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Conserved domains on  [gi|110590202|pdb|2G9B|A]
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Chain A, Calbindin

Protein Classification

EFh_HEF_CB domain-containing protein( domain architecture ID 11610852)

EFh_HEF_CB domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 18-261 6.30e-158

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


:

Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 438.50  E-value: 6.30e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRcQ 97
Cdd:cd16176   1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLELSDQMKAFVDQYGQSTDGKIGIVELAQILPTEENFLLFFR-Q 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       98 QLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQE 177
Cdd:cd16176  80 QLKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARLLPVQE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      178 NFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALI 257
Cdd:cd16176 160 NFLLKFQGVKMCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSDGGKLYRTELALI 239


                ....
2G9B_A      258 LSAG 261
Cdd:cd16176 240 LCAE 243
 
Name Accession Description Interval E-value
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 18-261 6.30e-158

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 438.50  E-value: 6.30e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRcQ 97
Cdd:cd16176   1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLELSDQMKAFVDQYGQSTDGKIGIVELAQILPTEENFLLFFR-Q 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       98 QLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQE 177
Cdd:cd16176  80 QLKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARLLPVQE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      178 NFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALI 257
Cdd:cd16176 160 NFLLKFQGVKMCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSDGGKLYRTELALI 239


                ....
2G9B_A      258 LSAG 261
Cdd:cd16176 240 LCAE 243
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-219 2.10e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      103 EEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVD---DTKL--AEYTDLMLK---------------LFDSNNDG 162
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADtdgDGRIsrEEFVAGMESlfeatvepfaraafdLLDTDGDG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
2G9B_A      163 KLELTEMARLLpvqenfllkfQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKD 219
Cdd:COG5126  85 KISADEFRRLL----------TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
103-173 3.47e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.48  E-value: 3.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2G9B_A        103 EEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDtklaeyTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 16-173 1.07e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A        16 SQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLElspEMKTFVDQYGqrdDGKIGIVElahvlpteenFLLLF- 94
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQ---DMINEVDADG---NGTIDFPE----------FLTLMa 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A        95 -RCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKtvddtklaEYTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:PTZ00184  75 rKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTD--------EEVDEMIREADVDGDGQINYEEFVKMM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 192-220 4.91e-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: 39.28  E-value: 4.91e-05
                           10        20
                   ....*....|....*....|....*....
2G9B_A         192 EFNKAFELYDQDGNGYIDENELDALLKDL 220
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 18-261 6.30e-158

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 438.50  E-value: 6.30e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRcQ 97
Cdd:cd16176   1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLELSDQMKAFVDQYGQSTDGKIGIVELAQILPTEENFLLFFR-Q 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       98 QLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQE 177
Cdd:cd16176  80 QLKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARLLPVQE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      178 NFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALI 257
Cdd:cd16176 160 NFLLKFQGVKMCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSDGGKLYRTELALI 239


                ....
2G9B_A      258 LSAG 261
Cdd:cd16176 240 LCAE 243
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 18-261 1.12e-108

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 314.29  E-value: 1.12e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQARK---KAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLF 94
Cdd:cd15902   1 FMEVWMHFDADGNGYIEGKELDSFLRELLKALNgkdKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILPTEENFLLLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       95 RC-QQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:cd15902  81 RReQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAKLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      174 PVQENFLLKFQ---GIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSD---GG 247
Cdd:cd15902 161 PVQENFLLKFQilgAMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENFRDAILRACDknkDG 240

                       250
                ....*....|....
2G9B_A      248 KLYRTDLALILSAG 261
Cdd:cd15902 241 KIQKTELALFLSAK 254
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 18-258 1.10e-107

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t specific neurons of the central and peripheral nervous system. It possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 311.42  E-value: 1.10e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLE-----LSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLL 92
Cdd:cd16177   1 FLEIWKHFDADGNGYIEGKELENFFRELERARRGAGVDsksanFGEKMKEFMQKYDKNADGRIEMAELAQILPTEENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       93 LFRcQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARL 172
Cdd:cd16177  81 CFR-QHVGSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEMARL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      173 LPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRT 252
Cdd:cd16177 160 LPVQENFLLKFQGMKLSSEEFNAIFAFYDKDGSGYIDENELDALLKDLYEKNKKEMDIQQLTNYKKSIMSLSDGGKLYRK 239


                ....*.
2G9B_A      253 DLALIL 258
Cdd:cd16177 240 ELEMVL 245
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 18-258 3.94e-71

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 219.20  E-value: 3.94e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQA--RKKAGLELSPE------MKTFVDQYGQRDDGKIGIVELAHVLPTEEN 89
Cdd:cd16179   1 FMDVWNHYDTDGNGYIEGTELDGFLREFVSSvnPEDVGPEVVSEtaleelKEEFMEAYDENQDGRIDIRELAQLLPTEEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       90 FLLLFRCQQ-LKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVD--DTKLAEYTDLMLKLFDSNNDGKLEL 166
Cdd:cd16179  81 FLLLFRRDNpLDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLLKEAKRDNDvsEDKLIEYTDTILQLFDRNKDGKLQL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      167 TEMARLLPVQENFLLK--FQGI-KMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMAL 243
Cdd:cd16179 161 SEMARLLPVKENFLCRpiFKGAgKLTREDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEIILRG 240

                       250
                ....*....|....*...
2G9B_A      244 SD---GGKLYRTDLALIL 258
Cdd:cd16179 241 WDfnnDGKISRKELTMLL 258
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 18-259 1.05e-68

EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 212.65  E-value: 1.05e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       18 FFEIWLHFDADGSGYLEGKELQNLIQELLQ---ARKKAGLELSPEMKT-FVDQYGQRDDGKIGIVELAHVLPTEENFLLL 93
Cdd:cd16178   1 FAEIWQHFDADESGYIEGKELDNFFKDLLKklgTKDTISADEVQDVKEcFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       94 F--RCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMAR 171
Cdd:cd16178  81 FfrREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      172 LLPVQENFLLKFQGIKMCGKE----FNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSD-- 245
Cdd:cd16178 161 ILALQENFLLQFKMDAMSEEErkrdFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDvn 240

                       250
                ....*....|....*
2G9B_A      246 -GGKLYRTDLALILS 259
Cdd:cd16178 241 kDGKIQKSELALCLG 255
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 104-220 6.73e-11

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 59.46  E-value: 6.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      104 EFMKTWRKYDTDHSGFIETEELKNFLKDLlekanktvDDTKLAEYT-DLMLKLFDSNNDGKLELTEMARLLpvqeNFLLK 182
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALSNG--------DWTPFSIETvRLMINMFDRDRSGTINFDEFVGLW----KYIQD 68

                        90       100       110
                ....*....|....*....|....*....|....*...
2G9B_A      183 FQGIkmcgkefnkaFELYDQDGNGYIDENELDALLKDL 220
Cdd:cd16180  69 WRRL----------FRRFDRDRSGSIDFNELQNALSSF 96
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 104-173 1.23e-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: 52.94  E-value: 1.23e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      104 EFMKTWRKYDTDHSGFIETEELKNFLKDLLEKanktvddtKLAEYTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEG--------LSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-219 2.10e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      103 EEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVD---DTKL--AEYTDLMLK---------------LFDSNNDG 162
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADtdgDGRIsrEEFVAGMESlfeatvepfaraafdLLDTDGDG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
2G9B_A      163 KLELTEMARLLpvqenfllkfQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKD 219
Cdd:COG5126  85 KISADEFRRLL----------TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 152-218 3.98e-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: 49.08  E-value: 3.98e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2G9B_A      152 MLKLFDSNNDGKLELTEMARLLPVQenfllkfqGIKMCGKEFNKAFELYDQDGNGYIDENELDALLK 218
Cdd:cd00051   5 AFRLFDKDGDGTISADELKAALKSL--------GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-173 8.50e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 8.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       24 HFDADGSGYLEGKELQNLIQELLQarkkaglelspemkTFVDQYGQRDDGKIgivelahvlpTEENFLLLFRCQQLKSCE 103
Cdd:COG5126  13 LLDADGDGVLERDDFEALFRRLWA--------------TLFSEADTDGDGRI----------SREEFVAGMESLFEATVE 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2G9B_A      104 EFMKTW-RKYDTDHSGFIETEELKNFLKDLlekankTVDDTKLAEytdlMLKLFDSNNDGKLELTEMARLL 173
Cdd:COG5126  69 PFARAAfDLLDTDGDGKISADEFRRLLTAL------GVSEEEADE----LFARLDTDGDGKISFEEFVAAV 129
EF-hand_7 pfam13499
EF-hand domain pair;
103-173 3.47e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.48  E-value: 3.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2G9B_A        103 EEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDtklaeyTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLELY 66
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 113-217 4.81e-07

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 48.41  E-value: 4.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      113 DTDHSGFIETEELKNflkdLLEKAN-KTVDDtklaEYTDLMLKLFDSNNDGKLELTEMARLLpvqeNFLLKFQGIkmcgk 191
Cdd:cd16184  10 DRDRSGKISAKELQQ----ALVNGNwSHFND----ETCRLMIGMFDKDKSGTIDIYEFQALW----NYIQQWKQV----- 72

                        90       100
                ....*....|....*....|....*.
2G9B_A      192 efnkaFELYDQDGNGYIDENELDALL 217
Cdd:cd16184  73 -----FQQFDRDRSGSIDENELHQAL 93
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 113-212 4.76e-06

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 45.67  E-value: 4.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      113 DTDHSGFIETEELKNflkdLLEKANKTVDDtklaEYTDLMLKLFDSNNDGKLELTEMARLlpvqENFLLKFQGikmcgke 192
Cdd:cd16185  10 DRDRSGSIDVNELQK----ALAGGGLLFSL----ATAEKLIRMFDRDGNGTIDFEEFAAL----HQFLSNMQN------- 70

                        90       100
                ....*....|....*....|
2G9B_A      193 fnkAFELYDQDGNGYIDENE 212
Cdd:cd16185  71 ---GFEQRDTSRSGRLDANE 87
PTZ00184 PTZ00184
calmodulin; Provisional
 16-173 1.07e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A        16 SQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLElspEMKTFVDQYGqrdDGKIGIVElahvlpteenFLLLF- 94
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQ---DMINEVDADG---NGTIDFPE----------FLTLMa 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A        95 -RCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKtvddtklaEYTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:PTZ00184  75 rKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTD--------EEVDEMIREADVDGDGQINYEEFVKMM 146
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 100-172 1.19e-05

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 43.18  E-value: 1.19e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2G9B_A      100 KSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDdtklAEyTDLMLKLFDSNNDGKLELTEMARL 172
Cdd:cd16255  31 KSADDVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGARELTD----AE-TKAFLKAGDSDGDGKIGVEEFQAL 98
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 104-219 3.84e-05

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 42.80  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      104 EFMKTWRKYDTDhSGFIETEELKNFLKdllEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLpvqeNFLLKF 183
Cdd:cd15897   1 QLRNVFQAVAGD-DGEISATELQQALS---NVGWTHFDLGFSLETCRSMIAMMDRDHSGKLNFSEFKGLW----NYIKAW 72

                        90       100       110
                ....*....|....*....|....*....|....*.
2G9B_A      184 QGIkmcgkefnkaFELYDQDGNGYIDENELDALLKD 219
Cdd:cd15897  73 QEI----------FRTYDTDGSGTIDSNELRQALSG 98
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 192-220 4.91e-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: 39.28  E-value: 4.91e-05
                           10        20
                   ....*....|....*....|....*....
2G9B_A         192 EFNKAFELYDQDGNGYIDENELDALLKDL 220
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 105-219 6.57e-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: 41.88  E-value: 6.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      105 FMKTWRKYDTDHSGFIETEELKNflkdLLEKANKTVDDTKLAEytdlMLKLFDSNNDGKLELTEMARLLpvqenFLLKFQ 184
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKK----LLKRLNIRVSEKELKK----LFKEVDTNGDGTLTFDEFEELY-----KSLTER 68

                        90       100       110
                ....*....|....*....|....*....|....*
2G9B_A      185 gikmcgKEFNKAFELYDQDGNGYIDENELDALLKD 219
Cdd:cd15898  69 ------PELEPIFKKYAGTNRDYMTLEEFIRFLRE 97
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 192-227 7.25e-05

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: 39.84  E-value: 7.25e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
2G9B_A      192 EFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQE 227
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE 36
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 100-172 8.48e-05

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 40.62  E-value: 8.48e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2G9B_A      100 KSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDdtklAEyTDLMLKLFDSNNDGKLELTEMARL 172
Cdd:cd16253  31 KSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGARVLSD----KE-TKNFLAAGDSDGDGKIGVDEFKSM 98
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 100-172 1.16e-04

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 40.21  E-value: 1.16e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2G9B_A      100 KSCEEFMKTWRKYDTDHSGFIETEELKNFLKDlLEKANKTVDDTKlaeyTDLMLKLFDSNNDGKLELTEMARL 172
Cdd:cd16251  31 KSEDQIKKVFQILDKDKSGFIEEEELKYILKG-FSIAGRDLTDEE----TKALLAAGDTDGDGKIGVEEFATL 98
PTZ00184 PTZ00184
calmodulin; Provisional
 103-229 1.60e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.90  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       103 EEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKtvddtklAEYTDlMLKLFDSNNDGKLELTE----MARLLPVQEN 178
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTE-------AELQD-MINEVDADGNGTIDFPEfltlMARKMKDTDS 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
2G9B_A       179 fllkfqgikmcGKEFNKAFELYDQDGNGYIDENELDALLKDLCEK-NKQELD 229
Cdd:PTZ00184  83 -----------EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKlTDEEVD 123
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 192-220 2.25e-04

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: 37.38  E-value: 2.25e-04
                          10        20
                  ....*....|....*....|....*....
2G9B_A        192 EFNKAFELYDQDGNGYIDENELDALLKDL 220
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
PTZ00183 PTZ00183
centrin; Provisional
 25-173 3.02e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.44  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A        25 FDADGSGYLEGKELQNLIQELLQARKKaglelsPEMKTFVDQYGQRDDGKIGIVELAHVLPTeenflllfRCQQLKSCEE 104
Cdd:PTZ00183  26 FDTDGSGTIDPKELKVAMRSLGFEPKK------EEIKQMIADVDKDGSGKIDFEEFLDIMTK--------KLGERDPREE 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2G9B_A       105 FMKTWRKYDTDHSGFIETEELKNFLKDLLEkankTVDDTKLAEytdlMLKLFDSNNDGKLELTEMARLL 173
Cdd:PTZ00183  92 ILKAFRLFDDDKTGKISLKNLKRVAKELGE----TITDEELQE----MIDEADRNGDGEISEEEFYRIM 152
EF-hand_7 pfam13499
EF-hand domain pair;
152-212 3.06e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 3.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
2G9B_A        152 MLKLFDSNNDGKLELTEMARLLpvqENFLLkfqGIKMCGKEFNKAFELYDQDGNGYIDENE 212
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLL---RKLEE---GEPLSDEEVEELFKEFDLDKDGRISFEE 61
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 25-121 6.44e-04

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.43  E-value: 6.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       25 FDADGSGYLEGKELQNLIQELlqarkkaGLELSPEM-KTFVDQYGQRDDGKIGivelahvlptEENFLLLfrCQQLKSCE 103
Cdd:cd16180  76 FDRDRSGSIDFNELQNALSSF-------GYRLSPQFvQLLVRKFDRRRRGSIS----------FDDFVEA--CVTLKRLT 136

                        90
                ....*....|....*...
2G9B_A      104 EfmkTWRKYDTDHSGFIE 121
Cdd:cd16180 137 D---AFRKYDTNRTGYAT 151
EF-hand_6 pfam13405
EF-hand domain;
192-220 7.18e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 7.18e-04
                          10        20
                  ....*....|....*....|....*....
2G9B_A        192 EFNKAFELYDQDGNGYIDENELDALLKDL 220
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 104-132 8.86e-04

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: 35.82  E-value: 8.86e-04
                           10        20
                   ....*....|....*....|....*....
2G9B_A         104 EFMKTWRKYDTDHSGFIETEELKNFLKDL 132
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 25-120 1.34e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 38.40  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A       25 FDADGSGYLEGKELQNLIQELlqarkkaGLELSPEMKTF-VDQYGQRDDGKIGIvelahvlpteENFLLLfrCQQLKSce 103
Cdd:cd16184  76 FDRDRSGSIDENELHQALSQM-------GYRLSPQFVQFlVSKYDPRARRSLTL----------DQFIQV--CVQLQS-- 134

                        90
                ....*....|....*..
2G9B_A      104 eFMKTWRKYDTDHSGFI 120
Cdd:cd16184 135 -LTDAFRQRDTQMTGTI 150
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 104-132 1.39e-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: 1.39e-03
                          10        20
                  ....*....|....*....|....*....
2G9B_A        104 EFMKTWRKYDTDHSGFIETEELKNFLKDL 132
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 100-173 1.81e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 37.11  E-value: 1.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2G9B_A      100 KSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDdtklaEYTDLMLKLFDSNNDGKLELTEMARLL 173
Cdd:cd16254  31 KSADDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGRDLSD-----KETKALLAAGDKDGDGKIGIDEFATLV 99
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 113-213 3.80e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 37.23  E-value: 3.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      113 DTDHSGFIETEELKNFLkdllekANKTVDDTKlAEYTDLMLKLFDSNNDGKLELTEmarllpvqenfllkFQGIKMCGKE 192
Cdd:cd16183  10 DKDRSGQISATELQQAL------SNGTWTPFN-PETVRLMIGMFDRDNSGTINFQE--------------FAALWKYITD 68

                        90       100
                ....*....|....*....|.
2G9B_A      193 FNKAFELYDQDGNGYIDENEL 213
Cdd:cd16183  69 WQNCFRSFDRDNSGNIDKNEL 89
EF-hand_6 pfam13405
EF-hand domain;
104-132 4.14e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.07  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|....*....
2G9B_A        104 EFMKTWRKYDTDHSGFIETEELKNFLKDL 132
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_PEF_CAPN12 cd16194
Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed ...
 120-213 5.48e-03

Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed calcium-activated neutral proteinase 12 (CANP 12), is a calpain large subunit mainly expressed in the cortex of the hair follicle. It may affect apoptosis regulation. CAPN12 contains a short N-terminal anchor helix, followed by 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: 320069 [Multi-domain]  Cd Length: 169  Bit Score: 36.78  E-value: 5.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G9B_A      120 IETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLpvqeNFLLKFQGIkmcgkeFNKafel 199
Cdd:cd16194  16 INASELQKILSIALERAHTSKPREFGLRTCRQLIQCFDHGQNGKLALEEFQQLW----GYLLEWQAI------FTK---- 81

                        90
                ....*....|....
2G9B_A      200 YDQDGNGYIDENEL 213
Cdd:cd16194  82 FDEDTSGTMDSYEL 95
EF-hand_7 pfam13499
EF-hand domain pair;
196-225 8.47e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.15  E-value: 8.47e-03
                          10        20        30
                  ....*....|....*....|....*....|
2G9B_A        196 AFELYDQDGNGYIDENELDALLKDLCEKNK 225
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEP 36
PTZ00183 PTZ00183
centrin; Provisional
 191-240 8.66e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 35.82  E-value: 8.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
2G9B_A       191 KEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNI 240
Cdd:PTZ00183  17 KEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDG 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 17-84 8.66e-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: 34.06  E-value: 8.66e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
2G9B_A       17 QFFEIWLHFDADGSGYLEGKELQNLIQELLqarkkaGLELSPEMKTFVDQYGQRDDGKIGIVELAHVL 84
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 187-218 9.99e-03

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 34.71  E-value: 9.99e-03
                        10        20        30
                ....*....|....*....|....*....|..
2G9B_A      187 KMCGKEFNKAFELYDQDGNGYIDENELDALLK 218
Cdd:cd16255  30 KKSADDVKKVFEIIDQDKSGFIEEEELKLFLQ 61
 
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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