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Conserved domains on  [gi|1958791406|ref|XP_038935834|]
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myosin light polypeptide 6 isoform X3 [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
 5-142 3.22e-38

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 126.80  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791406   5 TEDQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDemNVKVLDFEHFLPMLQTvaKNKDQG 84
Cdd:PTZ00184    6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791406  85 TYEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVdEMIREADVDGDGQINYE 140
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 5-142 3.22e-38

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 126.80  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791406   5 TEDQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDemNVKVLDFEHFLPMLQTvaKNKDQG 84
Cdd:PTZ00184    6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791406  85 TYEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVdEMIREADVDGDGQINYE 140
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 94-142 1.26e-05

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: 40.61  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958791406  94 RVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIdEMIREVDKDGDGKIDFE 56
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 11-39 6.91e-05

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: 37.74  E-value: 6.91e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958791406   11 EFKEAFQLFDRTGDGKILYSQCGDVMRAL 39
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_6 pfam13405
EF-hand domain;
11-40 1.45e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 1.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958791406  11 EFKEAFQLFDRTGDGKILYSQCGDVMRALG 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 5-142 3.22e-38

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 126.80  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791406   5 TEDQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDemNVKVLDFEHFLPMLQTvaKNKDQG 84
Cdd:PTZ00184    6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791406  85 TYEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVdEMIREADVDGDGQINYE 140
PTZ00183 PTZ00183
centrin; Provisional
 3-142 8.51e-16

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 69.72  E-value: 8.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791406   3 DFTEDQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDemNVKVLDFEHFLPMLQTVAKNKD 82
Cdd:PTZ00183   10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMTKKLGERD 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791406  83 qgTYEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:PTZ00183   88 --PREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELqEMIDEADRNGDGEISEE 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 94-142 1.26e-05

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: 40.61  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958791406  94 RVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEV-EMLVAGHEDSNGCINYE 142
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIdEMIREVDKDGDGKIDFE 56
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 12-47 4.42e-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: 4.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958791406  12 FKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAE 47
Cdd:cd22949     5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDE 40
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 11-39 6.91e-05

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: 37.74  E-value: 6.91e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958791406   11 EFKEAFQLFDRTGDGKILYSQCGDVMRAL 39
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_6 pfam13405
EF-hand domain;
11-40 1.45e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 1.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958791406  11 EFKEAFQLFDRTGDGKILYSQCGDVMRALG 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 11-75 3.07e-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: 34.06  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791406  11 EFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVlkvlgnpksDEMNVKV-------LDFEHFLPMLQ 75
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI---------DEMIREVdkdgdgkIDFEEFLELMA 63
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 11-39 4.39e-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: 4.39e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958791406  11 EFKEAFQLFDRTGDGKILYSQCGDVMRAL 39
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.
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