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Conserved domains on  [gi|32129214|ref|NP_061938|]
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N-terminal EF-hand calcium-binding protein 2 isoform 1 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040857)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to N-terminal EF-hand calcium-binding protein 1

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 ...
 288-358 1.07e-13

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: 65.75  E-value: 1.07e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214   288 VRQEMAVCPEQLSEFLDSLRQYLRGTTGVRNCFHITAVR-LSDGFTFVIYEFWETEEAWKRHLQSPLCKAFR 358
Cdd:pfam03992   3 VVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRsLEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
59-130 1.93e-09

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.57  E-value: 1.93e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214  59 RGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKElcdyFVDHMGDY 130
Cdd:COG5126  65 ATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEE----FVAAVRDY 132
PTZ00440 super family cl36566
reticulocyte binding protein 2-like protein; Provisional
 79-211 2.73e-03

reticulocyte binding protein 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00440:

Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129214    79 KLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKELCDYFVDH----MGDYEDVLASLETL---NHSVLK--AMG 149
Cdd:PTZ00440  357 KFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETLLDSEYFISKytniISLSEHTLKAAEDVlkeNSQKIAdyALY 436

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32129214   150 YTKKVYEGGSNVDQFVTRflLKETANQIQSLLSSVESAVEAIEEQTSQL-RQNHIKPSHSAAQ 211
Cdd:PTZ00440  437 SNLEIIEIKKKYDEKINE--LKKSINQLKTLISIMKSFYDLIISEKDSMdSKEKKESSDSNYQ 497
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 288-358 1.07e-13

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: 65.75  E-value: 1.07e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214   288 VRQEMAVCPEQLSEFLDSLRQYLRGTTGVRNCFHITAVR-LSDGFTFVIYEFWETEEAWKRHLQSPLCKAFR 358
Cdd:pfam03992   3 VVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRsLEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
59-130 1.93e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.57  E-value: 1.93e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214  59 RGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKElcdyFVDHMGDY 130
Cdd:COG5126  65 ATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEE----FVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-121 3.02e-07

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: 47.16  E-value: 3.02e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32129214  65 ILDIFRRADKNDDGKLSLEEFQLFF--ADGVLNEKELEDLFHTIDSDNTNHVDTKELCD 121
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
64-123 4.00e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32129214    64 VILDIFRRADKNDDGKLSLEEFQLFFA----DGVLNEKELEDLFHTIDSDNTNHVDTKELCDYF 123
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
296-358 3.16e-06

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 44.94  E-value: 3.16e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32129214 296 PEQLSEFLDSLRQYLRGTTGVRNCFHITAVR-LSDGFTFVIYEFWETEEAWKRHLQSPLCKAFR 358
Cdd:COG1359  11 PGKRDEFLAALRELVEATRAEPGCLSYELYRdPDDPNRFVLYERWEDEAALEAHLASPHFKAFL 74
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 79-211 2.73e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129214    79 KLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKELCDYFVDH----MGDYEDVLASLETL---NHSVLK--AMG 149
Cdd:PTZ00440  357 KFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETLLDSEYFISKytniISLSEHTLKAAEDVlkeNSQKIAdyALY 436

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32129214   150 YTKKVYEGGSNVDQFVTRflLKETANQIQSLLSSVESAVEAIEEQTSQL-RQNHIKPSHSAAQ 211
Cdd:PTZ00440  437 SNLEIIEIKKKYDEKINE--LKKSINQLKTLISIMKSFYDLIISEKDSMdSKEKKESSDSNYQ 497
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 65-90 5.80e-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: 5.80e-03
                           10        20
                   ....*....|....*....|....*.
gi 32129214     65 ILDIFRRADKNDDGKLSLEEFQLFFA 90
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 288-358 1.07e-13

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: 65.75  E-value: 1.07e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214   288 VRQEMAVCPEQLSEFLDSLRQYLRGTTGVRNCFHITAVR-LSDGFTFVIYEFWETEEAWKRHLQSPLCKAFR 358
Cdd:pfam03992   3 VVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRsLEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
59-130 1.93e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.57  E-value: 1.93e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214  59 RGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKElcdyFVDHMGDY 130
Cdd:COG5126  65 ATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEE----FVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-121 3.02e-07

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: 47.16  E-value: 3.02e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32129214  65 ILDIFRRADKNDDGKLSLEEFQLFF--ADGVLNEKELEDLFHTIDSDNTNHVDTKELCD 121
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
64-123 4.00e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 4.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32129214    64 VILDIFRRADKNDDGKLSLEEFQLFFA----DGVLNEKELEDLFHTIDSDNTNHVDTKELCDYF 123
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRkleeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
YgiN COG1359
Quinol monooxygenase YgiN [Energy production and conversion];
296-358 3.16e-06

Quinol monooxygenase YgiN [Energy production and conversion];


Pssm-ID: 440970  Cd Length: 91  Bit Score: 44.94  E-value: 3.16e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32129214 296 PEQLSEFLDSLRQYLRGTTGVRNCFHITAVR-LSDGFTFVIYEFWETEEAWKRHLQSPLCKAFR 358
Cdd:COG1359  11 PGKRDEFLAALRELVEATRAEPGCLSYELYRdPDDPNRFVLYERWEDEAALEAHLASPHFKAFL 74
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 64-127 7.45e-06

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share 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 C2 domain. PI-PLC-zeta lacks the PH 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. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 45.35  E-value: 7.45e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32129214  64 VILDIFRRADKNDDGKLSLEEF-QLFFADGV-LNEKELEDLFHTIDSDNTNHVDTKELCDYFVDHM 127
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIkKLLKRLNIrVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLT 66
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 65-144 7.83e-05

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share 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 C2 domain. PI-PLC-zeta lacks the PH 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. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 42.27  E-value: 7.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129214  65 ILDIFRRADKNDDGKLSLEEFQLFFADgvLNE-KELEDLFHTIDSDNTNHVDTKELCDYFVDHMG---DYEDVLASLETL 140
Cdd:cd15898  38 LKKLFKEVDTNGDGTLTFDEFEELYKS--LTErPELEPIFKKYAGTNRDYMTLEEFIRFLREEQGenvSEEECEELIEKY 115


                ....
gi 32129214 141 NHSV 144
Cdd:cd15898 116 EPER 119
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-119 3.10e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 3.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32129214  67 DIFRRADKNDDGKLSLEEFQLFFADGVLN--EKELEDLFHTIDSDNTNHVDTKEL 119
Cdd:COG5126  37 TLFSEADTDGDGRISREEFVAGMESLFEAtvEPFARAAFDLLDTDGDGKISADEF 91
EF-hand_8 pfam13833
EF-hand domain pair;
76-125 4.42e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 4.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 32129214    76 DDGKLSLEEFQLFFADGV---LNEKELEDLFHTIDSDNTNHVDTKELCDYFVD 125
Cdd:pfam13833   1 EKGVITREELKRALALLGlkdLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
EF-hand_5 pfam13202
EF hand;
65-88 5.37e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 5.37e-04
                          10        20
                  ....*....|....*....|....
gi 32129214    65 ILDIFRRADKNDDGKLSLEEFQLF 88
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRL 24
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 65-91 1.96e-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: 35.45  E-value: 1.96e-03
                          10        20
                  ....*....|....*....|....*..
gi 32129214    65 ILDIFRRADKNDDGKLSLEEFQLFFAD 91
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 79-211 2.73e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129214    79 KLSLEEFQLFFADGVLNEKELEDLFHTIDSDNTNHVDTKELCDYFVDH----MGDYEDVLASLETL---NHSVLK--AMG 149
Cdd:PTZ00440  357 KFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETLLDSEYFISKytniISLSEHTLKAAEDVlkeNSQKIAdyALY 436

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32129214   150 YTKKVYEGGSNVDQFVTRflLKETANQIQSLLSSVESAVEAIEEQTSQL-RQNHIKPSHSAAQ 211
Cdd:PTZ00440  437 SNLEIIEIKKKYDEKINE--LKKSINQLKTLISIMKSFYDLIISEKDSMdSKEKKESSDSNYQ 497
EF-hand_6 pfam13405
EF-hand domain;
65-89 3.57e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 3.57e-03
                          10        20
                  ....*....|....*....|....*
gi 32129214    65 ILDIFRRADKNDDGKLSLEEFQLFF 89
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKAL 26
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 69-132 4.66e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 38.33  E-value: 4.66e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32129214  69 FRRADKNDDGKLSLEEFQLF--------FADGVLNEKeLEDlfhtIDSDNTNHVDTKElcdyfvdHMGDYED 132
Cdd:cd16226 125 WKAADQDGDGKLTKEEFTAFlhpeefphMRDIVVQET-LED----IDKNKDGFISLEE-------YIGDMYR 184
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 65-90 5.80e-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: 5.80e-03
                           10        20
                   ....*....|....*....|....*.
gi 32129214     65 ILDIFRRADKNDDGKLSLEEFQLFFA 90
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
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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