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Conserved domains on  [gi|150261525]
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Chain A, Protein Zgc:100843

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11610854)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to Tetrahymena thermophila 23 kDa calcium-binding protein that may play a crucial role in calcium-dependent regulation of ciliary movement

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 13-269 4.14e-157

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: 437.22  E-value: 4.14e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKDKITDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENFLL 92
Cdd:cd16178    1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREAPLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:cd16178   81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 173 ILALQENFLLQFK*DASSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD*N 252
Cdd:cd16178  161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                        250
                 ....*....|....*..
gi 150261525 253 KDGKIQKSELALCLGLK 269
Cdd:cd16178  241 KDGKIQKSELALCLGLK 257
 
Name Accession Description Interval E-value
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 13-269 4.14e-157

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: 437.22  E-value: 4.14e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKDKITDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENFLL 92
Cdd:cd16178    1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREAPLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:cd16178   81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 173 ILALQENFLLQFK*DASSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD*N 252
Cdd:cd16178  161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                        250
                 ....*....|....*..
gi 150261525 253 KDGKIQKSELALCLGLK 269
Cdd:cd16178  241 KDGKIQKSELALCLGLK 257
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-175 6.51e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQpkdkitdervqqikksf*SAYDATFDGRLQIEELAN*ILPQeenFLL 92
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLF------------------SEADTDGDGRISREEFVAGMESL---FEA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREApldnsvef*KIWRKYDADSSGYISAAELKNFLKDLFLQhkkkippnklDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:COG5126   66 TVEPFA--------RAAFDLLDTDGDGKISADEFRRLLTALGVS----------EEEADELFARLDTDGDGKISFEEFVA 127


                 ...
gi 150261525 173 ILA 175
Cdd:COG5126  128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
109-174 1.00e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 1.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150261525  109 IWRKYDADSSGYISAAELKNFLKDLFLQHKKKippnklDEYTDA**KIFDKNKDGRLDLNDLARIL 174
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 105-133 1.72e-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: 35.05  E-value: 1.72e-03
                           10        20
                   ....*....|....*....|....*....
gi 150261525   105 EF*KIWRKYDADSSGYISAAELKNFLKDL 133
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00184 PTZ00184
calmodulin; Provisional
 48-174 8.53e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 35.89  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  48 DKITDERVQQIKKSF*SAYDATFDGRLQIEELA--------------------------N*ILPQEENFLLIFRREAPLD 101
Cdd:PTZ00184   3 DQLTEEQIAEFKEAF-SLFDKDGDGTITTKELGtvmrslgqnpteaelqdminevdadgNGTIDFPEFLTLMARKMKDTD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150261525 102 NSVEF*KIWRKYDADSSGYISAAELKNFLKDLflqhkkkipPNKL-DEYTDA**KIFDKNKDGRLDLNDLARIL 174
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNL---------GEKLtDEEVDEMIREADVDGDGQINYEEFVKMM 146
 
Name Accession Description Interval E-value
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 13-269 4.14e-157

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: 437.22  E-value: 4.14e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKDKITDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENFLL 92
Cdd:cd16178    1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREAPLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:cd16178   81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 173 ILALQENFLLQFK*DASSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD*N 252
Cdd:cd16178  161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                        250
                 ....*....|....*..
gi 150261525 253 KDGKIQKSELALCLGLK 269
Cdd:cd16178  241 KDGKIQKSELALCLGLK 257
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 13-269 2.43e-109

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: 316.22  E-value: 2.43e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKDKiTDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENFLL 92
Cdd:cd15902    1 FMEVWMHFDADGNGYIEGKELDSFLRELLKALNGKDK-TDDEVAEKKKEFMEKYDENEDGKIEIRELAN-ILPTEENFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREAPLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:cd15902   79 LFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 173 ILALQENFLLQFK*DaSSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD*N 252
Cdd:cd15902  159 LLPVQENFLLKFQIL-GAMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENFRDAILRACDKN 237

                        250
                 ....*....|....*..
gi 150261525 253 KDGKIQKSELALCLGLK 269
Cdd:cd15902  238 KDGKIQKTELALFLSAK 254
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 13-266 4.96e-78

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: 236.92  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKD----KITDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEE 88
Cdd:cd16179    1 FMDVWNHYDTDGNGYIEGTELDGFLREFVSSVNPEDvgpeVVSETALEELKEEFMEAYDENQDGRIDIRELAQ-LLPTEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  89 NFLLIFRREAPLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPP--NKLDEYTDA**KIFDKNKDGRLD 166
Cdd:cd16179   80 NFLLLFRRDNPLDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLLKEAKRDNDVseDKLIEYTDTILQLFDRNKDGKLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 167 LNDLARILALQENFLLQFK*DASSQVERkRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLL 246
Cdd:cd16179  160 LSEMARLLPVKENFLCRPIFKGAGKLTR-EDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEIIL 238

                        250       260
                 ....*....|....*....|
gi 150261525 247 THCD*NKDGKIQKSELALCL 266
Cdd:cd16179  239 RGWDFNNDGKISRKELTMLL 258
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 13-266 6.60e-57

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: 182.35  E-value: 6.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFfrh*LKKLQPKDKITDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENFLL 92
Cdd:cd16176    1 FLEIWHHYDNDGNGYIEGKELQSF----IQELQQARKKAGLELSDQMKAFVDQYGQSTDGKIGIVELAQ-ILPTEENFLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREapLDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:cd16176   76 FFRQQ--LKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 173 ILALQENFLLQFK*DASSqverKRDFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD*n 252
Cdd:cd16176  154 LLPVQENFLLKFQGVKMC----GKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSD-- 227

                        250
                 ....*....|....
gi 150261525 253 kDGKIQKSELALCL 266
Cdd:cd16176  228 -GGKLYRTELALIL 240
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 13-266 1.28e-55

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: 179.30  E-value: 1.28e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQPKDKI--TDERVQQIKKSF*SAYDATFDGRLQIEELAN*ILPQEENF 90
Cdd:cd16177    1 FLEIWKHFDADGNGYIEGKELENFFRE-LERARRGAGVdsKSANFGEKMKEFMQKYDKNADGRIEMAELAQ-ILPTEENF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  91 LLIFRREAplDNSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDKNKDGRLDLNDL 170
Cdd:cd16177   79 LLCFRQHV--GSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525 171 ARILALQENFLLQFK*DASSQVErkrdFEKIFAHYDVSRTGALEGPEVDGFVKD**ELVRPSISGGDLDKFRECLLTHCD 250
Cdd:cd16177  157 ARLLPVQENFLLKFQGMKLSSEE----FNAIFAFYDKDGSGYIDENELDALLKDLYEKNKKEMDIQQLTNYKKSIMSLSD 232

                        250
                 ....*....|....*.
gi 150261525 251 *nkdGKIQKSELALCL 266
Cdd:cd16177  233 G---GKLYRKELEMVL 245
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 10-174 2.30e-19

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: 84.50  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  10 AAGFLQIWQHFDADDNGYIEGKELDDFFRH*LKKlqPKDKITDERVQQIKKSF*SAYDATFDGRLQIEELAn*ILPQEEN 89
Cdd:cd16176   84 SEEFMQTWRKYDADHSGFIEADELKSFLKDLLKK--ANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMA-RLLPVQEN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  90 FLLIFRREAPLdnSVEF*KIWRKYDADSSGYISAAELKNFLKDLFLQHKKKIPPNKLDEYTDA**KIFDknkDGRLDLND 169
Cdd:cd16176  161 FLLKFQGVKMC--GKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSD---GGKLYRTE 235


                 ....*
gi 150261525 170 LARIL 174
Cdd:cd16176  236 LALIL 240
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 105-175 2.06e-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: 52.55  E-value: 2.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150261525 105 EF*KIWRKYDADSSGYISAAELKNFLKDLFlqhkkkipPNKLDEYTDA**KIFDKNKDGRLDLNDLARILA 175
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG--------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-175 6.51e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLQpkdkitdervqqikksf*SAYDATFDGRLQIEELAN*ILPQeenFLL 92
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLF------------------SEADTDGDGRISREEFVAGMESL---FEA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  93 IFRREApldnsvef*KIWRKYDADSSGYISAAELKNFLKDLFLQhkkkippnklDEYTDA**KIFDKNKDGRLDLNDLAR 172
Cdd:COG5126   66 TVEPFA--------RAAFDLLDTDGDGKISADEFRRLLTALGVS----------EEEADELFARLDTDGDGKISFEEFVA 127


                 ...
gi 150261525 173 ILA 175
Cdd:COG5126  128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
109-174 1.00e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 1.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150261525  109 IWRKYDADSSGYISAAELKNFLKDLFLQHKKKippnklDEYTDA**KIFDKNKDGRLDLNDLARIL 174
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 105-133 1.72e-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: 35.05  E-value: 1.72e-03
                           10        20
                   ....*....|....*....|....*....
gi 150261525   105 EF*KIWRKYDADSSGYISAAELKNFLKDL 133
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 105-133 2.00e-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: 35.07  E-value: 2.00e-03
                          10        20
                  ....*....|....*....|....*....
gi 150261525  105 EF*KIWRKYDADSSGYISAAELKNFLKDL 133
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 5-166 2.38e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 38.45  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525   5 FANLDAAGFLQIWQHFDADDNGYIEGKE-LDDFFRH*LKKLQP--KDKITDER--VQQIKKSF*SAyDATFDGRLQIEEL 79
Cdd:cd16227   66 FKMLDEEEANERFEEADEDGDGKVTWEEyLADSFGYDDEDNEEmiKDSTEDDLklLEDDKEMFEAA-DLNKDGKLDKTEF 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  80 AN*ILPQEenflliFRREAPldnsVEF*KIWRKYDADSSGYISAAElknFLKDLFLQHKKKIPPNKLDEYTda**KIFDK 159
Cdd:cd16227  145 SAFQHPEE------YPHMHP----VLIEQTLRDKDKDNDGFISFQE---FLGDRAGHEDKEWLLVEKDRFD----EDYDK 207


                 ....*..
gi 150261525 160 NKDGRLD 166
Cdd:cd16227  208 DGDGKLD 214
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 13-80 3.10e-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: 35.22  E-value: 3.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150261525  13 FLQIWQHFDADDNGYIEGKELDDFFRH*LKKLqpkdkiTDERVQQIkksf*SAYDATFDGRLQIEELA 80
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGL------SEEEIDEM----IREVDKDGDGKIDFEEFL 59
PTZ00184 PTZ00184
calmodulin; Provisional
 48-174 8.53e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 35.89  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150261525  48 DKITDERVQQIKKSF*SAYDATFDGRLQIEELA--------------------------N*ILPQEENFLLIFRREAPLD 101
Cdd:PTZ00184   3 DQLTEEQIAEFKEAF-SLFDKDGDGTITTKELGtvmrslgqnpteaelqdminevdadgNGTIDFPEFLTLMARKMKDTD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150261525 102 NSVEF*KIWRKYDADSSGYISAAELKNFLKDLflqhkkkipPNKL-DEYTDA**KIFDKNKDGRLDLNDLARIL 174
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNL---------GEKLtDEEVDEMIREADVDGDGQINYEEFVKMM 146
 
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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