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Conserved domains on  [gi|1559463273|gb|QAB07197|]
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calmodulin, partial [Trichoderma afarasin]

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
 2-41 4.22e-21

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 78.65  E-value: 4.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:PTZ00184   28 ITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFP 67
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 2-41 4.22e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 78.65  E-value: 4.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:PTZ00184   28 ITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFP 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 2-40 6.96e-11

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: 6.96e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 1559463273  2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDF 40
Cdd:cd00051   17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDF 55
EF-hand_8 pfam13833
EF-hand domain pair;
1-40 5.09e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.37  E-value: 5.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 1559463273  1 QITTKELGTVMRSLG-QNPSESELQDMINEVDADNNGSIDF 40
Cdd:pfam13833  4 VITREELKRALALLGlKDLSEDEVDILFREFDTDGDGYISF 44
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-40 6.53e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 34.00  E-value: 6.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   1 QITTKELGTVMRSLGqnPSESELQDMINEVDADNNGSIDF 40
Cdd:COG5126    85 KISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISF 122
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 22-40 2.16e-03

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: 30.81  E-value: 2.16e-03
                          10
                  ....*....|....*....
gi 1559463273  22 ELQDMINEVDADNNGSIDF 40
Cdd:smart00054  1 ELKEAFRLFDKDGDGKIDF 19
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 2-41 4.22e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 78.65  E-value: 4.22e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:PTZ00184   28 ITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFP 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 2-40 6.96e-11

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: 6.96e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 1559463273  2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDF 40
Cdd:cd00051   17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDF 55
PTZ00183 PTZ00183
centrin; Provisional
 2-40 2.09e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 2.09e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1559463273   2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDF 40
Cdd:PTZ00183  107 ISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISE 145
PTZ00183 PTZ00183
centrin; Provisional
 2-41 3.03e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.44  E-value: 3.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   2 ITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:PTZ00183   34 IDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFE 73
EF-hand_8 pfam13833
EF-hand domain pair;
1-40 5.09e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.37  E-value: 5.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 1559463273  1 QITTKELGTVMRSLG-QNPSESELQDMINEVDADNNGSIDF 40
Cdd:pfam13833  4 VITREELKRALALLGlKDLSEDEVDILFREFDTDGDGYISF 44
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-40 6.53e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 34.00  E-value: 6.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   1 QITTKELGTVMRSLGqnPSESELQDMINEVDADNNGSIDF 40
Cdd:COG5126    85 KISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISF 122
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 12-41 7.81e-04

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 33.76  E-value: 7.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1559463273  12 RSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:cd16207    29 RRLHINCSESYLRELFDKADTDKKGYLNFE 58
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 1-40 1.31e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. 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. Peflin 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+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 33.27  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1559463273   1 QITTKELGTVMRSLGQNP-SESELQDMINEVDADNNGSIDF 40
Cdd:cd16180    16 RISAKELQRALSNGDWTPfSIETVRLMINMFDRDRSGTINF 56
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 1-40 1.37e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 33.02  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1559463273   1 QITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDF 40
Cdd:cd15898    16 KLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTF 55
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 22-40 2.16e-03

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: 30.81  E-value: 2.16e-03
                          10
                  ....*....|....*....
gi 1559463273  22 ELQDMINEVDADNNGSIDF 40
Cdd:smart00054  1 ELKEAFRLFDKDGDGKIDF 19
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 1-41 2.80e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 32.57  E-value: 2.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1559463273   1 QITTKELGTVMRSLGQNPSESELQDMINEVDADNNGSIDFP 41
Cdd:cd16185    16 SIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFE 56
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 22-40 5.17e-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: 29.68  E-value: 5.17e-03
                         10
                 ....*....|....*....
gi 1559463273 22 ELQDMINEVDADNNGSIDF 40
Cdd:pfam00036  1 ELKEIFRLFDKDGDGKIDF 19
UPF0154 pfam03672
Uncharacterized protein family (UPF0154); This family contains a set of short bacterial ...
 1-28 8.22e-03

Uncharacterized protein family (UPF0154); This family contains a set of short bacterial proteins of unknown function.


Pssm-ID: 427437  Cd Length: 60  Bit Score: 29.88  E-value: 8.22e-03
                         10        20
                 ....*....|....*....|....*...
gi 1559463273  1 QITTKELGTVMRSLGQNPSESELQDMIN 28
Cdd:pfam03672 29 PINEKMIRAMMMQMGRKPSEKQIKQMMR 56
 
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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