myosin light chain 1/3, skeletal muscle isoform isoform X2 [Macaca mulatta]
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PTZ00184 super family | cl33172 | calmodulin; Provisional |
4-149 | 1.13e-35 | |||
calmodulin; Provisional The actual alignment was detected with superfamily member PTZ00184: Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 120.64 E-value: 1.13e-35
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Name | Accession | Description | Interval | E-value | |||
PTZ00184 | PTZ00184 | calmodulin; Provisional |
4-149 | 1.13e-35 | |||
calmodulin; Provisional Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 120.64 E-value: 1.13e-35
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
87-148 | 7.57e-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: 49.08 E-value: 7.57e-09
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
7-149 | 1.75e-05 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.09 E-value: 1.75e-05
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EF-hand_6 | pfam13405 | EF-hand domain; |
10-39 | 1.08e-03 | |||
EF-hand domain; Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 34.84 E-value: 1.08e-03
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Name | Accession | Description | Interval | E-value | |||
PTZ00184 | PTZ00184 | calmodulin; Provisional |
4-149 | 1.13e-35 | |||
calmodulin; Provisional Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 120.64 E-value: 1.13e-35
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PTZ00183 | PTZ00183 | centrin; Provisional |
1-148 | 3.80e-15 | |||
centrin; Provisional Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 68.18 E-value: 3.80e-15
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
87-148 | 7.57e-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: 49.08 E-value: 7.57e-09
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ELC_N | cd22949 | N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ... |
11-79 | 9.10e-06 | |||
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: 41.18 E-value: 9.10e-06
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FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
7-149 | 1.75e-05 | |||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.09 E-value: 1.75e-05
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EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
10-74 | 6.78e-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: 35.99 E-value: 6.78e-04
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EF-hand_6 | pfam13405 | EF-hand domain; |
10-39 | 1.08e-03 | |||
EF-hand domain; Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 34.84 E-value: 1.08e-03
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EFh_parvalbumin_like | cd16251 | EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
80-145 | 5.99e-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: 34.43 E-value: 5.99e-03
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EF-hand_7 | pfam13499 | EF-hand domain pair; |
93-148 | 6.43e-03 | |||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 33.38 E-value: 6.43e-03
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Blast search parameters | ||||
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