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Conserved domains on  [gi|4557038|ref|NP_002467.1|]
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myosin light chain 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_PEF super family cl25352
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
49-196 3.43e-31

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 330173  Cd Length: 149  Bit Score: 113.32  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038    49 TADQIEEFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKE 128
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557038   129 QGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 196
Cdd:PTZ00184  80 TDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
49-196 3.43e-31

calmodulin; Provisional


Pssm-ID: 185504  Cd Length: 149  Bit Score: 113.32  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038    49 TADQIEEFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKE 128
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557038   129 QGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 196
Cdd:PTZ00184  80 TDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
48-196 2.36e-28

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


Pssm-ID: 227455  Cd Length: 160  Bit Score: 106.24  E-value: 2.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038   48 FTADQIEEFKEAFSLFDRTPTGemKITYGQCGDVLRALGQNPTNAEVLRVLgkpkpEEMNVKM--LDFETFLPILqhiSR 125
Cdd:COG5126  14 LTEEQIQELKEAFQLFDRDSDG--LIDRNELGKILRSLGFNPSEAEINKLF-----EEIDAGNetVDFPEFLTVM---SV 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557038  126 NKEQG-TYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAG-QEDANGCINYEAFVKHIMS 196
Cdd:COG5126  84 KLKRGdKEEELREAFKLFDKDHDGYISIGELRRVLKSLGERLSDEEVEKLLKEyDEDGDGEIDYEEFKKLIKD 156
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
134-195 6.28e-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  Cd Length: 63  Bit Score: 47.93  E-value: 6.28e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557038  134 DFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLA-GQEDANGCINYEAFVKHIM 195
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
49-196 3.43e-31

calmodulin; Provisional


Pssm-ID: 185504  Cd Length: 149  Bit Score: 113.32  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038    49 TADQIEEFKEAFSLFDRTptGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFETFLPILQhiSRNKE 128
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKD--GDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMA--RKMKD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557038   129 QGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQE-DANGCINYEAFVKHIMS 196
Cdd:PTZ00184  80 TDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
48-196 2.36e-28

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


Pssm-ID: 227455  Cd Length: 160  Bit Score: 106.24  E-value: 2.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038   48 FTADQIEEFKEAFSLFDRTPTGemKITYGQCGDVLRALGQNPTNAEVLRVLgkpkpEEMNVKM--LDFETFLPILqhiSR 125
Cdd:COG5126  14 LTEEQIQELKEAFQLFDRDSDG--LIDRNELGKILRSLGFNPSEAEINKLF-----EEIDAGNetVDFPEFLTVM---SV 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557038  126 NKEQG-TYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAG-QEDANGCINYEAFVKHIMS 196
Cdd:COG5126  84 KLKRGdKEEELREAFKLFDKDHDGYISIGELRRVLKSLGERLSDEEVEKLLKEyDEDGDGEIDYEEFKKLIKD 156
PTZ00183 PTZ00183
centrin; Provisional
41-195 4.69e-14

centrin; Provisional


Pssm-ID: 185503  Cd Length: 158  Bit Score: 67.02  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038    41 PKSVKIDFTADQIEEFKEAFSLFDRTPTG-----EMKITygqcgdvLRALGQNPTNAEVLRVLGKPKPEemNVKMLDFET 115
Cdd:PTZ00183   4 RRSERPGLTEDQKKEIREAFDLFDTDGSGtidpkELKVA-------MRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038   116 FLPIL-QHISrnkEQGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLL-AGQEDANGCINYEAFVKh 193
Cdd:PTZ00183  75 FLDIMtKKLG---ERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIdEADRNGDGEISEEEFYR- 150

                 ..
gi 4557038   194 IM 195
Cdd:PTZ00183 151 IM 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
134-195 6.28e-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  Cd Length: 63  Bit Score: 47.93  E-value: 6.28e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557038  134 DFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLA-GQEDANGCINYEAFVKHIM 195
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIReVDKDGDGKIDFEEFLELMA 63
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
127-192 4.84e-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  Cd Length: 101  Bit Score: 35.20  E-value: 4.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557038  127 KEQGTYEDFVEGLRVFDKESNGTVMGAELRHVLATL---GEKMTEAEVEQLL-AGQEDANGCINYEAFVK 192
Cdd:cd16251  28 LKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLaAGDTDGDGKIGVEEFAT 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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