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Conserved domains on  [gi|685291220|ref|XP_009136560|]
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probable calcium-binding protein CML41 isoform X2 [Brassica rapa]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040236)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-163 6.08e-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: 54.86  E-value: 6.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685291220 100 ELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:cd00051    1 ELREAFRLFDKD-GDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-163 6.08e-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: 54.86  E-value: 6.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685291220 100 ELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:cd00051    1 ELREAFRLFDKD-GDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 64-163 1.23e-10

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 56.31  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  64 ELRRVFSHFDVNSDG---FEDFVGLMTRRDLDGNGDGggELKTAFEMFEvEKGSGCITPKGLQNMLTKLGESRTYGECEA 140
Cdd:PTZ00184  48 ELQDMINEVDADGNGtidFPEFLTLMARKMKDTDSEE--EIKEAFKVFD-RDGNGFISAAELRHVMTNLGEKLTDEEVDE 124

                         90       100
                 ....*....|....*....|...
gi 685291220 141 MINYYDIDGNGVLDYHEFRQMMT 163
Cdd:PTZ00184 125 MIREADVDGDGQINYEEFVKMMM 147
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
62-163 1.54e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  62 HDELRRVFSHFDVNSDG---FEDFVGLMTRRDLDGNGDgggELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTygEC 138
Cdd:COG5126   32 RRLWATLFSEADTDGDGrisREEFVAGMESLFEATVEP---FARAAFDLLDTD-GDGKISADEFRRLLTALGVSEE--EA 105

                         90       100
                 ....*....|....*....|....*
gi 685291220 139 EAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:COG5126  106 DELFARLDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
100-163 1.09e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685291220  100 ELKTAFEMFEVeKGSGCITPKGLQNMLTKLGESRTY--GECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:pfam13499   3 KLKEAFKLLDS-DGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 137-163 1.41e-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: 34.66  E-value: 1.41e-03
                           10        20
                   ....*....|....*....|....*..
gi 685291220   137 ECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-163 6.08e-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: 54.86  E-value: 6.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685291220 100 ELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:cd00051    1 ELREAFRLFDKD-GDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 64-163 1.23e-10

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 56.31  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  64 ELRRVFSHFDVNSDG---FEDFVGLMTRRDLDGNGDGggELKTAFEMFEvEKGSGCITPKGLQNMLTKLGESRTYGECEA 140
Cdd:PTZ00184  48 ELQDMINEVDADGNGtidFPEFLTLMARKMKDTDSEE--EIKEAFKVFD-RDGNGFISAAELRHVMTNLGEKLTDEEVDE 124

                         90       100
                 ....*....|....*....|...
gi 685291220 141 MINYYDIDGNGVLDYHEFRQMMT 163
Cdd:PTZ00184 125 MIREADVDGDGQINYEEFVKMMM 147
PTZ00184 PTZ00184
calmodulin; Provisional
 100-162 7.27e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 51.69  E-value: 7.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685291220 100 ELKTAFEMFEvEKGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQMM 162
Cdd:PTZ00184  12 EFKEAFSLFD-KDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLM 73
PTZ00183 PTZ00183
centrin; Provisional
 64-163 1.26e-08

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 51.23  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  64 ELRRVFSHFDVNSDG---FEDFVGLMTRRDLDGNGDGggELKTAFEMFEvEKGSGCITPKGLQNMLTKLGESRTYGECEA 140
Cdd:PTZ00183  54 EIKQMIADVDKDGSGkidFEEFLDIMTKKLGERDPRE--EILKAFRLFD-DDKTGKISLKNLKRVAKELGETITDEELQE 130

                         90       100
                 ....*....|....*....|...
gi 685291220 141 MINYYDIDGNGVLDYHEFRQMMT 163
Cdd:PTZ00183 131 MIDEADRNGDGEISEEEFYRIMK 153
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
62-163 1.54e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  62 HDELRRVFSHFDVNSDG---FEDFVGLMTRRDLDGNGDgggELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTygEC 138
Cdd:COG5126   32 RRLWATLFSEADTDGDGrisREEFVAGMESLFEATVEP---FARAAFDLLDTD-GDGKISADEFRRLLTALGVSEE--EA 105

                         90       100
                 ....*....|....*....|....*
gi 685291220 139 EAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:COG5126  106 DELFARLDTDGDGKISFEEFVAAVR 130
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
63-164 9.56e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 9.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685291220  63 DELRRVFSHFDVNSDGF---EDFVGLMTRrdldgngdgggELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECE 139
Cdd:COG5126    5 RKLDRRFDLLDADGDGVlerDDFEALFRR-----------LWATLFSEADTD-GDGRISREEFVAGMESLFEATVEPFAR 72

                         90       100
                 ....*....|....*....|....*
gi 685291220 140 AMINYYDIDGNGVLDYHEFRQMMTV 164
Cdd:COG5126   73 AAFDLLDTDGDGKISADEFRRLLTA 97
EF-hand_7 pfam13499
EF-hand domain pair;
100-163 1.09e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685291220  100 ELKTAFEMFEVeKGSGCITPKGLQNMLTKLGESRTY--GECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:pfam13499   3 KLKEAFKLLDS-DGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 100-164 1.88e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 1.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685291220 100 ELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQMMTV 164
Cdd:PTZ00183  18 EIREAFDLFDTD-GSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTK 81
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 100-161 1.87e-04

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: 39.89  E-value: 1.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685291220 100 ELKTAFEMFEVEkGSGCITPKGLQNMLTKLGESRTYGECEAMINYYDIDGNGVLDYHEFRQM 161
Cdd:cd16185    1 ELRQWFRAVDRD-RSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAAL 61
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 137-163 1.96e-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: 36.99  E-value: 1.96e-04
                          10        20
                  ....*....|....*....|....*..
gi 685291220  137 ECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLK 27
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 137-163 1.41e-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: 34.66  E-value: 1.41e-03
                           10        20
                   ....*....|....*....|....*..
gi 685291220   137 ECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
EF-hand_8 pfam13833
EF-hand domain pair;
113-163 1.76e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.98  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 685291220  113 GSGCITPKGLQNMLTKLGESR-TYGECEAMINYYDIDGNGVLDYHEFRQMMT 163
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDlSEDEVDILFREFDTDGDGYISFDEFCVLLE 52
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 115-161 3.23e-03

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 36.19  E-value: 3.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 685291220 115 GCITPKGLQNMLTKLGESRTYGE-----CEAMINYYDIDGNGVLDYHEFRQM 161
Cdd:cd16181   14 GQIDADELQRCLTQSGISGNYQPfsletCRLMIAMLDRDHSGKMGFNEFKEL 65
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 114-161 7.76e-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: 35.32  E-value: 7.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 685291220 114 SGCITPKGLQNMLTKLGESRTYGE-CEAMINYYDIDGNGVLDYHEFRQM 161
Cdd:cd16184   14 SGKISAKELQQALVNGNWSHFNDEtCRLMIGMFDKDKSGTIDIYEFQAL 62
 
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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