NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15055537|ref|NP_008929|]
View 

secretagogin [Homo sapiens]

Protein Classification

EFh_HEF_SCGN domain-containing protein( domain architecture ID 11610854)

EFh_HEF_SCGN domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.91e-164

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: 455.71  E-value: 2.91e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLL 96
Cdd:cd16178   1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 LFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178  81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 177 ILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178 161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                       250
                ....*....|....*..
gi 15055537 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 2.91e-164

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: 455.71  E-value: 2.91e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLL 96
Cdd:cd16178   1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 LFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178  81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 177 ILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178 161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                       250
                ....*....|....*..
gi 15055537 257 KDGKIQKSELALCLGLK 273
Cdd:cd16178 241 KDGKIQKSELALCLGLK 257
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
17-179 7.65e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.26  E-value: 7.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLmklgtddtvmkanlhkvkQQFMTTQDASKDGRIRMKELAGMFLSEDENfll 96
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLW------------------ATLFSEADTDGDGRISREEFVAGMESLFEA--- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 lfrrenplDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHhkkaiseaklEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:COG5126  66 --------TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVS----------EEEADELFARLDTDGDGKISFEEFVA 127


                ...
gi 15055537 177 ILA 179
Cdd:COG5126 128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
111-178 5.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 5.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15055537   111 MQIWRKYDADSSGFISAAELRNFLRDLFLHHKkaISEAKLEEytgtMMKIFDRNKDGRLDLNDLARIL 178
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP--LSDEEVEE----LFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 15-178 1.42e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537   15 AGFWQVWQRFDADEKGYIEEKELDafflhMLMK-LGTDDTvmKANLHKVKQQFmttqDASKDGRIRMKElagmFLSeden 93
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELG-----TVMRsLGQNPT--EAELQDMINEV----DADGNGTIDFPE----FLT---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537   94 flLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLflhhkkaiSEAKLEEYTGTMMKIFDRNKDGRLDLND 173
Cdd:PTZ00184  72 --LMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNL--------GEKLTDEEVDEMIREADVDGDGQINYEE 141


                 ....*
gi 15055537  174 LARIL 178
Cdd:PTZ00184 142 FVKMM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 109-137 9.75e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.12  E-value: 9.75e-03
                           10        20
                   ....*....|....*....|....*....
gi 15055537    109 EFMQIWRKYDADSSGFISAAELRNFLRDL 137
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
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 2.91e-164

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: 455.71  E-value: 2.91e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLL 96
Cdd:cd16178   1 FAEIWQHFDADESGYIEGKELDNFFKDLLKKLGTKDTISADEVQDVKECFMSAYDVTGDGRIQIQELANIILPDDENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 LFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd16178  81 FFRREEPLDSSVEFMRIWRKYDADSSGYISAAELKNFLRDLFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 177 ILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd16178 161 ILALQENFLLQFKMDAMSEEERKRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVQLDKFKEIILNHCDVN 240

                       250
                ....*....|....*..
gi 15055537 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 1.41e-94

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: 278.85  E-value: 1.41e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVmKANLHKVKQQFMTTQDASKDGRIRMKELAGMfLSEDENFLL 96
Cdd:cd15902   1 FMEVWMHFDADGNGYIEGKELDSFLRELLKALNGKDKT-DDEVAEKKKEFMEKYDENEDGKIEIRELANI-LPTEENFLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 LFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:cd15902  79 LFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 177 ILALQENFLLQFKMDAcSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVN 256
Cdd:cd15902 159 LLPVQENFLLKFQILG-AMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENFRDAILRACDKN 237

                       250
                ....*....|....*..
gi 15055537 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 3.64e-79

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: 240.00  E-value: 3.64e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDD----TVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMfLSEDE 92
Cdd:cd16179   1 FMDVWNHYDTDGNGYIEGTELDGFLREFVSSVNPEDvgpeVVSETALEELKEEFMEAYDENQDGRIDIRELAQL-LPTEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  93 NFLLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKK--AISEAKLEEYTGTMMKIFDRNKDGRLD 170
Cdd:cd16179  80 NFLLLFRRDNPLDSSVEFMKVWREYDKDNSGYIEADELKNFLKHLLKEAKRdnDVSEDKLIEYTDTILQLFDRNKDGKLQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 171 LNDLARILALQENFLLQ--FKMDACSTeerKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREI 248
Cdd:cd16179 160 LSEMARLLPVKENFLCRpiFKGAGKLT---REDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEI 236

                       250       260
                ....*....|....*....|..
gi 15055537 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 8.59e-56

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: 180.07  E-value: 8.59e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHM-LMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAgMFLSEDENFL 95
Cdd:cd16177   1 FLEIWKHFDADGNGYIEGKELENFFRELeRARRGAGVDSKSANFGEKMKEFMQKYDKNADGRIEMAELA-QILPTEENFL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  96 LLFRREnpLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLA 175
Cdd:cd16177  80 LCFRQH--VGSSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEMA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 176 RILALQENFLLQFKMDACSTEErkrdFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDv 255
Cdd:cd16177 158 RLLPVQENFLLKFQGMKLSSEE----FNAIFAFYDKDGSGYIDENELDALLKDLYEKNKKEMDIQQLTNYKKSIMSLSD- 232

                       250
                ....*....|....*
gi 15055537 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 4.21e-52

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: 170.40  E-value: 4.21e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLM---KLGTDDT-VMKAnlhkvkqqFMTTQDASKDGRIRMKELAGMFLSEdE 92
Cdd:cd16176   1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQarkKAGLELSdQMKA--------FVDQYGQSTDGKIGIVELAQILPTE-E 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  93 NFLLLFRREnpLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLN 172
Cdd:cd16176  72 NFLLFFRQQ--LKSSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLT 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 173 DLARILALQENFLLQFK-MDACSteerkRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLR 251
Cdd:cd16176 150 EMARLLPVQENFLLKFQgVKMCG-----KEFNKIFELYDQDGNGYIDENELDALLKDLCEKNKKDLDINNISTYKKSIMA 224

                       250
                ....*....|....*....
gi 15055537 252 HCDvnkDGKIQKSELALCL 270
Cdd:cd16176 225 LSD---GGKLYRTELALIL 240
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 110-275 1.09e-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: 99.18  E-value: 1.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 110 FMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTM---MKIFDRNKDGRLDLNDLARILALQENFLL 186
Cdd:cd16177   1 FLEIWKHFDADGNGYIEGKELENFFRELERARRGAGVDSKSANFGEKMkefMQKYDKNADGRIEMAELAQILPTEENFLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 187 QFKMDACSTEErkrdFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSEL 266
Cdd:cd16177  81 CFRQHVGSSSE----FMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEKKLQEYTQTILRMFDLNGDGKLGLSEM 156


                ....*....
gi 15055537 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 6.40e-24

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: 96.83  E-value: 6.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 110 FMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEakLEEYTGTMMKIFDRNKDGRLDLNDLARILALQENFLLQFK 189
Cdd:cd16176   1 FLEIWHHYDNDGNGYIEGKELQSFIQELQQARKKAGLE--LSDQMKAFVDQYGQSTDGKIGIVELAQILPTEENFLLFFR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 190 MDACSTEErkrdFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELALC 269
Cdd:cd16176  79 QQLKSSEE----FMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFDESKLEEYTHTMLKMFDSNNDGKLGLTEMARL 154


                ....*.
gi 15055537 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 2.14e-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: 55.25  E-value: 2.14e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15055537 109 EFMQIWRKYDADSSGFISAAELRNFLrdlflhhkKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLARILA 179
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAAL--------KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
17-179 7.65e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.26  E-value: 7.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  17 FWQVWQRFDADEKGYIEEKELDAFFLHMLmklgtddtvmkanlhkvkQQFMTTQDASKDGRIRMKELAGMFLSEDENfll 96
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLW------------------ATLFSEADTDGDGRISREEFVAGMESLFEA--- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  97 lfrrenplDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHhkkaiseaklEEYTGTMMKIFDRNKDGRLDLNDLAR 176
Cdd:COG5126  66 --------TVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVS----------EEEADELFARLDTDGDGKISFEEFVA 127


                ...
gi 15055537 177 ILA 179
Cdd:COG5126 128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
111-178 5.59e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 5.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15055537   111 MQIWRKYDADSSGFISAAELRNFLRDLFLHHKkaISEAKLEEytgtMMKIFDRNKDGRLDLNDLARIL 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 9.24e-05

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: 41.82  E-value: 9.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 111 MQIW-RKYDADSSGFISAAELRNflrdlflhhkkAISEAKLE---EYTGTMMKIFDRNKDGRLDLNDLArilALQEnFLL 186
Cdd:cd16185   2 LRQWfRAVDRDRSGSIDVNELQK-----------ALAGGGLLfslATAEKLIRMFDRDGNGTIDFEEFA---ALHQ-FLS 66

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15055537 187 QfkMDACsteerkrdfekiFAYYDVSKTGALEGPEV 222
Cdd:cd16185  67 N--MQNG------------FEQRDTSRSGRLDANEV 88
PTZ00184 PTZ00184
calmodulin; Provisional
 15-178 1.42e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537   15 AGFWQVWQRFDADEKGYIEEKELDafflhMLMK-LGTDDTvmKANLHKVKQQFmttqDASKDGRIRMKElagmFLSeden 93
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTITTKELG-----TVMRsLGQNPT--EAELQDMINEV----DADGNGTIDFPE----FLT---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537   94 flLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLflhhkkaiSEAKLEEYTGTMMKIFDRNKDGRLDLND 173
Cdd:PTZ00184  72 --LMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNL--------GEKLTDEEVDEMIREADVDGDGQINYEE 141


                 ....*
gi 15055537  174 LARIL 178
Cdd:PTZ00184 142 FVKMM 146
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 23-266 2.49e-04

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 41.66  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  23 RFDADEKGYIEEKELDAFFLHMLMKLGTDDtvmkanlhkVKQQFmTTQDASKDGRIRMKELAGMFL-----SEDENFLLL 97
Cdd:cd15899  43 KMDVDKDGFISAKELHSWILESFKRHAMEE---------SKEQF-RAVDPDEDGHVSWDEYKNDTYgsvgdDEENVADNI 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537  98 FRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLR-DLFLHHKKAISEAKLEEytgtmmkiFDRNKDGRLDLndlar 176
Cdd:cd15899 113 KEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHpEESPYMLDFVIKETLED--------LDKNGDGFISL----- 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 177 ilalqENFLLQFKMDACSTEE------RKRDFEKifaYYDVSKTGALEGPEVdgfvkdmMELVQPSISGVDLDKFREiLL 250
Cdd:cd15899 180 -----EEFISDPYSADENEEEpewvkvEKERFVE---LRDKDKDGKLDGEEL-------LSWVDPSNQEIALEEAKH-LI 243

                       250
                ....*....|....*.
gi 15055537 251 RHCDVNKDGKIQKSEL 266
Cdd:cd15899 244 AESDENKDGKLSPEEI 259
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 109-221 5.47e-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: 39.82  E-value: 5.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 109 EFMQIWRKYDADSSGFISAAELRNFLRdLFLHHKKAISEAKLeeytgtMMKIFDRNKDGRLDLNDLARILalqeNFLLQF 188
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALS-NGDWTPFSIETVRL------MINMFDRDRSGTINFDEFVGLW----KYIQDW 69

                        90       100       110
                ....*....|....*....|....*....|...
gi 15055537 189 KmdacsteerkrdfeKIFAYYDVSKTGALEGPE 221
Cdd:cd16180  70 R--------------RLFRRFDRDRSGSIDFNE 88
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
110-267 7.98e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 7.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 110 FMQIWRKYDADSSGFISAAELrnflrdlflhhkkaisEAKLEEYTGTMMKIFDRNKDGRLDLNDLARIlalqenfllqfk 189
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDF----------------EALFRRLWATLFSEADTDGDGRISREEFVAG------------ 58

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15055537 190 MDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMmelvqpsisGVDLDKFREILlRHCDVNKDGKIQKSELA 267
Cdd:COG5126  59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL---------GVSEEEADELF-ARLDTDGDGKISFEEFV 126
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
 249-272 1.36e-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: 1.36e-03
                        10        20
                ....*....|....*....|....
gi 15055537 249 LLRHCDVNKDGKIQKSELALCLGL 272
Cdd:cd16234  81 FPKYCDVNKDKKISLTEWLNCLGV 104
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 237-272 5.10e-03

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: 35.81  E-value: 5.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15055537 237 ISGVDLDKFREILLRH----------CDVNKDGKIQKSELALCLGL 272
Cdd:cd00252  62 LDKRELAPFRAPLMPLehcargffesCDLNKDKKISLQEWLGCFGV 107
EF-hand_6 pfam13405
EF-hand domain;
109-137 7.23e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.30  E-value: 7.23e-03
                          10        20
                  ....*....|....*....|....*....
gi 15055537   109 EFMQIWRKYDADSSGFISAAELRNFLRDL 137
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
157-271 8.65e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 35.92  E-value: 8.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15055537 157 MMKIFDRNKDGRLDLNDLARILAlqenfllqfkmdacsteerkRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQps 236
Cdd:COG5126  10 RFDLLDADGDGVLERDDFEALFR--------------------RLWATLFSEADTDGDGRISREEFVAGMESLFEATV-- 67

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15055537 237 isgvdlDKFREILLRHCDVNKDGKIQKSELALCLG 271
Cdd:COG5126  68 ------EPFARAAFDLLDTDGDGKISADEFRRLLT 96
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 109-137 9.75e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.12  E-value: 9.75e-03
                           10        20
                   ....*....|....*....|....*....
gi 15055537    109 EFMQIWRKYDADSSGFISAAELRNFLRDL 137
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH