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Conserved domains on  [gi|1824163928|ref|NP_001366078|]
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N-terminal EF-hand calcium-binding protein 3 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 222-294 4.18e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


:

Pssm-ID: 427635  Cd Length: 74  Bit Score: 52.27  E-value: 4.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824163928 222 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 294
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3-43 6.44e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 6.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 43
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 222-294 4.18e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 52.27  E-value: 4.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824163928 222 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 294
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3-43 6.44e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 6.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 43
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
227-310 7.00e-05

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 41.09  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824163928 227 QVQVAEDALQDFHRALCCYMNFTGAQSHCLHVS-AQKMLDNAAFTLYEFWQDEASWRRHQQSPCSKAFQRTLIDHLQAPD 305
Cdd:COG1359     6 KLTVKPGKRDEFLAALRELVEATRAEPGCLSYElYRDPDDPNRFVLYERWEDEAALEAHLASPHFKAFLAALAPLLAEPP 85


                  ....*
gi 1824163928 306 TLTTV 310
Cdd:COG1359    86 EVRVY 90
EF-hand_7 pfam13499
EF-hand domain pair;
1-43 5.84e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 5.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1824163928   1 MFQVFRRADKNDDGKLSFEEFQNYFA----DGVLSSAELRELFSGID 43
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFD 50
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4-43 8.23e-04

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: 37.14  E-value: 8.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1824163928   4 VFRRADKNDDGKLSFEEFQNYF--ADGVLSSAELRELFSGID 43
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVD 46
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 222-294 4.18e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 52.27  E-value: 4.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824163928 222 LVAQRQVQVAEDALQDFHRALCCYMNFTGAQSHCLHVSAQKMLDNA-AFTLYEFWQDEASWRRHQQSPCSKAFQ 294
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPdEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3-43 6.44e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 6.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYFADGVLSSAELRELFSGID 43
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLD 113
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
227-310 7.00e-05

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 41.09  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824163928 227 QVQVAEDALQDFHRALCCYMNFTGAQSHCLHVS-AQKMLDNAAFTLYEFWQDEASWRRHQQSPCSKAFQRTLIDHLQAPD 305
Cdd:COG1359     6 KLTVKPGKRDEFLAALRELVEATRAEPGCLSYElYRDPDDPNRFVLYERWEDEAALEAHLASPHFKAFLAALAPLLAEPP 85


                  ....*
gi 1824163928 306 TLTTV 310
Cdd:COG1359    86 EVRVY 90
EF-hand_7 pfam13499
EF-hand domain pair;
1-43 5.84e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 5.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1824163928   1 MFQVFRRADKNDDGKLSFEEFQNYFA----DGVLSSAELRELFSGID 43
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFD 50
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4-43 8.23e-04

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: 37.14  E-value: 8.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1824163928   4 VFRRADKNDDGKLSFEEFQNYF--ADGVLSSAELRELFSGID 43
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVD 46
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3-27 3.11e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 3.11e-03
                          10        20
                  ....*....|....*....|....*
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYFAD 27
Cdd:COG5126   107 ELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_5 pfam13202
EF hand;
3-23 3.31e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 34.60  E-value: 3.31e-03
                          10        20
                  ....*....|....*....|.
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQN 23
Cdd:pfam13202   3 DTFRQIDLNGDGKISKEELRR 23
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 3-27 3.57e-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: 3.57e-03
                          10        20
                  ....*....|....*....|....*
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYFAD 27
Cdd:pfam00036   4 EIFRLFDKDGDGKIDFEEFKELLKK 28
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 3-22 5.96e-03

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: 34.83  E-value: 5.96e-03
                          10        20
                  ....*....|....*....|
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQ 22
Cdd:cd00051    40 EMIREVDKDGDGKIDFEEFL 59
EF-hand_6 pfam13405
EF-hand domain;
1-25 8.58e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.30  E-value: 8.58e-03
                          10        20
                  ....*....|....*....|....*
gi 1824163928   1 MFQVFRRADKNDDGKLSFEEFQNYF 25
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKAL 26
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 4-58 8.74e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 36.05  E-value: 8.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1824163928   4 VFRRADKNDDGKLSFEEFQNYFADgVLSSAELRELFSGIDDHlTDNLETEKLCDY 58
Cdd:cd16202    41 LFQEADTSGEDVLDEEEFVQFYNR-LTKRPEIEELFKKYSGD-DEALTVEELRRF 93
EF-hand_7 pfam13499
EF-hand domain pair;
3-25 8.83e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.54  E-value: 8.83e-03
                          10        20
                  ....*....|....*....|...
gi 1824163928   3 QVFRRADKNDDGKLSFEEFQNYF 25
Cdd:pfam13499  44 ELFKEFDLDKDGRISFEEFLELY 66
 
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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