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Conserved domains on  [gi|1034599866|ref|XP_016880172|]
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myosin light chain 4 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
 86-227 1.95e-31

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 112.55  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866  86 EFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKEQGTYED 165
Cdd:PTZ00184   12 EFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKDTDSEEE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599866 166 FVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 227
Cdd:PTZ00184   86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 86-227 1.95e-31

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 112.55  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866  86 EFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKEQGTYED 165
Cdd:PTZ00184   12 EFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKDTDSEEE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599866 166 FVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 227
Cdd:PTZ00184   86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 165-226 1.16e-08

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: 50.24  E-value: 1.16e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599866 165 DFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLA-GQEDANGCINYEAFVKHIM 226
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 86-227 1.95e-31

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 112.55  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866  86 EFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKEQGTYED 165
Cdd:PTZ00184   12 EFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKDTDSEEE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599866 166 FVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 227
Cdd:PTZ00184   86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
PTZ00183 PTZ00183
centrin; Provisional
 85-226 5.35e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 61.63  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866  85 HEFKEAFSLFDRTPTG-----EMKITygqcgdvLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPIL-QHISrnk 158
Cdd:PTZ00183   17 KEIREAFDLFDTDGSGtidpkELKVA-------MRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMtKKLG--- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034599866 159 EQGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLL-AGQEDANGCINYEAFVKhIM 226
Cdd:PTZ00183   85 ERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIdEADRNGDGEISEEEFYR-IM 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 165-226 1.16e-08

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: 50.24  E-value: 1.16e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599866 165 DFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLA-GQEDANGCINYEAFVKHIM 226
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 164-222 2.39e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.13  E-value: 2.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866 164 EDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFV 222
Cdd:PTZ00184   11 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDaDGNGTIDFPEFL 70
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 83-157 2.29e-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: 35.40  E-value: 2.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034599866  83 CPHEFKEAFSLFDRTPTGEmkITYGQCGDVLRALGQNPTNAEVLRVlgkpkPEEMNvkMLDFETFLpiLQHISRN 157
Cdd:cd22949     1 MEEKFREAFILFDRDGDGE--LTMYEAVLAMRSCGIPLTNDEKDAL-----PASMN--WDQFENWA--KKKLAYS 64
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 158-223 2.93e-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: 35.97  E-value: 2.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599866 158 KEQGTYEDFVEGLRVFDKESNGTVMGAELRHVLATL---GEKMTEAEVEQLL-AGQEDANGCINYEAFVK 223
Cdd:cd16251    28 LKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLaAGDTDGDGKIGVEEFAT 97
 
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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