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Conserved domains on  [gi|2462597361|ref|XP_054206074|]
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myosin light chain 5 isoform X1 [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
 31-163 2.31e-23

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.21  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  31 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 106
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462597361 107 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 163
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 31-163 2.31e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.21  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  31 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 106
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462597361 107 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 163
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-160 5.82e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.80  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  35 TQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKTNVKDDELDamlkeASGPINFTMFLNlFGEKLSGTDAEETILNAF 114
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTD-----GDGRISREEFVA-GMESLFEATVEPFARAAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462597361 115 KMLDPDGKGKINKEYIKRLLmsQADKMTAEEVDQMfqFASIDVAGN 160
Cdd:COG5126    76 DLLDTDGDGKISADEFRRLL--TALGVSEEEADEL--FARLDTDGD 117
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 86-171 9.61e-07

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: 9.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  86 GPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGKGKINKEYIKRLLMSQADKM-----TAEEVDQMFQFASIDVAGN 160
Cdd:cd16252    15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIQAADTDGDGR 94

                          90
                  ....*....|.
gi 2462597361 161 LDYKALSYVIT 171
Cdd:cd16252    95 IDFQEFSDMVK 105
EF-hand_8 pfam13833
EF-hand domain pair;
52-97 1.29e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462597361  52 DGFIDKEDLKDTYASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLF 97
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 39-67 2.45e-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: 36.97  E-value: 2.45e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462597361   39 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 67
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 31-163 2.31e-23

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.21  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  31 NFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKE----ASGPINFTMFLNLFGEKLSGTDA 106
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462597361 107 EETILNAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDY 163
Cdd:PTZ00184   83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
PTZ00183 PTZ00183
centrin; Provisional
 36-162 4.18e-17

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 73.96  E-value: 4.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  36 QIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGkTNVKDDELDAML----KEASGPINFTMFLNLFGEKLSGTDAEETIL 111
Cdd:PTZ00183   15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEIL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462597361 112 NAFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLD 162
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEIS 144
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
35-160 5.82e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.80  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  35 TQIQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKTNVKDDELDamlkeASGPINFTMFLNlFGEKLSGTDAEETILNAF 114
Cdd:COG5126     2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTD-----GDGRISREEFVA-GMESLFEATVEPFARAAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462597361 115 KMLDPDGKGKINKEYIKRLLmsQADKMTAEEVDQMfqFASIDVAGN 160
Cdd:COG5126    76 DLLDTDGDGKISADEFRRLL--TALGVSEEEADEL--FARLDTDGD 117
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 86-171 9.61e-07

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: 9.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  86 GPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGKGKINKEYIKRLLMSQADKM-----TAEEVDQMFQFASIDVAGN 160
Cdd:cd16252    15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIQAADTDGDGR 94

                          90
                  ....*....|.
gi 2462597361 161 LDYKALSYVIT 171
Cdd:cd16252    95 IDFQEFSDMVK 105
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 39-97 4.49e-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: 39.84  E-value: 4.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462597361  39 EFKEAFTLMDQNRDGFIDKEDLKDTYASLGKtNVKDDELDAMLKEA----SGPINFTMFLNLF 97
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVdkdgDGKIDFEEFLELM 62
EF-hand_8 pfam13833
EF-hand domain pair;
52-97 1.29e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462597361  52 DGFIDKEDLKDTYASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLF 97
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 38-105 1.59e-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: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462597361  38 QEFKEAFTLMDQNRDGFIDKEDLKDTYASLGkTNVKDDELDAMlkeaSGPINFTMFLNLFGEKLSGTD 105
Cdd:cd22949     3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSD 65
EF-hand_7 pfam13499
EF-hand domain pair;
37-97 2.08e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 2.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462597361  37 IQEFKEAFTLMDQNRDGFIDKEDLKDTYASLGKT-NVKDDELDAMLKEA----SGPINFTMFLNLF 97
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLSDEEVEELFKEFdldkDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 113-164 2.44e-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: 37.53  E-value: 2.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462597361 113 AFKMLDPDGKGKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDYK 164
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFE 56
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 39-67 2.45e-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: 36.97  E-value: 2.45e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462597361   39 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 67
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-99 3.33e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 3.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462597361  30 SNFEQTQIQEFKEAFTLMDQNRDGFIDKEDLKdtyASLGKTNVKDDELDAMLKEA----SGPINFTMFLNLFGE 99
Cdd:COG5126    61 SLFEATVEPFARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARLdtdgDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
39-68 6.93e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 6.93e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462597361  39 EFKEAFTLMDQNRDGFIDKEDLKDTYASLG 68
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 39-67 2.41e-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: 2.41e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462597361  39 EFKEAFTLMDQNRDGFIDKEDLKDTYASL 67
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_7 pfam13499
EF-hand domain pair;
107-160 5.39e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.15  E-value: 5.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462597361 107 EETILNAFKMLDPDGKGKINKEYIKRLLM--SQADKMTAEEVDQMFQfaSIDVAGN 160
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFK--EFDLDKD 54
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 73-167 9.69e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 34.05  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597361  73 KDDELDAMLKEASGPINFTMFLNLFGEKlSGTDAEetILNAFKMLDPDGKGKINKEYIKRLLM---SQADKMTAEEVDQM 149
Cdd:cd16251     2 KDIEKAPSAFRAHGSFNYKKFFEHVGLK-QKSEDQ--IKKVFQILDKDKSGFIEEEELKYILKgfsIAGRDLTDEETKAL 78

                          90
                  ....*....|....*...
gi 2462597361 150 FQFASIDVAGNLDYKALS 167
Cdd:cd16251    79 LAAGDTDGDGKIGVEEFA 96
 
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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