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Conserved domains on  [gi|4506457|ref|NP_002893|]
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reticulocalbin-2 isoform a precursor [Homo sapiens]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610930)

CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family protein; the family consists of a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55, reticulocalbin-3 (RCN-3), cab45 Ca2+-binding protein, and calumenin (also known as crocalbin or CBP-50); EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 29-296 1.14e-166

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: 463.83  E-value: 1.14e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd16224   1 HYPNGEHNAEYDKEAFLGGEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd16224  81 YDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEEESFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd16224 161 FVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEA 240

                       250       260
                ....*....|....*....|....*...
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16224 241 LHLIDEMDLNGDGRLSEEEILENQDLFL 268
 
Name Accession Description Interval E-value
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 29-296 1.14e-166

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: 463.83  E-value: 1.14e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd16224   1 HYPNGEHNAEYDKEAFLGGEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd16224  81 YDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEEESFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd16224 161 FVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEA 240

                       250       260
                ....*....|....*....|....*...
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16224 241 LHLIDEMDLNGDGRLSEEEILENQDLFL 268
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
153-290 2.77e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 2.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  153 KDKKRFEKANQDSGPGLSLEEFIAfehpeevdyMTEFVIQEALEEHDKNGDGFVSLEEFLGDYrwdptANEDPEWILVEK 232
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGM-----ESLFEATVEPFA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506457  233 DRFVNDYDKDNDGRLDPQELLPWVvpNNQGIAQEEALHLIDEMDLNGDKKLSEEEILE 290
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
239-290 2.75e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4506457    239 YDKDNDGRLDPQELLPWVVPNNQG--IAQEEALHLIDEMDLNGDKKLSEEEILE 290
Cdd:pfam13499  11 LDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLE 64
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
61-121 2.21e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506457    61 EQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVTWDE 121
Cdd:NF041410  24 RSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDE 84
PRK12309 PRK12309
transaldolase;
143-253 5.19e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 38.18  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   143 EEESFRKLHLKDKKRFEKAnqDSG-PGLS-----LEEFIAfEHPEEVDYMTEF--VIQEALEEHDKNGDGFVSLEEFLGd 214
Cdd:PRK12309 283 DRATFDKMHAEDRMASEKL--DEGiKGFSkaletLEKLLA-HRLARLEGGEAFthAAQEIFRLYDLDGDGFITREEWLG- 358

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 4506457   215 yrwdptanedpewilveKDRFVNDYDKDNDGRLDPQELL 253
Cdd:PRK12309 359 -----------------SDAVFDALDLNHDGKITPEEMR 380
 
Name Accession Description Interval E-value
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 29-296 1.14e-166

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: 463.83  E-value: 1.14e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd16224   1 HYPNGEHNAEYDKEAFLGGEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd16224  81 YDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEEESFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd16224 161 FVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEA 240

                       250       260
                ....*....|....*....|....*...
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16224 241 LHLIDEMDLNGDGRLSEEEILENQDLFL 268
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 29-296 1.29e-122

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: 352.13  E-value: 1.29e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGVqEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd15899   1 HEMDGHLNSDYDHEAFLGK-EEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd15899  80 VDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd15899 160 FVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEA 239

                       250       260
                ....*....|....*....|....*...
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd15899 240 KHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 29-295 2.29e-76

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: 234.40  E-value: 2.29e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGvQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLG-KEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDrvidFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd16226  80 YDPNKDGKLSWEEYKKATYG----FLDDEEEDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd16226 156 IVVQETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEA 235

                       250       260
                ....*....|....*....|....*..
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLF 295
Cdd:cd16226 236 KHLIYEADDDKDGKLTKEEILDKYDLF 262
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 29-296 7.76e-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: 212.56  E-value: 7.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   29 HYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVE 108
Cdd:cd16227   1 HAKDGEHNPEFDHEAVLGSRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  109 YDKNSDDTVTWDEYNIQMYDrvIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTE 188
Cdd:cd16227  81 ADEDGDGKVTWEEYLADSFG--YDDEDNEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  189 FVIQEALEEHDKNGDGFVSLEEFLGDyrwdPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEA 268
Cdd:cd16227 159 VLIEQTLRDKDKDNDGFISFQEFLGD----RAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEV 234

                       250       260
                ....*....|....*....|....*...
gi 4506457  269 LHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16227 235 DHLFASADDDHDDRLSFDEILDHHEIFV 262
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 38-296 4.70e-56

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: 182.45  E-value: 4.70e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   38 DYDREALLGvQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTV 117
Cdd:cd16228  10 DYDHDAFLG-AEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDLNEDGLV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  118 TWDEYNIQMYdrvidfdeNTALDDAEEE---SFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEA 194
Cdd:cd16228  89 SWEEYKNATY--------GYILDDPDPDdgfNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  195 LEEHDKNGDGFVSLEEFLGD-YRWDPTANEdPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLID 273
Cdd:cd16228 161 MEDIDKNGDGFIDLEEYIGDmYSQDGDADE-PEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVY 239

                       250       260
                ....*....|....*....|...
gi 4506457  274 EMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16228 240 ESDQNKDGKLTKEEIVDKYDLFV 262
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 39-296 2.29e-54

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: 178.24  E-value: 2.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   39 YDREALLGvQEDVDEYVKLGHEEQQKRLQAIIKKIDL--DSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDT 116
Cdd:cd16230  11 YDHEAFLG-REVAKEFDQLSPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRDGR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  117 VTWDEYNIQMYDRVIDFDENTALDDAEeeSFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEALE 196
Cdd:cd16230  90 VGWEELRNATYGHYEPGEEFHDVEDAE--TYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVVAETLE 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  197 EHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLIDEMD 276
Cdd:cd16230 168 DLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESD 247

                       250       260
                ....*....|....*....|
gi 4506457  277 LNGDKKLSEEEILENPDLFL 296
Cdd:cd16230 248 TDKDGRLSKAEILGNWNMFV 267
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 39-296 3.20e-53

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: 175.45  E-value: 3.20e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   39 YDREALLGvQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVT 118
Cdd:cd16229  11 YDHEAFLG-KEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDYDLNKDNKIS 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  119 WDEYNIQMYDRVIDfDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEALEEH 198
Cdd:cd16229  90 WEEYKQATYGYYLG-NPEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVVLETLEDI 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  199 DKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLIDEMDLN 278
Cdd:cd16229 169 DKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDKD 248

                       250
                ....*....|....*...
gi 4506457  279 GDKKLSEEEILENPDLFL 296
Cdd:cd16229 249 KDQKLTKEEILDNWNMFV 266
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 33-296 6.52e-38

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: 135.89  E-value: 6.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   33 GERRSDYDREALLGvqEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFK-HY--AMQEAKQQFVEY 109
Cdd:cd16225   5 GHLNKEFHKEVFLG--NEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQeHFqeAVEENEQIFKAV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  110 DKNSDDTVTWDEYNIQmYDRVIDFDENTALDDAEEESFRKLHLKD-------KKRFEKANQDSGPGLSLEEFIAFEHPEE 182
Cdd:cd16225  83 DTDKDGNVSWEEYRVH-FLLSKGYSEEEAEEKIKNNEELKLDEDDkevldryKDRWSQADEPEDGLLDVEEFLSFRHPEH 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  183 VDYMTEFVIQEALEEHDKNGDGFVSLEEFL-GDYRWDP--TANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPN 259
Cdd:cd16225 162 SRGMLKNMVKEILHDLDQDGDEKLTLDEFVsLPPGTVEeqQAEDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPR 241

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 4506457  260 NQGIAQEEALHLIDEMDLNGDKKLSEEEILENPDLFL 296
Cdd:cd16225 242 NERHALNEAKQLIAVADENKDGKLSLEEILKNSDLFT 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
153-290 2.77e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 2.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  153 KDKKRFEKANQDSGPGLSLEEFIAfehpeevdyMTEFVIQEALEEHDKNGDGFVSLEEFLGDYrwdptANEDPEWILVEK 232
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGM-----ESLFEATVEPFA 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506457  233 DRFVNDYDKDNDGRLDPQELLPWVvpNNQGIAQEEALHLIDEMDLNGDKKLSEEEILE 290
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
60-212 7.17e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 7.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   60 EEQQKRLQAIIKKIDLDSDGFLTESELSSwiqmsfkhYAMQEAKQQFVEYDKNSDDTVTWDEYNIQMYDRVIDFDENTAl 139
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506457  140 ddaeeesfrklhlkdKKRFEKANQDSGPGLSLEEFIAFEHPEEVdymTEFVIQEALEEHDKNGDGFVSLEEFL 212
Cdd:COG5126  72 ---------------RAAFDLLDTDGDGKISADEFRRLLTALGV---SEEEADELFARLDTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
98-256 5.11e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   98 AMQEAKQQ--FVEYDKNSDDTVTWDEYNiQMYDRVIDfdentalddaeeesfrklhlkdkKRFEKANQDSGPGLSLEEFI 175
Cdd:COG5126   1 DLQRRKLDrrFDLLDADGDGVLERDDFE-ALFRRLWA-----------------------TLFSEADTDGDGRISREEFV 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457  176 AFEHPEEVDYMTEFViQEALEEHDKNGDGFVSLEEFLgdyrwdpTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPW 255
Cdd:COG5126  57 AGMESLFEATVEPFA-RAAFDLLDTDGDGKISADEFR-------RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128


                .
gi 4506457  256 V 256
Cdd:COG5126 129 V 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-121 3.06e-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: 40.99  E-value: 3.06e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4506457   65 RLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVTWDE 121
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEE 57
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 191-256 4.07e-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: 40.61  E-value: 4.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506457  191 IQEALEEHDKNGDGFVSLEEF---LGDYRWDPTaneDPEWilvekDRFVNDYDKDNDGRLDPQELLPWV 256
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELkaaLKSLGEGLS---EEEI-----DEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 237-290 5.98e-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: 40.22  E-value: 5.98e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506457  237 NDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLIDEMDLNGDKKLSEEEILE 290
Cdd:cd00051   7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
36-121 1.32e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   36 RSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMsfKHYAMQEAKQQFVEYDKNSDD 115
Cdd:COG5126  41 EADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA--LGVSEEEADELFARLDTDGDG 118


                ....*.
gi 4506457  116 TVTWDE 121
Cdd:COG5126 119 KISFEE 124
EF-hand_7 pfam13499
EF-hand domain pair;
239-290 2.75e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4506457    239 YDKDNDGRLDPQELLPWVVPNNQG--IAQEEALHLIDEMDLNGDKKLSEEEILE 290
Cdd:pfam13499  11 LDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 65-212 3.78e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 39.96  E-value: 3.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   65 RLQAIIKKIDLDSDGFLTESELSSWIQ-MSFKHYAmQEAKQQFVEYDKNSDDTVTWDEYniqmydrvidfdentalddae 143
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKrLNIRVSE-KELKKLFKEVDTNGDGTLTFDEF--------------------- 58

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506457  144 EESFRKLHLKD--KKRFEKANQDSGPGLSLEEFIAF---EHPEEVDYMTEFVIQEALEEHDKNgdGFVSLEEFL 212
Cdd:cd15898  59 EELYKSLTERPelEPIFKKYAGTNRDYMTLEEFIRFlreEQGENVSEEECEELIEKYEPEREN--RQLSFEGFT 130
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
61-121 2.21e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506457    61 EQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVTWDE 121
Cdd:NF041410  24 RSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDE 84
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 169-212 3.15e-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: 35.60  E-value: 3.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 4506457  169 LSLEEFIAFeHPEEVDYMTEFVIQEALEEHDKNGDGFVSLEEFL 212
Cdd:cd00051  17 ISADELKAA-LKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
PRK12309 PRK12309
transaldolase;
143-253 5.19e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 38.18  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506457   143 EEESFRKLHLKDKKRFEKAnqDSG-PGLS-----LEEFIAfEHPEEVDYMTEF--VIQEALEEHDKNGDGFVSLEEFLGd 214
Cdd:PRK12309 283 DRATFDKMHAEDRMASEKL--DEGiKGFSkaletLEKLLA-HRLARLEGGEAFthAAQEIFRLYDLDGDGFITREEWLG- 358

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 4506457   215 yrwdptanedpewilveKDRFVNDYDKDNDGRLDPQELL 253
Cdd:PRK12309 359 -----------------SDAVFDALDLNHDGKITPEEMR 380
EF-hand_7 pfam13499
EF-hand domain pair;
64-122 6.53e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.54  E-value: 6.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506457     64 KRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAM--QEAKQQFVEYDKNSDDTVTWDEY 122
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEF 62
EF-hand_7 pfam13499
EF-hand domain pair;
188-253 7.87e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.54  E-value: 7.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506457    188 EFVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEwilVEKDRFVNDYDKDNDGRLDPQELL 253
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSD---EEVEELFKEFDLDKDGRISFEEFL 63
 
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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