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Conserved domains on  [gi|384875338|gb|AFI26261|]
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supercoiling factor variant C [Drosophila melanogaster]

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 ...
 45-313 2.14e-138

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: 392.72  E-value: 2.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQH 124
Cdd:cd16226    1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 125 NPDNNETISWDSYMQTVYGFMDDLSPDEKEQEengvSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGV 204
Cdd:cd16226   81 DPNKDGKLSWEEYKKATYGFLDDEEEDDDLHE----SYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 205 VLRETITDLDKDHDGKISVDEYIGDMYRSTGaEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEA 284
Cdd:cd16226  157 VVQETLEDIDKNKDGFISLEEYIGDMYRDDD-EEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEA 235

                        250       260
                 ....*....|....*....|....*....
gi 384875338 285 KHLLFEADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16226  236 KHLIYEADDDKDGKLTKEEILDKYDLFVG 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 ...
 45-313 2.14e-138

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: 392.72  E-value: 2.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQH 124
Cdd:cd16226    1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 125 NPDNNETISWDSYMQTVYGFMDDLSPDEKEQEengvSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGV 204
Cdd:cd16226   81 DPNKDGKLSWEEYKKATYGFLDDEEEDDDLHE----SYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 205 VLRETITDLDKDHDGKISVDEYIGDMYRSTGaEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEA 284
Cdd:cd16226  157 VVQETLEDIDKNKDGFISLEEYIGDMYRDDD-EEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEA 235

                        250       260
                 ....*....|....*....|....*....
gi 384875338 285 KHLLFEADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16226  236 KHLIYEADDDKDGKLTKEEILDKYDLFVG 264
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
167-306 1.40e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 167 KRDRYRWSVADQDLDDNLTKDEFTAFLHPedhpsmkgvVLRETITDLDKDHDGKISVDEYIgdmyrsTGAEDEEPEWVAN 246
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEALFRR---------LWATLFSEADTDGDGRISREEFV------AGMESLFEATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 247 EREAFSTHRDLDKDGYLNEEEVKQWIAPHDFdhSEAEAKHLLFEADADHDDKLTKEEILD 306
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
170-231 3.09e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 3.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384875338  170 RYRWSVADQDLDDNLTKDEFTAFLHPED-HPSMKGVVLRETITDLDKDHDGKISVDEYIGDMY 231
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 206-303 6.27e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.74  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 206 LRETITDLDKDHDGKISVDEYIGDMYRSTGAEDEEPEWvaneREAFSTHrDLDKDGYLNEEEVKQWIAPHDFDHSEAEAK 285
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEI----KEAFKVF-DRDGNGFISAAELRHVMTNLGEKLTDEEVD 123

                         90
                 ....*....|....*...
gi 384875338 286 HLLFEADADHDDKLTKEE 303
Cdd:PTZ00184 124 EMIREADVDGDGQINYEE 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 ...
 45-313 2.14e-138

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: 392.72  E-value: 2.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQH 124
Cdd:cd16226    1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 125 NPDNNETISWDSYMQTVYGFMDDLSPDEKEQEengvSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGV 204
Cdd:cd16226   81 DPNKDGKLSWEEYKKATYGFLDDEEEDDDLHE----SYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 205 VLRETITDLDKDHDGKISVDEYIGDMYRSTGaEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEA 284
Cdd:cd16226  157 VVQETLEDIDKNKDGFISLEEYIGDMYRDDD-EEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEA 235

                        250       260
                 ....*....|....*....|....*....
gi 384875338 285 KHLLFEADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16226  236 KHLIYEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 50-313 2.59e-92

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: 275.67  E-value: 2.59e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  50 EHNAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQHNPDNN 129
Cdd:cd16228    6 AQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDLNED 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 130 ETISWDSYMQTVYGF-MDDLSPDekeqeeNGVSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGVVLRE 208
Cdd:cd16228   86 GLVSWEEYKNATYGYiLDDPDPD------DGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 209 TITDLDKDHDGKISVDEYIGDMYRSTGaEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEAKHLL 288
Cdd:cd16228  160 TMEDIDKNGDGFIDLEEYIGDMYSQDG-DADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLV 238

                        250       260
                 ....*....|....*....|....*
gi 384875338 289 FEADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16228  239 YESDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 54-313 8.30e-90

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: 269.44  E-value: 8.30e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  54 QFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQHNPDNNETIS 133
Cdd:cd16229   10 QYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDYDLNKDNKIS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 134 WDSYMQTVYGFMDDlSPDEKEQEENGVSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGVVLRETITDL 213
Cdd:cd16229   90 WEEYKQATYGYYLG-NPEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVVLETLEDI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 214 DKDHDGKISVDEYIGDMYrSTGAEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEAKHLLFEADA 293
Cdd:cd16229  169 DKNGDGFVDEDEYIADMF-SHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDK 247

                        250       260
                 ....*....|....*....|
gi 384875338 294 DHDDKLTKEEILDKYDVFVG 313
Cdd:cd16229  248 DKDQKLTKEEILDNWNMFVG 267
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 52-313 1.12e-84

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: 256.44  E-value: 1.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  52 NAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDE--NKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQHNPDNN 129
Cdd:cd16230    8 NFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 130 ETISWDSYMQTVYGFMDDlsPDEKEQEENGVSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGVVLRET 209
Cdd:cd16230   88 GRVGWEELRNATYGHYEP--GEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVVAET 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 210 ITDLDKDHDGKISVDEYIGDMYRSTGAEdEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEAKHLLF 289
Cdd:cd16230  166 LEDLDKNKDGYVQVEEYIADLYSGEPGE-EEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLH 244

                        250       260
                 ....*....|....*....|....
gi 384875338 290 EADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16230  245 ESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 45-312 1.40e-83

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: 253.52  E-value: 1.40e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLGPDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQH 124
Cdd:cd15899    1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 125 NPDNNETISWDSYMQTVYGFMDDLSPDEKEQEENGVSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGV 204
Cdd:cd15899   81 DPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 205 VLRETITDLDKDHDGKISVDEYIGDMYRSTGAEdEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEA 284
Cdd:cd15899  161 VIKETLEDLDKNGDGFISLEEFISDPYSADENE-EEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEA 239

                        250       260
                 ....*....|....*....|....*...
gi 384875338 285 KHLLFEADADHDDKLTKEEILDKYDVFV 312
Cdd:cd15899  240 KHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 45-313 5.51e-69

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: 216.03  E-value: 5.51e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLGP-DESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQ 123
Cdd:cd16227    1 HAKDGEHNPEFDHEAVLGSrKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 124 HNPDNNETISWDSYMQTVYGFMD-DLSPDEKEQEENgvsYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMK 202
Cdd:cd16227   81 ADEDGDGKVTWEEYLADSFGYDDeDNEEMIKDSTED---DLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 203 GVVLRETITDLDKDHDGKISVDEYIGDMyrstgAEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEA 282
Cdd:cd16227  158 PVLIEQTLRDKDKDNDGFISFQEFLGDR-----AGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEE 232

                        250       260       270
                 ....*....|....*....|....*....|.
gi 384875338 283 EAKHLLFEADADHDDKLTKEEILDKYDVFVG 313
Cdd:cd16227  233 EVDHLFASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 45-311 7.43e-55

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: 179.94  E-value: 7.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  45 HFDGGEHNAQFDHEAFLG-PDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGRVWKQ 123
Cdd:cd16224    1 HYPNGEHNAEYDKEAFLGgEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 124 HNPDNNETISWDSYMQTVYG----FMDDLSPDEKEQEengvSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHP 199
Cdd:cd16224   81 YDKDGDGAVTWDEYNMQMYDrvidYDEDTVLDDEEEE----SFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 200 SMKGVVLRETITDLDKDHDGKISVDEYIGDmYRSTGAEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDH 279
Cdd:cd16224  157 YMTEFVIQEALEEHDKDGDGFISLEEFLGD-YRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGI 235

                        250       260       270
                 ....*....|....*....|....*....|..
gi 384875338 280 SEAEAKHLLFEADADHDDKLTKEEILDKYDVF 311
Cdd:cd16224  236 AQEEALHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 49-311 1.33e-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: 145.91  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338  49 GEHNAQFDHEAFLGpDESKKFDSLTPEESRRRLGVIVDRIDENKDGSVTLAELKNWIAYTQRRYIEEDVGR---VWKQHN 125
Cdd:cd16225    5 GHLNKEFHKEVFLG-NEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEEneqIFKAVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 126 PDNNETISWDSYMQTvygFMDDLSPDEKEQEENGVSYKSL---------LKRDRYRWSVADQDLDDNLTKDEFTAFLHPE 196
Cdd:cd16225   84 TDKDGNVSWEEYRVH---FLLSKGYSEEEAEEKIKNNEELkldeddkevLDRYKDRWSQADEPEDGLLDVEEFLSFRHPE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 197 DHPSMKGVVLRETITDLDKDHDGKISVDEYI--GDMYRSTGAEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAP 274
Cdd:cd16225  161 HSRGMLKNMVKEILHDLDQDGDEKLTLDEFVslPPGTVEEQQAEDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDP 240

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 384875338 275 HDFDHSEAEAKHLLFEADADHDDKLTKEEILDKYDVF 311
Cdd:cd16225  241 RNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
167-306 1.40e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 167 KRDRYRWSVADQDLDDNLTKDEFTAFLHPedhpsmkgvVLRETITDLDKDHDGKISVDEYIgdmyrsTGAEDEEPEWVAN 246
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEALFRR---------LWATLFSEADTDGDGRISREEFV------AGMESLFEATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 247 EREAFSTHRDLDKDGYLNEEEVKQWIAPHDFdhSEAEAKHLLFEADADHDDKLTKEEILD 306
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVA 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
170-275 5.24e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 170 RYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMkGVVLRETITDLDKDHDGKISVDEYiGDMYRSTGAEDEEPEwvanerE 249
Cdd:COG5126   36 ATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEF-RRLLTALGVSEEEAD------E 107

                         90       100
                 ....*....|....*....|....*.
gi 384875338 250 AFStHRDLDKDGYLNEEEVKQWIAPH 275
Cdd:COG5126  108 LFA-RLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 206-273 1.19e-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: 42.53  E-value: 1.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384875338 206 LRETITDLDKDHDGKISVDEYIGDMyRSTGAEDEEPEWvaneREAFStHRDLDKDGYLNEEEVKQWIA 273
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAAL-KSLGEGLSEEEI----DEMIR-EVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
206-327 2.74e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 206 LRETITDLDKDHDGKISVDEYigdmyrstgaedeEPEWVANEREAFSTHrDLDKDGYLNEEEVKQWIAPHDFDHSEAEAK 285
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDF-------------EALFRRLWATLFSEA-DTDGDGRISREEFVAGMESLFEATVEPFAR 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 384875338 286 HLLFEADADHDDKLTKEEILDKYDVFvGSQATDFGEALARHD 327
Cdd:COG5126   73 AAFDLLDTDGDGKISADEFRRLLTAL-GVSEEEADELFARLD 113
EF-hand_7 pfam13499
EF-hand domain pair;
170-231 3.09e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 3.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384875338  170 RYRWSVADQDLDDNLTKDEFTAFLHPED-HPSMKGVVLRETITDLDKDHDGKISVDEYIGDMY 231
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EF-hand_7 pfam13499
EF-hand domain pair;
248-308 5.01e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 5.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384875338  248 REAFSTHrDLDKDGYLNEEEVKQWIAPH--DFDHSEAEAKHLLFEADADHDDKLTKEEILDKY 308
Cdd:pfam13499   5 KEAFKLL-DSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 206-303 6.27e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.74  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384875338 206 LRETITDLDKDHDGKISVDEYIGDMYRSTGAEDEEPEWvaneREAFSTHrDLDKDGYLNEEEVKQWIAPHDFDHSEAEAK 285
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEI----KEAFKVF-DRDGNGFISAAELRHVMTNLGEKLTDEEVD 123

                         90
                 ....*....|....*...
gi 384875338 286 HLLFEADADHDDKLTKEE 303
Cdd:PTZ00184 124 EMIREADVDGDGQINYEE 141
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 248-306 6.71e-04

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: 37.53  E-value: 6.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384875338 248 REAFSTHrDLDKDGYLNEEEVKQWIAPHDFDHSEAEAKHLLFEADADHDDKLTKEEILD 306
Cdd:cd00051    3 REAFRLF-DKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 248-303 1.39e-03

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


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 37.51  E-value: 1.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384875338 248 REAFSThRDLDKDGYLNEEEVK---QWIAPHDFDHSEAEAKHLLFEADADHDDKLTKEE 303
Cdd:cd16251   37 KKVFQI-LDKDKSGFIEEEELKyilKGFSIAGRDLTDEETKALLAAGDTDGDGKIGVEE 94
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 256-303 4.71e-03

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


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 35.95  E-value: 4.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384875338 256 DLDKDGYLNEEEVK---QWIAPHDFDHSEAEAKHLLFEADADHDDKLTKEE 303
Cdd:cd16254   44 DKDKSGFIEEDELKfvlKGFSPDGRDLSDKETKALLAAGDKDGDGKIGIDE 94
 
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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