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Conserved domains on  [gi|50344972|ref|NP_001002158|]
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reticulocalbin-3 precursor [Danio rerio]

Protein Classification

EFh_CREC_Calumenin_like domain-containing protein( domain architecture ID 11610932)

EFh_CREC_Calumenin_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 35-299 4.85e-137

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


:

Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 388.48  E-value: 4.85e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEY 114
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 115 DQNKDGKIGWIEYKNTTYGYYIDTEfDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIVIQ 194
Cdd:cd16226  81 DPNKDGKLSWEEYKKATYGFLDDEE-EDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 195 ETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEARHLI 274
Cdd:cd16226 160 ETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLI 239

                       250       260
                ....*....|....*....|....*
gi 50344972 275 HETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16226 240 YEADDDKDGKLTKEEILDKYDLFVG 264
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 35-299 4.85e-137

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 388.48  E-value: 4.85e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEY 114
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 115 DQNKDGKIGWIEYKNTTYGYYIDTEfDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIVIQ 194
Cdd:cd16226  81 DPNKDGKLSWEEYKKATYGFLDDEE-EDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 195 ETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEARHLI 274
Cdd:cd16226 160 ETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLI 239

                       250       260
                ....*....|....*....|....*
gi 50344972 275 HETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16226 240 YEADDDKDGKLTKEEILDKYDLFVG 264
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
65-212 5.58e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 5.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  65 EESKDRLGKIVDKIDTDKDGFVSHAELhhwikhrqRRYIEENVDKHWNEYDQNKDGKIGWIEYKNttygyYIDTEFDDVD 144
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDF--------EALFRRLWATLFSEADTDGDGRISREEFVA-----GMESLFEATV 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50344972 145 DKATyksmlnrdERRFKSADRDGDGVATREEFTAFLHPEEFDfmrDIVIQETIEDIDKNGDGKIDLQE 212
Cdd:COG5126  68 EPFA--------RAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEE 124
EF-hand_7 pfam13499
EF-hand domain pair;
158-218 6.97e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 6.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50344972   158 RRFKSADRDGDGVATREEFTAFLHPEEFDF-MRDIVIQETIEDIDKNGDGKIDLQEYIGDMY 218
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 160-289 1.09e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  160 FKSA----DRDGDGVATREEFTAFL-----HPEEFDfmrdivIQETIEDIDKNGDGKIDLQEYIGDMYNP-EDGETEPDW 229
Cdd:PTZ00184  13 FKEAfslfDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMARKmKDTDSEEEI 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  230 VTTekkqFSEFrDMNKDGFLDATEVSHWILPTEVDHADNEARHLIHETDKDNDDKITKKE 289
Cdd:PTZ00184  87 KEA----FKVF-DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 35-299 4.85e-137

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 388.48  E-value: 4.85e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEY 114
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 115 DQNKDGKIGWIEYKNTTYGYYIDTEfDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIVIQ 194
Cdd:cd16226  81 DPNKDGKLSWEEYKKATYGFLDDEE-EDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 195 ETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEARHLI 274
Cdd:cd16226 160 ETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLI 239

                       250       260
                ....*....|....*....|....*
gi 50344972 275 HETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16226 240 YEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 35-299 1.43e-128

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 367.28  E-value: 1.43e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEY 114
Cdd:cd16229   1 QLHEDNQSFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 115 DQNKDGKIGWIEYKNTTYGYYIDT--EFDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIV 192
Cdd:cd16229  81 DLNKDNKISWEEYKQATYGYYLGNpeEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 193 IQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEARH 272
Cdd:cd16229 161 VLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARH 240

                       250       260
                ....*....|....*....|....*..
gi 50344972 273 LIHETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16229 241 LVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 36-299 1.02e-118

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 342.34  E-value: 1.02e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  36 AHDDAH-GFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDT--DKDGFVSHAELHHWIKHRQRRYIEENVDKHWN 112
Cdd:cd16230   1 PHDDAHgNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 113 EYDQNKDGKIGWIEYKNTTYGYYIDT-EFDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDI 191
Cdd:cd16230  81 TYDTDRDGRVGWEELRNATYGHYEPGeEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 192 VIQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEAR 271
Cdd:cd16230 161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240

                       250       260
                ....*....|....*....|....*...
gi 50344972 272 HLIHETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16230 241 HLLHESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-299 4.24e-114

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 330.37  E-value: 4.24e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  37 HDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEYDQ 116
Cdd:cd16228   3 HDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 117 NKDGKIGWIEYKNTTYGYYIDTEfdDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIVIQET 196
Cdd:cd16228  83 NEDGLVSWEEYKNATYGYILDDP--DPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 197 IEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEARHLIHE 276
Cdd:cd16228 161 MEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYE 240

                       250       260
                ....*....|....*....|...
gi 50344972 277 TDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16228 241 SDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 35-298 3.51e-106

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: 310.53  E-value: 3.51e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEY 114
Cdd:cd15899   1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 115 DQNKDGKIGWIEYKNTTYGYYIDTE---FDDVDDKATYKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDI 191
Cdd:cd15899  81 DPDEDGHVSWDEYKNDTYGSVGDDEenvADNIKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 192 VIQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEAR 271
Cdd:cd15899 161 VIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEAK 240

                       250       260
                ....*....|....*....|....*..
gi 50344972 272 HLIHETDKDNDDKITKKEILENWNMFV 298
Cdd:cd15899 241 HLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 35-299 1.04e-68

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: 214.87  E-value: 1.04e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLG-KEESKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNE 113
Cdd:cd16227   1 HAKDGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 114 YDQNKDGKIGWIEYKNTTYGYyIDTEFDDVDDKAT--YKSMLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDI 191
Cdd:cd16227  81 ADEDGDGKVTWEEYLADSFGY-DDEDNEEMIKDSTedDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 192 VIQETIEDIDKNGDGKIDLQEYIGDMYnpedGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEAR 271
Cdd:cd16227 160 LIEQTLRDKDKDNDGFISFQEFLGDRA----GHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVD 235

                       250       260
                ....*....|....*....|....*...
gi 50344972 272 HLIHETDKDNDDKITKKEILENWNMFVG 299
Cdd:cd16227 236 HLFASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 35-297 8.48e-65

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 204.97  E-value: 8.48e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  35 HAHDDAHGFQFDHEAFLGKEESK-TFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNE 113
Cdd:cd16224   1 HYPNGEHNAEYDKEAFLGGEEDAdEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 114 YDQNKDGKIGWIEYKNTTYGYYIDTEFDDVDDKATYKSMLN---RDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRD 190
Cdd:cd16224  81 YDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEEESFRQlhlKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 191 IVIQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHADNEA 270
Cdd:cd16224 161 FVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEA 240

                       250       260
                ....*....|....*....|....*..
gi 50344972 271 RHLIHETDKDNDDKITKKEILENWNMF 297
Cdd:cd16224 241 LHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 45-297 6.82e-41

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 143.59  E-value: 6.82e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  45 FDHEAFLGKEeSKTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVD---KHWNEYDQNKDGK 121
Cdd:cd16225  11 FHKEVFLGNE-KEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEeneQIFKAVDTDKDGN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 122 IGWIEYK-----------NTTYGYYIDTEFDDVDDKATYKsmLNRDERRFKSADRDGDGVATREEFTAFLHPEEFDFMRD 190
Cdd:cd16225  90 VSWEEYRvhfllskgyseEEAEEKIKNNEELKLDEDDKEV--LDRYKDRWSQADEPEDGLLDVEEFLSFRHPEHSRGMLK 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 191 IVIQETIEDIDKNGDGKIDLQEYIG---DMYNPEDGETEPDWVTTEKKQFSEFRDMNKDGFLDATEVSHWILPTEVDHAD 267
Cdd:cd16225 168 NMVKEILHDLDQDGDEKLTLDEFVSlppGTVEEQQAEDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPRNERHAL 247

                       250       260       270
                ....*....|....*....|....*....|
gi 50344972 268 NEARHLIHETDKDNDDKITKKEILENWNMF 297
Cdd:cd16225 248 NEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
65-212 5.58e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 5.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  65 EESKDRLGKIVDKIDTDKDGFVSHAELhhwikhrqRRYIEENVDKHWNEYDQNKDGKIGWIEYKNttygyYIDTEFDDVD 144
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDF--------EALFRRLWATLFSEADTDGDGRISREEFVA-----GMESLFEATV 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50344972 145 DKATyksmlnrdERRFKSADRDGDGVATREEFTAFLHPEEFDfmrDIVIQETIEDIDKNGDGKIDLQE 212
Cdd:COG5126  68 EPFA--------RAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEE 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
155-297 1.28e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 155 RDERRFKSADRDGDGVATREEFTAflhpeefdfMRDIVIQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDwvtteK 234
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-----A 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50344972 235 KQFSEFRDMNKDGFLDATEVSHWILPTEVDHAdnEARHLIHETDKDNDDKITKKEILENWNMF 297
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 157-214 2.18e-07

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 47.16  E-value: 2.18e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50344972 157 ERRFKSADRDGDGVATREEFTAFLHPEEFDFMRDIvIQETIEDIDKNGDGKIDLQEYI 214
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEE-IDEMIREVDKDGDGKIDFEEFL 59
EF-hand_7 pfam13499
EF-hand domain pair;
158-218 6.97e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 6.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50344972   158 RRFKSADRDGDGVATREEFTAFLHPEEFDF-MRDIVIQETIEDIDKNGDGKIDLQEYIGDMY 218
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 160-289 1.09e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  160 FKSA----DRDGDGVATREEFTAFL-----HPEEFDfmrdivIQETIEDIDKNGDGKIDLQEYIGDMYNP-EDGETEPDW 229
Cdd:PTZ00184  13 FKEAfslfDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMARKmKDTDSEEEI 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  230 VTTekkqFSEFrDMNKDGFLDATEVSHWILPTEVDHADNEARHLIHETDKDNDDKITKKE 289
Cdd:PTZ00184  87 KEA----FKVF-DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
71-182 2.00e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  71 LGKIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEYDQNKDGKIGWIEYKNTTYGYYIDTEfddvddkatyk 150
Cdd:COG5126  35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE----------- 103

                        90       100       110
                ....*....|....*....|....*....|..
gi 50344972 151 smlnRDERRFKSADRDGDGVATREEFTAFLHP 182
Cdd:COG5126 104 ----EADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 73-122 1.56e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.15  E-value: 1.56e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 50344972  73 KIVDKIDTDKDGFVSHAELHHWIKHRQRRYIEENVDKHWNEYDQNKDGKI 122
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKI 53
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
46-135 4.57e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 4.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  46 DHEAFLGKEESKTF-DQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIkhRQRRYIEENVDKHWNEYDQNKDGKIGW 124
Cdd:COG5126  45 DGDGRISREEFVAGmESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISF 122

                        90
                ....*....|.
gi 50344972 125 IEYKNTTYGYY 135
Cdd:COG5126 123 EEFVAAVRDYY 133
PTZ00183 PTZ00183
centrin; Provisional
 164-297 6.95e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  164 DRDGDGVATREEFTAFLHPEEFDFMRDiVIQETIEDIDKNGDGKIDLQEYIgDMYNPEDGETEPDwvTTEKKQFSEFRDM 243
Cdd:PTZ00183  27 DTDGSGTIDPKELKVAMRSLGFEPKKE-EIKQMIADVDKDGSGKIDFEEFL-DIMTKKLGERDPR--EEILKAFRLFDDD 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50344972  244 N--KDGFLDATEVSHWILPTevdHADNEARHLIHETDKDNDDKITKKE---ILENWNMF 297
Cdd:PTZ00183 103 KtgKISLKNLKRVAKELGET---ITDEELQEMIDEADRNGDGEISEEEfyrIMKKTNLF 158
EF-hand_7 pfam13499
EF-hand domain pair;
68-129 6.97e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 6.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50344972    68 KDRLGKIVDKIDTDKDGFVSHAELHHWIKHRQRRY--IEENVDKHWNEYDQNKDGKIGWIEYKN 129
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 57-208 1.55e-03

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: 39.26  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972  57 KTFDQLSPEESKDRLGKIVDKIDTDKDGFVSHAELHHWIKH----RQRRYIEENVDKHWN----EYDQNKDGKigwIEYK 128
Cdd:cd15902  78 LLFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKDlllkNKKHVSPPKLDEYTKlilkEFDANKDGK---LELD 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50344972 129 NTTYGYYIDTEFDDVDDKATYKSMLNRD-ERRFKSADRDGDGVATREEFTAFLH------------PEEFDFMRDIviqe 195
Cdd:cd15902 155 EMAKLLPVQENFLLKFQILGAMDLTKEDfEKVFEHYDKDNNGVIEGNELDALLKdlleknkadidkPDLENFRDAI---- 230

                       170
                ....*....|...
gi 50344972 196 tIEDIDKNGDGKI 208
Cdd:cd15902 231 -LRACDKNKDGKI 242
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 193-258 1.83e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 1.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50344972 193 IQETIEDIDKNGDGKIDLQEYIGDMYNPEDGETEPDWvtteKKQFSEFrDMNKDGFLDATEVSHWI 258
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI----DEMIREV-DKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 234-292 4.22e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.22  E-value: 4.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50344972 234 KKQFSEFrDMNKDGFLDATEVSHWILPTEVDHADNEARHLIHETDKDNDDKITKKEILE 292
Cdd:cd00051   3 REAFRLF-DKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 161-214 8.70e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 34.77  E-value: 8.70e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50344972 161 KSADRDGDGVA-TREEFTAFLHPEEFDFMRDIVIQETIEDI----DKNGDGKIDLQEYI 214
Cdd:cd00213  16 KYSGKEGDKDTlSKKELKELLETELPNFLKNQKDPEAVDKImkdlDVNKDGKVDFQEFL 74
 
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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