553 104 KVFDPEGKGVLKADYVREMLTtqAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITH 161
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLLT--ALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 28-73 1.07e-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: 43.69  E-value: 1.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 94981553  28 EFKEAFTIMDQNRDGFIDKNDLRDTFAALGRvNVKNEEIDEMIKEA 73
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREV 45
EF-hand_7 pfam13499
EF-hand domain pair;
26-86 5.22e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 5.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94981553    26 IQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGR-VNVKNEEIDEMIKEAP----GPINFTVFLTMF 86
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 27-95 6.18e-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: 6.18e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94981553  27 QEFKEAFTIMDQNRDGFIDKNDLRDTFAALGrVNVKNEEIDEMikeaPGPINFTVFLTMFGEKLKGADP 95
Cdd:cd22949   3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
19-73 9.38e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 9.38e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 94981553  19 SMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRdtfAALGRVNVKNEEIDEMIKEA 73
Cdd:COG5126  61 SLFEATVEPFARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARL 112
EF-hand_6 pfam13405
EF-hand domain;
28-57 2.45e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.77  E-value: 2.45e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 94981553    28 EFKEAFTIMDQNRDGFIDKNDLRDTFAALG 57
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 28-56 5.22e-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: 5.22e-04
                           10        20
                   ....*....|....*....|....*....
gi 94981553     28 EFKEAFTIMDQNRDGFIDKNDLRDTFAAL 56
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 102-160 2.06e-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: 34.83  E-value: 2.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 94981553 102 AFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIIT 160
Cdd:cd00051   5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 28-56 2.67e-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: 2.67e-03
                          10        20
                  ....*....|....*....|....*....
gi 94981553    28 EFKEAFTIMDQNRDGFIDKNDLRDTFAAL 56
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH