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Conserved domains on  [gi|2311615164|ref|NP_963855|]
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secretagogin [Rattus norvegicus]

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 ...
17-273 3.26e-153

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: 427.59  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTLMEENVQKMKEQLMVGHDISKEGRILMKELASMFLSEDENFLL 96
Cdd:cd16178     1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 FFRLETPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178    81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 177 ILALQENFLLQFKMDASSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178   161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240
                         250
                  ....*....|....*..
gi 2311615164 257 KDGKIQKSELALCLGLK 273
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 ...
17-273 3.26e-153

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: 427.59  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTLMEENVQKMKEQLMVGHDISKEGRILMKELASMFLSEDENFLL 96
Cdd:cd16178     1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 FFRLETPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178    81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 177 ILALQENFLLQFKMDASSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178   161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240
                         250
                  ....*....|....*..
gi 2311615164 257 KDGKIQKSELALCLGLK 273
Cdd:cd16178   241 KDGKIQKSELALCLGLK 257
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
17-179 3.52e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLakfgiedtlmeenvqkmkEQLMVGHDISKEGRILMKELASMFLSEDENfll 96
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDFEALFRRLW------------------ATLFSEADTDGDGRISREEFVAGMESLFEA--- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 ffrletplDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLhhkkviSEAELEEytstMMKIFDRNKDGRLDLNDLAR 176
Cdd:COG5126    66 --------TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV------SEEEADE----LFARLDTDGDGKISFEEFVA 127

                  ...
gi 2311615164 177 ILA 179
Cdd:COG5126   128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
111-178 7.29e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 7.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2311615164 111 MQIWRKYDADSSGFISAAELSNFLRDLFLHHKkvISEAELEEytstMMKIFDRNKDGRLDLNDLARIL 178
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEE----LFKEFDLDKDGRISFEEFLELY 66
 
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 ...
17-273 3.26e-153

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: 427.59  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTLMEENVQKMKEQLMVGHDISKEGRILMKELASMFLSEDENFLL 96
Cdd:cd16178     1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 FFRLETPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178    81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 177 ILALQENFLLQFKMDASSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178   161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240
                         250
                  ....*....|....*..
gi 2311615164 257 KDGKIQKSELALCLGLK 273
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 ...
17-273 1.25e-88

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: 263.83  E-value: 1.25e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTlMEENVQKMKEQLMVGHDISKEGRILMKELASMfLSEDENFLL 96
Cdd:cd15902     1 FMEVWMHFDADGNGYIEGKELDSFLRELLKALNGKDK-TDDEVAEKKKEFMEKYDENEDGKIEIRELANI-LPTEENFLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 FFRLETPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd15902    79 LFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 177 ILALQENFLLQFKMDaSSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd15902   159 LLPVQENFLLKFQIL-GAMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENFRDAILRACDKN 237
                         250
                  ....*....|....*..
gi 2311615164 257 KDGKIQKSELALCLGLK 273
Cdd:cd15902   238 KDGKIQKTELALFLSAK 254
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
17-270 4.46e-72

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: 221.90  E-value: 4.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIED----TLMEENVQKMKEQLMVGHDISKEGRILMKELASMfLSEDE 92
Cdd:cd16179     1 FMDVWNHYDTDGNGYIEGTELDGFLREFVSSVNPEDvgpeVVSETALEELKEEFMEAYDENQDGRIDIRELAQL-LPTEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  93 NFLLFFRLETPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKK--VISEAELEEYTSTMMKIFDRNKDGRLD 170
Cdd:cd16179    80 NFLLLFRRDNPLDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLLKEAKRdnDVSEDKLIEYTDTILQLFDRNKDGKLQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 171 LNDLARILALQENFLLQ--FKmdaSSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREI 248
Cdd:cd16179   160 LSEMARLLPVKENFLCRpiFK---GAGKLTREDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEI 236
                         250       260
                  ....*....|....*....|..
gi 2311615164 249 LLRHCDVNKDGKIQKSELALCL 270
Cdd:cd16179   237 ILRGWDFNNDGKISRKELTMLL 258
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
17-270 1.82e-48

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: 161.20  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDL-LAKFGIEDTLMEENVQKMKEQLMVGHDISKEGRILMKELASMfLSEDENFL 95
Cdd:cd16177     1 FLEIWKHFDADGNGYIEGKELENFFRELeRARRGAGVDSKSANFGEKMKEFMQKYDKNADGRIEMAELAQI-LPTEENFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  96 LFFRleTPLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLA 175
Cdd:cd16177    80 LCFR--QHVGSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 176 RILALQENFLLQFKMDASSTEErkrdFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDv 255
Cdd:cd16177   158 RLLPVQENFLLKFQGMKLSSEE----FNAIFAFYDKDGSGYIDENELDALLKDLYEKNKKEMDIQQLTNYKKSIMSLSD- 232
                         250
                  ....*....|....*
gi 2311615164 256 nkDGKIQKSELALCL 270
Cdd:cd16177   233 --GGKLYRKELEMVL 245
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
17-270 1.94e-46

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: 155.77  E-value: 1.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTLMEENVQKMKEQlmvgHDISKEGRILMKELASMFLSEdENFLL 96
Cdd:cd16176     1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLELSDQMKAFVDQ----YGQSTDGKIGIVELAQILPTE-ENFLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 FFRLEtpLDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16176    76 FFRQQ--LKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 177 ILALQENFLLQFKmdasSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDvn 256
Cdd:cd16176   154 LLPVQENFLLKFQ----GVKMCGKEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMALSD-- 227
                         250
                  ....*....|....
gi 2311615164 257 kDGKIQKSELALCL 270
Cdd:cd16176   228 -GGKLYRTELALIL 240
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
110-275 6.02e-32

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: 118.22  E-value: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 110 FMQIWRKYDADSSGFISAAELSNFLRDLFLHHK-KVISEAELEEYTSTMMKIFDRNKDGRLDLNDLARILALQENFLLQF 188
Cdd:cd15902     1 FMEVWMHFDADGNGYIEGKELDSFLRELLKALNgKDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILPTEENFLLLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 189 KMDASstEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELAL 268
Cdd:cd15902    81 RREQP--LISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158

                  ....*..
gi 2311615164 269 CLGLKIN 275
Cdd:cd15902   159 LLPVQEN 165
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
110-275 2.80e-24

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: 98.02  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 110 FMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKV---ISEAELEEYTSTMMKIFDRNKDGRLDLNDLARILALQENFLL 186
Cdd:cd16177     1 FLEIWKHFDADGNGYIEGKELENFFRELERARRGAgvdSKSANFGEKMKEFMQKYDKNADGRIEMAELAQILPTEENFLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 187 QFKMDASSTEErkrdFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSEL 266
Cdd:cd16177    81 CFRQHVGSSSE----FMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEM 156

                  ....*....
gi 2311615164 267 ALCLGLKIN 275
Cdd:cd16177   157 ARLLPVQEN 165
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
110-275 2.59e-23

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: 95.29  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 110 FMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKviSEAELEEYTSTMMKIFDRNKDGRLDLNDLARILALQENFLLQFK 189
Cdd:cd16176     1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKK--AGLELSDQMKAFVDQYGQSTDGKIGIVELAQILPTEENFLLFFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 190 MDASSTEErkrdFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELALC 269
Cdd:cd16176    79 QQLKSSEE----FMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARL 154

                  ....*.
gi 2311615164 270 LGLKIN 275
Cdd:cd16176   155 LPVQEN 160
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
109-179 8.71e-10

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: 53.71  E-value: 8.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311615164 109 EFMQIWRKYDADSSGFISAAELSNFLrdlflhhkKVISEAELEEYTSTMMKIFDRNKDGRLDLNDLARILA 179
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAAL--------KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
17-179 3.52e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  17 FWQIWQRFDKDEKGYIKETELDAFFDDLLakfgiedtlmeenvqkmkEQLMVGHDISKEGRILMKELASMFLSEDENfll 96
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDFEALFRRLW------------------ATLFSEADTDGDGRISREEFVAGMESLFEA--- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  97 ffrletplDNSVEFMQIWRKYDADSSGFISAAELSNFLRDLFLhhkkviSEAELEEytstMMKIFDRNKDGRLDLNDLAR 176
Cdd:COG5126    66 --------TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV------SEEEADE----LFARLDTDGDGKISFEEFVA 127

                  ...
gi 2311615164 177 ILA 179
Cdd:COG5126   128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
111-178 7.29e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 7.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2311615164 111 MQIWRKYDADSSGFISAAELSNFLRDLFLHHKkvISEAELEEytstMMKIFDRNKDGRLDLNDLARIL 178
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEE----LFKEFDLDKDGRISFEEFLELY 66
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
111-222 3.33e-04

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: 40.28  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 111 MQIW-RKYDADSSGFISAAELSNFLrdlflhhkkviSEAELEEYTST---MMKIFDRNKDGRLDLNDLArilALQEnFLL 186
Cdd:cd16185     2 LRQWfRAVDRDRSGSIDVNELQKAL-----------AGGGLLFSLATaekLIRMFDRDGNGTIDFEEFA---ALHQ-FLS 66
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2311615164 187 QfkMDASsteerkrdfekiFAHYDVSKTGALEGPEV 222
Cdd:cd16185    67 N--MQNG------------FEQRDTSRSGRLDANEV 88
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
110-267 5.55e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 110 FMQIWRKYDADSSGFISAAELsnflrdlflhhkkvisEAELEEYTSTMMKIFDRNKDGRLDLNDLARIlalqenfllqfk 189
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDF----------------EALFRRLWATLFSEADTDGDGRISREEFVAG------------ 58
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2311615164 190 MDASSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMmelvqpsisGVDLDKFREIlLRHCDVNKDGKIQKSELA 267
Cdd:COG5126    59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL---------GVSEEEADEL-FARLDTDGDGKISFEEFV 126
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
174-272 6.43e-04

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 38.51  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 174 LARILALQENFLLQFKMDASSTEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELvQPSISGvdldkfreiLLRHC 253
Cdd:cd00252    19 LLKEQDENRSYDNNKRGHDLSGTMRKEIAQWEFDNLDNNKDGKLDKRELAPFRAPLMPL-EHCARG---------FFESC 88
                          90
                  ....*....|....*....
gi 2311615164 254 DVNKDGKIQKSELALCLGL 272
Cdd:cd00252    89 DLNKDKKISLQEWLGCFGV 107
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
249-272 1.32e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.


Pssm-ID: 320013  Cd Length: 104  Bit Score: 37.26  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|....
gi 2311615164 249 LLRHCDVNKDGKIQKSELALCLGL 272
Cdd:cd16234    81 FPKYCDVNKDKKISLTEWLNCLGV 104
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
109-221 2.65e-03

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: 37.51  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 109 EFMQIWRKYDADSSGFISAAELSNFLRDLFLHHKKViseaeleEYTSTMMKIFDRNKDGRLDLNDLARILalqeNFLLQF 188
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSI-------ETVRLMINMFDRDRSGTINFDEFVGLW----KYIQDW 69
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2311615164 189 KmdassteerkrdfeKIFAHYDVSKTGALEGPE 221
Cdd:cd16180    70 R--------------RLFRRFDRDRSGSIDFNE 88
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
110-235 2.99e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 110 FMQIWR----KYDADSSGFISAAELSNFLRDLFlhhkkvisEAELEEYTSTMMKIFDRNKDGRLDLNDLARilalqenFL 185
Cdd:COG5126    31 FRRLWAtlfsEADTDGDGRISREEFVAGMESLF--------EATVEPFARAAFDLLDTDGDGKISADEFRR-------LL 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2311615164 186 LQFKMDASSTEErkrdfekIFAHYDVSKTGALegpEVDGFVKDMMELVQP 235
Cdd:COG5126    96 TALGVSEEEADE-------LFARLDTDGDGKI---SFEEFVAAVRDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
157-271 3.08e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164 157 MMKIFDRNKDGRLDLNDLARILAlqenfllqfkmdassteerkRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVQps 236
Cdd:COG5126    10 RFDLLDADGDGVLERDDFEALFR--------------------RLWATLFSEADTDGDGRISREEFVAGMESLFEATV-- 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2311615164 237 isgvdlDKFREILLRHCDVNKDGKIQKSELALCLG 271
Cdd:COG5126    68 ------EPFARAAFDLLDTDGDGKISADEFRRLLT 96
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
41-170 4.53e-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: 37.68  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164  41 FDDLLAK-FGIEDTLMEENVQkmkeqlmvghDISKEGRILMKELASMFLSEDEN---------FLLFFRLE-TPLDNSVE 109
Cdd:cd16227    91 WEEYLADsFGYDDEDNEEMIK----------DSTEDDLKLLEDDKEMFEAADLNkdgkldkteFSAFQHPEeYPHMHPVL 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311615164 110 FMQIWRKYDADSSGFISAAElsnFLRDLFLHHKKVISEAELEEYTstmmKIFDRNKDGRLD 170
Cdd:cd16227   161 IEQTLRDKDKDNDGFISFQE---FLGDRAGHEDKEWLLVEKDRFD----EDYDKDGDGKLD 214
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
3-89 5.44e-03

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: 37.39  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311615164   3 NAHRQTQAHLDaacfwQIWQRFDKDEKGYIKETELDAFFDDLLAKFGIEDTlmEENVQKMKEQLMVGHDISKEGRILMKE 82
Cdd:cd16179   181 GAGKLTREDID-----RVFALYDRDNNGTIENEELTGFLKDLLELVQEDYD--EQDLEEFKEIILRGWDFNNDGKISRKE 253

                  ....*..
gi 2311615164  83 LASMFLS 89
Cdd:cd16179   254 LTMLLLQ 260
 
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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