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Conserved domains on  [gi|164664497|ref|NP_001106858|]
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myosin light chain 1/3, skeletal muscle isoform isoform 3f [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
 4-149 4.67e-34

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 116.40  E-value: 4.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   4 SADQIADFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQG 83
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664497  84 GYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 149
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 4-149 4.67e-34

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 116.40  E-value: 4.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   4 SADQIADFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQG 83
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664497  84 GYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 149
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-148 3.52e-08

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: 47.54  E-value: 3.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164664497  87 DFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLA-GQEDSNGCINYEAFVKHIM 148
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-149 5.73e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   7 QIADFKEAFLLFDRTGECKITLSQvgdvLRALGTNPTNAEVKKVLGNPSNeemnakKIEFEQFLPMMQAISnnkDQGGYE 86
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDD----FEALFRRLWATLFSEADTDGDG------RISREEFVAGMESLF---EATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164664497  87 DFVEGLRVFDKEGNGTVMGAELRHVLATLGekMKEEEVEALLAgQEDSN--GCINYEAFVKHIMS 149
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFA-RLDTDgdGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
93-148 9.38e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 33.00  E-value: 9.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164664497   93 RVFDKEGNGTVMGAELRHVLATL--GEKMKEEEVEALLagQE---DSNGCINYEAFVKHIM 148
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELF--KEfdlDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 4-149 4.67e-34

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 116.40  E-value: 4.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   4 SADQIADFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQG 83
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164664497  84 GYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 149
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
PTZ00183 PTZ00183
centrin; Provisional
 1-148 9.58e-14

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 64.33  E-value: 9.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   1 MSFSADQIADFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEemNAKKIEFEQFLPMMQAISNNK 80
Cdd:PTZ00183   9 PGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMTKKLGER 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164664497  81 DQggYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEV-EALLAGQEDSNGCINYEAFVKhIM 148
Cdd:PTZ00183  87 DP--REEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELqEMIDEADRNGDGEISEEEFYR-IM 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-148 3.52e-08

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: 47.54  E-value: 3.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164664497  87 DFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLA-GQEDSNGCINYEAFVKHIM 148
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 11-79 1.73e-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: 1.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497  11 FKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEvKKVLGNpsneemnakKIEFEQFLP-MMQAISNN 79
Cdd:cd22949    5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDE-KDALPA---------SMNWDQFENwAKKKLAYS 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-149 5.73e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164664497   7 QIADFKEAFLLFDRTGECKITLSQvgdvLRALGTNPTNAEVKKVLGNPSNeemnakKIEFEQFLPMMQAISnnkDQGGYE 86
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDD----FEALFRRLWATLFSEADTDGDG------RISREEFVAGMESLF---EATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164664497  87 DFVEGLRVFDKEGNGTVMGAELRHVLATLGekMKEEEVEALLAgQEDSN--GCINYEAFVKHIMS 149
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFA-RLDTDgdGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 10-74 9.11e-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: 32.90  E-value: 9.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164664497  10 DFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgnpsnEEM---NAKKIEFEQFLPMMQ 74
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI-----REVdkdGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
93-148 9.38e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 33.00  E-value: 9.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164664497   93 RVFDKEGNGTVMGAELRHVLATL--GEKMKEEEVEALLagQE---DSNGCINYEAFVKHIM 148
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELF--KEfdlDKDGRISFEEFLELYS 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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