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Conserved domains on  [gi|21357187|ref|NP_649568|]
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ethanol sensitive with low memory, isoform A [Drosophila melanogaster]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-174 1.35e-10

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187  27 QIERLYSRFTSLDRNDCGTLSREDLMRIPELAINPLcerivHSFFAESNDDRVNFRQFMNVLAHFRPlrdnkqsklNSRE 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL-----FSEADTDGDGRISREEFVAGMESLFE---------ATVE 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357187 107 EKLKFAFKMYDLDDDGVISRDELLSilhMMVGANISQDQLVSIAERTILEADlccqGKISFEDFCKAL 174
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRR---LLTALGVSEEEADELFARLDTDGD----GKISFEEFVAAV 129
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-174 1.35e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187  27 QIERLYSRFTSLDRNDCGTLSREDLMRIPELAINPLcerivHSFFAESNDDRVNFRQFMNVLAHFRPlrdnkqsklNSRE 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL-----FSEADTDGDGRISREEFVAGMESLFE---------ATVE 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357187 107 EKLKFAFKMYDLDDDGVISRDELLSilhMMVGANISQDQLVSIAERTILEADlccqGKISFEDFCKAL 174
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRR---LLTALGVSEEEADELFARLDTDGD----GKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
108-174 3.43e-09

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: 51.01  E-value: 3.43e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357187 108 KLKFAFKMYDLDDDGVISRDELLSILHMMvGANISQDQLvsiaERTILEADLCCQGKISFEDFCKAL 174
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
106-174 3.93e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 3.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357187   106 EEKLKFAFKMYDLDDDGVISRDELLSILHMMVGANISQDQLVsiaERTILEADLCCQGKISFEDFCKAL 174
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEV---EELFKEFDLDKDGRISFEEFLELY 66
PTZ00183 PTZ00183
centrin; Provisional
19-177 7.62e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 52.38  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   19 EETGFTPNQIERLYSRFTSLDRNDCGTLSREDL---MRipELAINPLCERIvHSFFAE---SNDDRVNFRQFMNVLAhfr 92
Cdd:PTZ00183   7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELkvaMR--SLGFEPKKEEI-KQMIADvdkDGSGKIDFEEFLDIMT--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   93 plrdNKQSKLNSREEKLKfAFKMYDLDDDGVISRDELLSILHMMvGANISQDQLvsiaERTILEADLCCQGKISFEDFCK 172
Cdd:PTZ00183  81 ----KKLGERDPREEILK-AFRLFDDDKTGKISLKNLKRVAKEL-GETITDEEL----QEMIDEADRNGDGEISEEEFYR 150

                 ....*
gi 21357187  173 ALDRT 177
Cdd:PTZ00183 151 IMKKT 155
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
108-136 3.36e-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: 33.89  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*....
gi 21357187    108 KLKFAFKMYDLDDDGVISRDELLSILHMM 136
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-174 1.35e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187  27 QIERLYSRFTSLDRNDCGTLSREDLMRIPELAINPLcerivHSFFAESNDDRVNFRQFMNVLAHFRPlrdnkqsklNSRE 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL-----FSEADTDGDGRISREEFVAGMESLFE---------ATVE 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357187 107 EKLKFAFKMYDLDDDGVISRDELLSilhMMVGANISQDQLVSIAERTILEADlccqGKISFEDFCKAL 174
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRR---LLTALGVSEEEADELFARLDTDGD----GKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
108-174 3.43e-09

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: 51.01  E-value: 3.43e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357187 108 KLKFAFKMYDLDDDGVISRDELLSILHMMvGANISQDQLvsiaERTILEADLCCQGKISFEDFCKAL 174
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
106-174 3.93e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 3.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357187   106 EEKLKFAFKMYDLDDDGVISRDELLSILHMMVGANISQDQLVsiaERTILEADLCCQGKISFEDFCKAL 174
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEV---EELFKEFDLDKDGRISFEEFLELY 66
PTZ00183 PTZ00183
centrin; Provisional
19-177 7.62e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 52.38  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   19 EETGFTPNQIERLYSRFTSLDRNDCGTLSREDL---MRipELAINPLCERIvHSFFAE---SNDDRVNFRQFMNVLAhfr 92
Cdd:PTZ00183   7 ERPGLTEDQKKEIREAFDLFDTDGSGTIDPKELkvaMR--SLGFEPKKEEI-KQMIADvdkDGSGKIDFEEFLDIMT--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   93 plrdNKQSKLNSREEKLKfAFKMYDLDDDGVISRDELLSILHMMvGANISQDQLvsiaERTILEADLCCQGKISFEDFCK 172
Cdd:PTZ00183  81 ----KKLGERDPREEILK-AFRLFDDDKTGKISLKNLKRVAKEL-GETITDEEL----QEMIDEADRNGDGEISEEEFYR 150

                 ....*
gi 21357187  173 ALDRT 177
Cdd:PTZ00183 151 IMKKT 155
PTZ00184 PTZ00184
calmodulin; Provisional
24-174 2.81e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.53  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   24 TPNQIERLYSRFTSLDRNDCGTLSREDL---MRipELAINPlCERIVHSFFAESNDD---RVNFRQFMNVLAhfrplrdn 97
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELgtvMR--SLGQNP-TEAELQDMINEVDADgngTIDFPEFLTLMA-------- 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357187   98 KQSKLNSREEKLKFAFKMYDLDDDGVISRDELLSILHMMvGANISQDQlvsiAERTILEADLCCQGKISFEDFCKAL 174
Cdd:PTZ00184  75 RKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEE----VDEMIREADVDGDGQINYEEFVKMM 146
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
9-140 2.11e-04

serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This subfamily includes protein phosphatase subunit G5PR (also known as serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma, G4-1, G5pr, GDRM, SPGF36, or C14orf10) that is encoded by the PPP2R3C gene. It is involved in the control of the dynamic organization of the cortical cytoskeleton and plays an important role in the organization of interphase microtubule arrays in part through the regulation of nucleation geometry. G5PR is involved in the ontogeny of multiple organs, especially critical for testis development and spermatogenesis. PPP2R3C gene variants cause syndromic 46,XY gonadal dysgenesis and impaired spermatogenesis in humans, and thus is emerging as a potential therapeutic target for male infertility.


Pssm-ID: 410338 [Multi-domain]  Cd Length: 382  Bit Score: 41.02  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357187   9 LRNEEIAQIQEETG-FTPNQIERLYSRFTSLDRNDCGTLSREDLMRIPELAINPL-CERIvhsfFAESN--DDRVNFRQF 84
Cdd:cd21505 200 LRDEELSEELQESNwFSAPSALRVYGQYLNLDKDHNGMLSKQELSRYGKGTLTSVfIDRV----FQECLtyNGEMDYKTF 275
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357187  85 MN-VLAHfrplrDNKQSKlnsreEKLKFAFKMYDLDDDGVISRDELLS----ILHMMVGAN 140
Cdd:cd21505 276 LDfVLAM-----ENRKEP-----QALQYFFRILDLKGQGYLTPFTLNYffraIQEKMKEHG 326
EF-hand_6 pfam13405
EF-hand domain;
108-136 9.98e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 9.98e-04
                          10        20
                  ....*....|....*....|....*....
gi 21357187   108 KLKFAFKMYDLDDDGVISRDELLSILHMM 136
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
105-176 1.02e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 1.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357187 105 REEKLKFAFKMYDLDDDGVISRDELLSILHMMVganisqdqlvsiaERTILEADLCCQGKISFEDFCKALDR 176
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLW-------------ATLFSEADTDGDGRISREEFVAGMES 61
EF-hand_8 pfam13833
EF-hand domain pair;
120-176 1.82e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.98  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21357187   120 DDGVISRDELLSILHMMVGANISQDQLVSIaertILEADLCCQGKISFEDFCKALDR 176
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDIL----FREFDTDGDGYISFDEFCVLLER 53
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
108-136 2.20e-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: 34.30  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 21357187   108 KLKFAFKMYDLDDDGVISRDELLSILHMM 136
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
108-136 3.36e-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: 33.89  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*....
gi 21357187    108 KLKFAFKMYDLDDDGVISRDELLSILHMM 136
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 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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