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Conserved domains on  [gi|442618714|ref|NP_001262501|]
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uncharacterized protein Dmel_CG33098, 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
 75-221 1.32e-17

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 76.34  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  75 PHELDIAKLAELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAKE----PLDYEAFVRLMSRRTQELD 150
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMKDTD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442618714 151 PEDVLLEAWSKWDDHGTGKIDERKIYEELTNYGDKMTLNEAKEALSHApmakpkSLEEPPMIDYPAFCRML 221
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREA------DVDGDGQINYEEFVKMM 146
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 75-221 1.32e-17

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 76.34  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  75 PHELDIAKLAELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAKE----PLDYEAFVRLMSRRTQELD 150
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMKDTD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442618714 151 PEDVLLEAWSKWDDHGTGKIDERKIYEELTNYGDKMTLNEAKEALSHApmakpkSLEEPPMIDYPAFCRML 221
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREA------DVDGDGQINYEEFVKMM 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 85-143 3.26e-08

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: 48.70  E-value: 3.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442618714  85 ELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAKEP----LDYEAFVRLMS 143
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDgdgkIDFEEFLELMA 63
EF-hand_6 pfam13405
EF-hand domain;
85-114 9.29e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 442618714   85 ELKEVFSLFDTDCDGLISKDDLRFTYTALG 114
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-142 3.35e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  64 PEEMRAddnVAPHELDIAKLAELKEVFSLFDTDCDGLISKDDLRFTYTALG--NEPNEQLLEQMMQEAKEPLDYEAFVRL 141
Cdd:COG5126   52 REEFVA---GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEFVAA 128


                 .
gi 442618714 142 M 142
Cdd:COG5126  129 V 129
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 85-107 5.32e-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: 33.51  E-value: 5.32e-03
                           10        20
                   ....*....|....*....|...
gi 442618714    85 ELKEVFSLFDTDCDGLISKDDLR 107
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFK 23
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 75-221 1.32e-17

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 76.34  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  75 PHELDIAKLAELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAKE----PLDYEAFVRLMSRRTQELD 150
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMKDTD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442618714 151 PEDVLLEAWSKWDDHGTGKIDERKIYEELTNYGDKMTLNEAKEALSHApmakpkSLEEPPMIDYPAFCRML 221
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREA------DVDGDGQINYEEFVKMM 146
PTZ00183 PTZ00183
centrin; Provisional
 85-198 3.12e-13

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 65.10  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  85 ELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAK----EPLDYEAFVRLMSRRTQELDPEDVLLEAWS 160
Cdd:PTZ00183  18 EIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDkdgsGKIDFEEFLDIMTKKLGERDPREEILKAFR 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442618714 161 KWDDHGTGKIDERKIYEELTNYGDKMTLNEAKEALSHA 198
Cdd:PTZ00183  98 LFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEA 135
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 85-143 3.26e-08

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: 48.70  E-value: 3.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442618714  85 ELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEAKEP----LDYEAFVRLMS 143
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDgdgkIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 85-145 1.11e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.76  E-value: 1.11e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442618714  85 ELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMMQEA----KEPLDYEAFVRLMSRR 145
Cdd:PTZ00184  85 EIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAdvdgDGQINYEEFVKMMMSK 149
EF-hand_6 pfam13405
EF-hand domain;
85-114 9.29e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 442618714   85 ELKEVFSLFDTDCDGLISKDDLRFTYTALG 114
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_7 pfam13499
EF-hand domain pair;
85-129 4.56e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 4.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442618714   85 ELKEVFSLFDTDCDGLISKDDLRFTYTAL--GNEPNEQLLEQMMQEA 129
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEF 49
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 82-190 2.84e-03

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 37.18  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  82 KLAELKEVFSLFDTDCDGLISKDDLRFTYTALGNEPNEQLLEQMM---QEAKEPLDYEAFVRLMSRrtqeldpedvlLEA 158
Cdd:cd16195   71 KLRKYKDIFQKADVSKSGFLSLSELRNAIQAAGIRVSDDLLNLMAlryGDSSGRISFESFICLMLR-----------LEC 139

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442618714 159 WSkwddhgtgkiderKIYEELTNYGDKMTLNE 190
Cdd:cd16195  140 MA-------------KIFRNLSKDGGGIYLTE 158
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-142 3.35e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618714  64 PEEMRAddnVAPHELDIAKLAELKEVFSLFDTDCDGLISKDDLRFTYTALG--NEPNEQLLEQMMQEAKEPLDYEAFVRL 141
Cdd:COG5126   52 REEFVA---GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGvsEEEADELFARLDTDGDGKISFEEFVAA 128


                 .
gi 442618714 142 M 142
Cdd:COG5126  129 V 129
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 85-107 5.32e-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: 33.51  E-value: 5.32e-03
                           10        20
                   ....*....|....*....|...
gi 442618714    85 ELKEVFSLFDTDCDGLISKDDLR 107
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFK 23
 
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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