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Conserved domains on  [gi|31563524|ref|NP_852667|]
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myosin regulatory light polypeptide 9 isoform b [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
 25-109 8.87e-12

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 57.85  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524   25 MFDQSQIQEFKEAFNMIDQNRDGFIDKEDLhdmlaslgfihedhlRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVE 104
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNGFISAAEL---------------RHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141


                 ....*
gi 31563524  105 FTRIL 109
Cdd:PTZ00184 142 FVKMM 146
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 25-109 8.87e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 57.85  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524   25 MFDQSQIQEFKEAFNMIDQNRDGFIDKEDLhdmlaslgfihedhlRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVE 104
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNGFISAAEL---------------RHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141


                 ....*
gi 31563524  105 FTRIL 109
Cdd:PTZ00184 142 FVKMM 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 33-110 2.07e-07

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: 44.46  E-value: 2.07e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563524  33 EFKEAFNMIDQNRDGFIDKEDlhdmlaslgfihedhLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILK 110
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADE---------------LKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
31-110 3.35e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524    31 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGfihedhlrellttMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILK 110
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLE-------------EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 33-61 1.69e-05

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: 38.90  E-value: 1.69e-05
                           10        20
                   ....*....|....*....|....*....
gi 31563524     33 EFKEAFNMIDQNRDGFIDKEDLHDMLASL 61
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-111 4.34e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524  24 AMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGfihedhlrellttmgdrFTDEEVDEMYREAPIDKKGNFNYV 103
Cdd:COG5126  61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG-----------------VSEEEADELFARLDTDGDGKISFE 123


                ....*...
gi 31563524 104 EFTRILKH 111
Cdd:COG5126 124 EFVAAVRD 131
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 25-109 8.87e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 57.85  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524   25 MFDQSQIQEFKEAFNMIDQNRDGFIDKEDLhdmlaslgfihedhlRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVE 104
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNGFISAAEL---------------RHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141


                 ....*
gi 31563524  105 FTRIL 109
Cdd:PTZ00184 142 FVKMM 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 33-110 2.07e-07

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: 44.46  E-value: 2.07e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563524  33 EFKEAFNMIDQNRDGFIDKEDlhdmlaslgfihedhLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILK 110
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADE---------------LKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
31-110 3.35e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524    31 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGfihedhlrellttMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILK 110
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLE-------------EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 33-61 1.69e-05

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: 38.90  E-value: 1.69e-05
                           10        20
                   ....*....|....*....|....*....
gi 31563524     33 EFKEAFNMIDQNRDGFIDKEDLHDMLASL 61
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_6 pfam13405
EF-hand domain;
33-62 1.99e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.70  E-value: 1.99e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 31563524    33 EFKEAFNMIDQNRDGFIDKEDLHDMLASLG 62
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 33-61 3.59e-04

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: 35.45  E-value: 3.59e-04
                          10        20
                  ....*....|....*....|....*....
gi 31563524    33 EFKEAFNMIDQNRDGFIDKEDLHDMLASL 61
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-111 4.34e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524  24 AMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGfihedhlrellttmgdrFTDEEVDEMYREAPIDKKGNFNYV 103
Cdd:COG5126  61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG-----------------VSEEEADELFARLDTDGDGKISFE 123


                ....*...
gi 31563524 104 EFTRILKH 111
Cdd:COG5126 124 EFVAAVRD 131
PTZ00183 PTZ00183
centrin; Provisional
 26-118 8.94e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 36.59  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563524   26 FDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGFihedhlrellttmgdRFTDEEVDEMYREAPIDKKGNFNYVEF 105
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGF---------------EPKKEEIKQMIADVDKDGSGKIDFEEF 75

                         90
                 ....*....|....*
gi 31563524  106 TRIL--KHGAKDKDD 118
Cdd:PTZ00183  76 LDIMtkKLGERDPRE 90
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 31-63 1.38e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 36.09  E-value: 1.38e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 31563524  31 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGF 63
Cdd:cd16184  66 IQQWKQVFQQFDRDRSGSIDENELHQALSQMGY 98
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 32-109 2.88e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 35.79  E-value: 2.88e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563524  32 QEFKEAFNMIDQNRDGFIDKEDLHDMLASLgfihedhLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRIL 109
Cdd:cd15902  90 VEFMKIWRKYDTDGSGFIEAKELKGFLKDL-------LLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAKLL 160
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 31-80 7.07e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 34.15  E-value: 7.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 31563524  31 IQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGFIHEDHLRELLTTMGDRF 80
Cdd:cd16183  66 ITDWQNCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQ 115
EF-hand_5 pfam13202
EF hand;
34-58 9.68e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 31.52  E-value: 9.68e-03
                          10        20
                  ....*....|....*....|....*
gi 31563524    34 FKEAFNMIDQNRDGFIDKEDLHDML 58
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
 
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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