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Conserved domains on  [gi|314122181|ref|NP_001186602|]
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calumenin isoform e precursor [Homo sapiens]

Protein Classification

CREC-EF hand family protein( domain architecture ID 707362)

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)

Gene Ontology:  GO:0005509
PubMed:  28707401

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC super family cl25354
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 37-223 3.44e-119

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.


The actual alignment was detected with superfamily member cd16228:

Pssm-ID: 330175 [Multi-domain]  Cd Length: 263  Bit Score: 339.61  E-value: 3.44e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228    1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228   81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                        170       180
                 ....*....|....*....|....*..
gi 314122181 197 MEDIDKNADGFIDLEEYIGWQAYQGGD 223
Cdd:cd16228  161 MEDIDKNGDGFIDLEEYIGDMYSQDGD 187
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-223 3.44e-119

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: 339.61  E-value: 3.44e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228    1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228   81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                        170       180
                 ....*....|....*....|....*..
gi 314122181 197 MEDIDKNADGFIDLEEYIGWQAYQGGD 223
Cdd:cd16228  161 MEDIDKNGDGFIDLEEYIGDMYSQDGD 187
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-212 1.58e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  67 EESKERLGKIVSKIDGDKDGFVTVDELKdwiKFAQKRWiyedvERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDg 146
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFE---ALFRRLW-----ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 314122181 147 fnykqmmvrdERRFKMADKDGDLIATKEEFTAFLHPEEYDymkDIVVQETMEDIDKNADGFIDLEE 212
Cdd:COG5126   72 ----------RAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEE 124
EF-hand_7 pfam13499
EF-hand domain pair;
158-216 9.14e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 9.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  158 RRFKMADKDGDLIATKEEFTAFLHPEEYDY-MKDIVVQETMEDIDKNADGFIDLEEYIGW 216
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
PLN02964 PLN02964
phosphatidylserine decarboxylase
 31-128 1.68e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  31 EPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLT-------PEESKERLGK-IVSKIDGDKDGFVTVDELKDWIKFAQK 102
Cdd:PLN02964 131 ELDLFDFVTQEPESACESFDLLDPSSSNKVVGSIFvscsiedPVETERSFARrILAIVDYDEDGQLSFSEFSDLIKAFGN 210

                         90       100
                 ....*....|....*....|....*.
gi 314122181 103 RWIYEDVERQWKGHDLNEDGLVSWEE 128
Cdd:PLN02964 211 LVAANKKEELFKAADLNGDGVVTIDE 236
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-223 3.44e-119

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: 339.61  E-value: 3.44e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228    1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228   81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                        170       180
                 ....*....|....*....|....*..
gi 314122181 197 MEDIDKNADGFIDLEEYIGWQAYQGGD 223
Cdd:cd16228  161 MEDIDKNGDGFIDLEEYIGDMYSQDGD 187
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 39-215 1.17e-95

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: 279.85  E-value: 1.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  39 HNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDL 118
Cdd:cd16226    3 DDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 119 NEDGLVSWEEYKNATYGYVLDDP-DPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETM 197
Cdd:cd16226   83 NKDGKLSWEEYKKATYGFLDDEEeDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQETL 162

                        170
                 ....*....|....*...
gi 314122181 198 EDIDKNADGFIDLEEYIG 215
Cdd:cd16226  163 EDIDKNKDGFISLEEYIG 180
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 37-215 5.87e-87

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: 258.14  E-value: 5.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd15899    1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDDPDPD-----DGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDI 191
Cdd:cd15899   81 DPDEDGHVSWDEYKNDTYGSVGDDEENVadnikEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDF 160

                        170       180
                 ....*....|....*....|....
gi 314122181 192 VVQETMEDIDKNADGFIDLEEYIG 215
Cdd:cd15899  161 VIKETLEDLDKNGDGFISLEEFIS 184
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 37-215 7.04e-86

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: 255.19  E-value: 7.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16229    1 QLHEDNQSFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDDP----DPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIV 192
Cdd:cd16229   81 DLNKDNKISWEEYKQATYGYYLGNPeefqDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIV 160

                        170       180
                 ....*....|....*....|...
gi 314122181 193 VQETMEDIDKNADGFIDLEEYIG 215
Cdd:cd16229  161 VLETLEDIDKNGDGFVDEDEYIA 183
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 39-214 2.03e-72

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: 221.00  E-value: 2.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  39 HNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKID--GDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16230    3 DDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 117 DLNEDGLVSWEEYKNATYGYVLDD---PDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVV 193
Cdd:cd16230   83 DTDRDGRVGWEELRNATYGHYEPGeefHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVV 162

                        170       180
                 ....*....|....*....|.
gi 314122181 194 QETMEDIDKNADGFIDLEEYI 214
Cdd:cd16230  163 AETLEDLDKNKDGYVQVEEYI 183
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 39-215 7.39e-45

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: 150.66  E-value: 7.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  39 HNDAQSFDYDHDAFLGAE-EAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHD 117
Cdd:cd16224    3 PNGEHNAEYDKEAFLGGEeDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPEYD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 118 LNEDGLVSWEEYKNATYGYVLD---DPDPDDGF--NYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIV 192
Cdd:cd16224   83 KDGDGAVTWDEYNMQMYDRVIDydeDTVLDDEEeeSFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTEFV 162

                        170       180
                 ....*....|....*....|...
gi 314122181 193 VQETMEDIDKNADGFIDLEEYIG 215
Cdd:cd16224  163 IQEALEEHDKDGDGFISLEEFLG 185
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 40-215 2.08e-42

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: 144.00  E-value: 2.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  40 NDAQSFDYDHDAFLG-AEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDL 118
Cdd:cd16227    4 DGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 119 NEDGLVSWEEYKNATYGYVLDDPDP---DDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQE 195
Cdd:cd16227   84 DGDGKVTWEEYLADSFGYDDEDNEEmikDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQ 163

                        170       180
                 ....*....|....*....|
gi 314122181 196 TMEDIDKNADGFIDLEEYIG 215
Cdd:cd16227  164 TLRDKDKDNDGFISFQEFLG 183
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 46-214 4.23e-22

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: 91.21  E-value: 4.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  46 DYDHDAFLGaEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDV---ERQWKGHDLNEDG 122
Cdd:cd16225   10 EFHKEVFLG-NEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVeenEQIFKAVDTDKDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 123 LVSWEEY---------------KNATYGYVLDDPDPDDgfnyKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDY 187
Cdd:cd16225   89 NVSWEEYrvhfllskgyseeeaEEKIKNNEELKLDEDD----KEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHPEHSRG 164

                        170       180
                 ....*....|....*....|....*..
gi 314122181 188 MKDIVVQETMEDIDKNADGFIDLEEYI 214
Cdd:cd16225  165 MLKNMVKEILHDLDQDGDEKLTLDEFV 191
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-212 1.58e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  67 EESKERLGKIVSKIDGDKDGFVTVDELKdwiKFAQKRWiyedvERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDg 146
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFE---ALFRRLW-----ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 314122181 147 fnykqmmvrdERRFKMADKDGDLIATKEEFTAFLHPEEYDymkDIVVQETMEDIDKNADGFIDLEE 212
Cdd:COG5126   72 ----------RAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEE 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
36-182 8.64e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  36 DKVHNDAQSFDYDHDAFLGAEEAKTFdqltpeeSKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKG 115
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEAL-------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 314122181 116 HDLNEDGLVSWEEYKNATYGYVLDDPDPDDgfnykqmmvrderRFKMADKDGDLIATKEEFTAFLHP 182
Cdd:COG5126   78 LDTDGDGKISADEFRRLLTALGVSEEEADE-------------LFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 157-216 1.83e-06

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: 44.08  E-value: 1.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181 157 ERRFKMADKDGDLIATKEEFTAFLhPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYIGW 216
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAAL-KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 45-98 6.59e-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: 39.84  E-value: 6.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 314122181  45 FDYDHDAFLGAEEAKTF-DQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIK 98
Cdd:cd00051    9 FDKDGDGTISADELKAAlKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
158-216 9.14e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 9.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  158 RRFKMADKDGDLIATKEEFTAFLHPEEYDY-MKDIVVQETMEDIDKNADGFIDLEEYIGW 216
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
157-213 1.53e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 314122181 157 ERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVvQETMEDIDKNADGFIDLEEY 213
Cdd:COG5126   36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA-RAAFDLLDTDGDGKISADEF 91
PLN02964 PLN02964
phosphatidylserine decarboxylase
 31-128 1.68e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 314122181  31 EPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLT-------PEESKERLGK-IVSKIDGDKDGFVTVDELKDWIKFAQK 102
Cdd:PLN02964 131 ELDLFDFVTQEPESACESFDLLDPSSSNKVVGSIFvscsiedPVETERSFARrILAIVDYDEDGQLSFSEFSDLIKAFGN 210

                         90       100
                 ....*....|....*....|....*.
gi 314122181 103 RWIYEDVERQWKGHDLNEDGLVSWEE 128
Cdd:PLN02964 211 LVAANKKEELFKAADLNGDGVVTIDE 236
 
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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