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Conserved domains on  [gi|4505305|ref|NP_002468|]
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myosin light chain 5 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

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List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 26-158 7.47e-23

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 88.66  E-value: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305    26 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 101
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505305   102 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 158
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 26-158 7.47e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 88.66  E-value: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305    26 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 101
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505305   102 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 158
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-155 1.38e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305   30 TQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKTNVKDDELDamlkeASGPINFTMFLNlFGEKLSGTDAEETILNAF 109
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTD-----GDGRISREEFVA-GMESLFEATVEPFARAAF 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4505305  110 KMLDPDGKGKINKEYIKRLLmsQADKMTAEEVDQMfqFASIDVAGN 155
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLL--TALGVSEEEADEL--FARLDTDGD 117
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 81-166 1.13e-06

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 45.21  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305   81 GPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGKGKINKEYIKRLLMSQADKM-----TAEEVDQMFQFASIDVAGN 155
Cdd:cd16252  15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIQAADTDGDGR 94

                        90
                ....*....|.
gi 4505305  156 LDYKALSYVIT 166
Cdd:cd16252  95 IDFQEFSDMVK 105
EF-hand_8 pfam13833
EF-hand domain pair;
47-92 2.27e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 37.29  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4505305     47 DGFIDKEDLKDTYASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLF 92
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 34-62 4.02e-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: 36.20  E-value: 4.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 4505305      34 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 62
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 26-158 7.47e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 88.66  E-value: 7.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305    26 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 101
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505305   102 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 158
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
PTZ00183 PTZ00183
centrin; Provisional
 31-157 1.15e-16

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 72.80  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305    31 QIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGkTNVKDDELDAML----KEASGPINFTMFLNLFGEKLSGTDAEETIL 106
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEIL 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4505305   107 NAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLD 157
Cdd:PTZ00183  94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEIS 144
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-155 1.38e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305   30 TQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKTNVKDDELDamlkeASGPINFTMFLNlFGEKLSGTDAEETILNAF 109
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTD-----GDGRISREEFVA-GMESLFEATVEPFARAAF 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4505305  110 KMLDPDGKGKINKEYIKRLLmsQADKMTAEEVDQMfqFASIDVAGN 155
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLL--TALGVSEEEADEL--FARLDTDGD 117
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 81-166 1.13e-06

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 45.21  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505305   81 GPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGKGKINKEYIKRLLMSQADKM-----TAEEVDQMFQFASIDVAGN 155
Cdd:cd16252  15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIQAADTDGDGR 94

                        90
                ....*....|.
gi 4505305  156 LDYKALSYVIT 166
Cdd:cd16252  95 IDFQEFSDMVK 105
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 34-92 9.20e-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: 38.68  E-value: 9.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505305   34 EFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKEA----SGPINFTMFLNLF 92
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVdkdgDGKIDFEEFLELM 62
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 33-100 1.71e-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: 1.71e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505305   33 QEFKEAFTLMDQNRDGFIDKEDLKDTYASLGkTNVKDDELDAMlkeaSGPINFTMFLNLFGEKLSGTD 100
Cdd:cd22949   3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSD 65
EF-hand_8 pfam13833
EF-hand domain pair;
47-92 2.27e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 37.29  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4505305     47 DGFIDKEDLKDTYASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLF 92
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 34-62 4.02e-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: 36.20  E-value: 4.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 4505305      34 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 62
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 108-159 4.04e-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: 37.14  E-value: 4.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 4505305  108 AFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDYK 159
Cdd:cd00051   5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFE 56
EF-hand_7 pfam13499
EF-hand domain pair;
32-92 4.05e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 4.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505305     32 IQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKT-NVKDDELDAMLKEA----SGPINFTMFLNLF 92
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLSDEEVEELFKEFdldkDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
25-94 5.43e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.43e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505305   25 SNFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKdtyASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLFGE 94
Cdd:COG5126  61 SLFEATVEPFARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARLdtdgDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
34-63 1.14e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 1.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4505305     34 EFKEAFTLMDQNRDGFIDKEDLKDTYASLG 63
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 34-62 3.78e-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: 33.53  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 4505305     34 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 62
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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