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Conserved domains on  [gi|767945666|ref|XP_011513766|]
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myosin regulatory light chain 2, atrial isoform isoform X2 [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
 28-143 4.78e-21

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 84.81  E-value: 4.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  28 MFEQAQIQEFKEAFSCIDQNRDGIICKADLRETYSQLGKvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767945666 104 EEAILSAFRMFDPSGKGVVNKDEFKQLLLTQADKFSPAEV 143
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV 122
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 28-143 4.78e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 84.81  E-value: 4.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  28 MFEQAQIQEFKEAFSCIDQNRDGIICKADLRETYSQLGKvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767945666 104 EEAILSAFRMFDPSGKGVVNKDEFKQLLLTQADKFSPAEV 143
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV 122
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
33-144 5.18e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  33 QIQEFKEAFSCIDQNRDGIICKADLRETYSQLgkvsvPEEELDAMLQEGKGPINFTVFLTlFGEKLNGTDPEEAILSAFR 112
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL-----WATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFD 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 767945666 113 MFDPSGKGVVNKDEFKQLLltQADKFSPAEVR 144
Cdd:COG5126   77 LLDTDGDGKISADEFRRLL--TALGVSEEEAD 106
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 36-131 3.22e-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: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  36 EFKEAFSCIDQNRDGIICKADLRETYSQLGkVSVPEEELDAMlqegkgpinftvfltlfgeklngtdpeeailsaFRMFD 115
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-EGLSEEEIDEM---------------------------------IREVD 46

                         90
                 ....*....|....*.
gi 767945666 116 PSGKGVVNKDEFKQLL 131
Cdd:cd00051   47 KDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
34-132 6.98e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666   34 IQEFKEAFSCIDQNRDGIICKADLREtysqlgkvsvpeeeldamlqegkgpinftvFLTLFGEKLNGTDpeEAILSAFRM 113
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK------------------------------LLRKLEEGEPLSD--EEVEELFKE 48

                          90
                  ....*....|....*....
gi 767945666  114 FDPSGKGVVNKDEFKQLLL 132
Cdd:pfam13499  49 FDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 28-143 4.78e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 84.81  E-value: 4.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  28 MFEQAQIQEFKEAFSCIDQNRDGIICKADLRETYSQLGKvSVPEEELDAMLQE----GKGPINFTVFLTLFGEKLNGTDP 103
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767945666 104 EEAILSAFRMFDPSGKGVVNKDEFKQLLLTQADKFSPAEV 143
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEV 122
PTZ00183 PTZ00183
centrin; Provisional
 33-120 2.68e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 56.62  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  33 QIQEFKEAFSCIDQNRDGIIckaDLRETYSQLGKVSV--PEEELDAMLQ----EGKGPINFTVFLTLFGEKLNGTDPEEA 106
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTI---DPKELKVAMRSLGFepKKEEIKQMIAdvdkDGSGKIDFEEFLDIMTKKLGERDPREE 91

                         90
                 ....*....|....
gi 767945666 107 ILSAFRMFDPSGKG 120
Cdd:PTZ00183  92 ILKAFRLFDDDKTG 105
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
33-144 5.18e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  33 QIQEFKEAFSCIDQNRDGIICKADLRETYSQLgkvsvPEEELDAMLQEGKGPINFTVFLTlFGEKLNGTDPEEAILSAFR 112
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL-----WATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFD 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 767945666 113 MFDPSGKGVVNKDEFKQLLltQADKFSPAEVR 144
Cdd:COG5126   77 LLDTDGDGKISADEFRRLL--TALGVSEEEAD 106
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 36-131 3.22e-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: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  36 EFKEAFSCIDQNRDGIICKADLRETYSQLGkVSVPEEELDAMlqegkgpinftvfltlfgeklngtdpeeailsaFRMFD 115
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG-EGLSEEEIDEM---------------------------------IREVD 46

                         90
                 ....*....|....*.
gi 767945666 116 PSGKGVVNKDEFKQLL 131
Cdd:cd00051   47 KDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
34-132 6.98e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666   34 IQEFKEAFSCIDQNRDGIICKADLREtysqlgkvsvpeeeldamlqegkgpinftvFLTLFGEKLNGTDpeEAILSAFRM 113
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK------------------------------LLRKLEEGEPLSD--EEVEELFKE 48

                          90
                  ....*....|....*....
gi 767945666  114 FDPSGKGVVNKDEFKQLLL 132
Cdd:pfam13499  49 FDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-131 8.41e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666  27 SMFEQAQIQEFKEAFSCIDQNRDGIICKADLRETYSQLGkvsVPEEELDAMlqegkgpinftvfltlfgeklngtdpeea 106
Cdd:COG5126   61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG---VSEEEADEL----------------------------- 108

                         90       100
                 ....*....|....*....|....*
gi 767945666 107 ilsaFRMFDPSGKGVVNKDEFKQLL 131
Cdd:COG5126  109 ----FARLDTDGDGKISFEEFVAAV 129
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 35-103 1.16e-03

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: 36.17  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767945666  35 QEFKEAFSCIDQNRDGIICKADLRETYSQLGkVSVPEEELDAMlqegKGPINFTVFLTLFGEKLNGTDP 103
Cdd:cd22949    3 EKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EF-hand_8 pfam13833
EF-hand domain pair;
49-134 3.57e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.60  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945666   49 DGIICKADLRETYSQLGKVSVPEEELDAMlqegkgpinftvfltlfgeklngtdpeeailsaFRMFDPSGKGVVNKDEFK 128
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDIL---------------------------------FREFDTDGDGYISFDEFC 48


                  ....*.
gi 767945666  129 QLLLTQ 134
Cdd:pfam13833  49 VLLERR 54
EF-hand_7 pfam13499
EF-hand domain pair;
104-145 3.72e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.92  E-value: 3.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767945666  104 EEAILSAFRMFDPSGKGVVNKDEFKQLL--LTQADKFSPAEVRL 145
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEE 44
EF-hand_6 pfam13405
EF-hand domain;
107-131 4.09e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.69  E-value: 4.09e-03
                          10        20
                  ....*....|....*....|....*
gi 767945666  107 ILSAFRMFDPSGKGVVNKDEFKQLL 131
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKAL 26
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 107-131 9.29e-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: 32.76  E-value: 9.29e-03
                          10        20
                  ....*....|....*....|....*
gi 767945666  107 ILSAFRMFDPSGKGVVNKDEFKQLL 131
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELL 26
 
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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