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Conserved domains on  [gi|665389890|ref|NP_001284931|]
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spaghetti squash, isoform E [Drosophila melanogaster]

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
 27-164 2.96e-30

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 107.54  E-value: 2.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  27 MFDQAQIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNE----APGPINFTMFLTLFGERLQGTDPE 102
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665389890 103 DVIKNAFGCFDEENMGVLPEDRLRELLTTMGDRFTDEDVDEMYREAPIK-NGLFDYLEFTRIL 164
Cdd:PTZ00184  84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDgDGQINYEEFVKMM 146
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 27-164 2.96e-30

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 107.54  E-value: 2.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  27 MFDQAQIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNE----APGPINFTMFLTLFGERLQGTDPE 102
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665389890 103 DVIKNAFGCFDEENMGVLPEDRLRELLTTMGDRFTDEDVDEMYREAPIK-NGLFDYLEFTRIL 164
Cdd:PTZ00184  84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDgDGQINYEEFVKMM 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 35-79 3.07e-06

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: 42.92  E-value: 3.07e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 665389890  35 EFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNEA 79
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREV 45
EF-hand_6 pfam13405
EF-hand domain;
35-64 6.76e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 6.76e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 665389890   35 EFKEAFNMIDQNRDGFVEKEDLHDMLASLG 64
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 35-63 9.58e-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: 37.74  E-value: 9.58e-05
                           10        20
                   ....*....|....*....|....*....
gi 665389890    35 EFKEAFNMIDQNRDGFVEKEDLHDMLASL 63
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-166 3.97e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  32 QIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLgknpTDDYLDGMMNEAPGPINFTMFLTlFGERLQGTDPEDVIKNAFGC 111
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL----WATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFDL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665389890 112 FDEENMGVLPEDRLRELLTTMGdrFTDEDVDEMYREA-PIKNGLFDYLEFTRILKH 166
Cdd:COG5126   78 LDTDGDGKISADEFRRLLTALG--VSEEEADELFARLdTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 27-164 2.96e-30

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 107.54  E-value: 2.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  27 MFDQAQIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNE----APGPINFTMFLTLFGERLQGTDPE 102
Cdd:PTZ00184   4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665389890 103 DVIKNAFGCFDEENMGVLPEDRLRELLTTMGDRFTDEDVDEMYREAPIK-NGLFDYLEFTRIL 164
Cdd:PTZ00184  84 EEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDgDGQINYEEFVKMM 146
PTZ00183 PTZ00183
centrin; Provisional
 32-165 2.44e-12

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 61.24  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  32 QIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMM----NEAPGPINFTMFLTLFGERLQGTDPEDVIKN 107
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEILK 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665389890 108 AFGCFDEENMGVLPEDRLRELLTTMGDRFTDEDVDEMYREAPIKN-GLFDYLEFTRILK 165
Cdd:PTZ00183  95 AFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGdGEISEEEFYRIMK 153
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 35-79 3.07e-06

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: 42.92  E-value: 3.07e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 665389890  35 EFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNEA 79
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREV 45
EF-hand_6 pfam13405
EF-hand domain;
35-64 6.76e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 6.76e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 665389890   35 EFKEAFNMIDQNRDGFVEKEDLHDMLASLG 64
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 36-101 8.31e-05

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: 38.87  E-value: 8.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665389890  36 FKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMmneaPGPINFTMFLTLFGERLQGTDP 101
Cdd:cd22949    5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 35-63 9.58e-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: 37.74  E-value: 9.58e-05
                           10        20
                   ....*....|....*....|....*....
gi 665389890    35 EFKEAFNMIDQNRDGFVEKEDLHDMLASL 63
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-166 3.97e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389890  32 QIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLgknpTDDYLDGMMNEAPGPINFTMFLTlFGERLQGTDPEDVIKNAFGC 111
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL----WATLFSEADTDGDGRISREEFVA-GMESLFEATVEPFARAAFDL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665389890 112 FDEENMGVLPEDRLRELLTTMGdrFTDEDVDEMYREA-PIKNGLFDYLEFTRILKH 166
Cdd:COG5126   78 LDTDGDGKISADEFRRLLTALG--VSEEEADELFARLdTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
37-92 7.77e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.46  E-value: 7.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389890   37 KEAFNMIDQNRDGFVEKEDLHDMLASL--GKNPTDDYLDGMMNEAP----GPINFTMFLTLF 92
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 35-63 1.48e-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: 34.68  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|....*....
gi 665389890   35 EFKEAFNMIDQNRDGFVEKEDLHDMLASL 63
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
 
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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