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Conserved domains on  [gi|672065823|ref|XP_008765516|]
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myosin light chain 1/3, skeletal muscle isoform isoform X1 [Rattus norvegicus]

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
 72-211 9.62e-36

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 122.95  E-value: 9.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  72 EFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQGGYEDFV 151
Cdd:PTZ00184  12 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTDSEEEIK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823 152 EGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 211
Cdd:PTZ00184  88 EAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 72-211 9.62e-36

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 122.95  E-value: 9.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  72 EFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQGGYEDFV 151
Cdd:PTZ00184  12 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTDSEEEIK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823 152 EGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 211
Cdd:PTZ00184  88 EAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 149-210 1.95e-09

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: 51.78  E-value: 1.95e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672065823 149 DFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLA-GQEDSNGCINYEAFVKHIM 210
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
73-211 1.33e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  73 FKEAFLLFDRTGECKITLSQvgdvLRALGTNPTNAEVKKVLGNPSNeemnakKIEFEQFLPMMQAISnnkDQGGYEDFVE 152
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDD----FEALFRRLWATLFSEADTDGDG------RISREEFVAGMESLF---EATVEPFARA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823 153 GLRVFDKEGNGTVMGAELRHVLATLGekMKEEEVEALLAgQEDSN--GCINYEAFVKHIMS 211
Cdd:COG5126   74 AFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFA-RLDTDgdGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
155-210 1.32e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823  155 RVFDKEGNGTVMGAELRHVLATL--GEKMKEEEVEALLagQE---DSNGCINYEAFVKHIM 210
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELF--KEfdlDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 72-211 9.62e-36

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 122.95  E-value: 9.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  72 EFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgNPSNEEMNAKkIEFEQFLPMMQaiSNNKDQGGYEDFV 151
Cdd:PTZ00184  12 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGT-IDFPEFLTLMA--RKMKDTDSEEEIK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823 152 EGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFVKHIMS 211
Cdd:PTZ00184  88 EAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
PTZ00183 PTZ00183
centrin; Provisional
 68-210 6.39e-14

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 66.64  E-value: 6.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  68 ELHHEFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEemNAKKIEFEQFLPMMQAISNNKDQggY 147
Cdd:PTZ00183  14 DQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMTKKLGERDP--R 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672065823 148 EDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEV-EALLAGQEDSNGCINYEAFVKhIM 210
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELqEMIDEADRNGDGEISEEEFYR-IM 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 149-210 1.95e-09

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: 51.78  E-value: 1.95e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672065823 149 DFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLA-GQEDSNGCINYEAFVKHIM 210
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
73-211 1.33e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  73 FKEAFLLFDRTGECKITLSQvgdvLRALGTNPTNAEVKKVLGNPSNeemnakKIEFEQFLPMMQAISnnkDQGGYEDFVE 152
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDD----FEALFRRLWATLFSEADTDGDG------RISREEFVAGMESLF---EATVEPFARA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823 153 GLRVFDKEGNGTVMGAELRHVLATLGekMKEEEVEALLAgQEDSN--GCINYEAFVKHIMS 211
Cdd:COG5126   74 AFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFA-RLDTDgdGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 72-136 2.16e-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: 38.30  E-value: 2.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672065823  72 EFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLgnpsnEEM---NAKKIEFEQFLPMMQ 136
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI-----REVdkdGDGKIDFEEFLELMA 63
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 73-141 2.31e-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: 38.10  E-value: 2.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823  73 FKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEvKKVLGNpsneemnakKIEFEQFLP-MMQAISNN 141
Cdd:cd22949    5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDE-KDALPA---------SMNWDQFENwAKKKLAYS 64
PTZ00184 PTZ00184
calmodulin; Provisional
 148-206 1.11e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 38.20  E-value: 1.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065823 148 EDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQE-DSNGCINYEAFV 206
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDaDGNGTIDFPEFL 70
EF-hand_7 pfam13499
EF-hand domain pair;
155-210 1.32e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672065823  155 RVFDKEGNGTVMGAELRHVLATL--GEKMKEEEVEALLagQE---DSNGCINYEAFVKHIM 210
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELF--KEfdlDKDGRISFEEFLELYS 67
EF-hand_6 pfam13405
EF-hand domain;
72-101 5.46e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.30  E-value: 5.46e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 672065823   72 EFKEAFLLFDRTGECKITLSQVGDVLRALG 101
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
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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