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Conserved domains on  [gi|1240085842|ref|NP_001341974|]
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reticulocalbin-3 precursor [Mus musculus]

Protein Classification

EFh_CREC_RCN3 domain-containing protein( domain architecture ID 11610940)

EFh_CREC_RCN3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 44-311 1.27e-179

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: 497.19  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  44 PHDDAHGNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 204 VVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEAN 283
Cdd:cd16230   161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 284 HLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16230   241 HLLHESDTDKDGRLSKAEILGNWNMFVG 268
 
Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 44-311 1.27e-179

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: 497.19  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  44 PHDDAHGNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 204 VVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEAN 283
Cdd:cd16230   161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 284 HLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16230   241 HLLHESDTDKDGRLSKAEILGNWNMFVG 268
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
166-309 7.11e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 166 ARDERRFRVADQDGDSMATREELTAflhpeefphMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPawvqTE 245
Cdd:COG5126     5 RKLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP----FA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240085842 246 RQQFREFrDLNKDGRLDGSEVGywVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILSNWNMF 309
Cdd:COG5126    72 RAAFDLL-DTDGDGKISADEFR--RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
170-227 7.53e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 7.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085842 170 RRFRVADQDGDSMATREELTAFLHP-EEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIA 227
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
72-234 3.17e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.59  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  72 SPEESQARLGRIVDRM--DLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWHTYDTDRDGRVGWEELRNATYGHYEPG 149
Cdd:NF041410   17 SSSTSSARSQQFQKQLfaKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 150 EEFHDVEDAETykkmlarderRFRVADQDGDSMATREELTAFLhpeefpHMRDIV--VAETLEDLDKNKDGYVQVEEYIA 227
Cdd:NF041410   97 DQAPSTELADD----------LLSALDTDGDGSISSDELSAGL------TSAGSSadSSQLFSALDSDGDGSVSSDELAA 160


                  ....*..
gi 1240085842 228 DLYSEEP 234
Cdd:NF041410  161 ALQPPPP 167
 
Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 44-311 1.27e-179

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: 497.19  E-value: 1.27e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  44 PHDDAHGNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 204 VVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEAN 283
Cdd:cd16230   161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 284 HLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16230   241 HLLHESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 44-311 5.58e-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: 391.56  E-value: 5.58e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  44 PHDDAHGNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDlaGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16226     1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKID--KNGDGFVTEEELKDWIKYVQKKYIREDVDRQWK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDveDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16226    79 EYDPNKDGKLSWEEYKKATYGFLDDEEEDDD--LHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 204 VVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEAN 283
Cdd:cd16226   157 VVQETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAK 236

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 284 HLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16226   237 HLIYEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 44-310 1.47e-130

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: 372.93  E-value: 1.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  44 PHDDAHGNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDlaGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd15899     1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMD--VDKDGFISAKELHSWILESFKRHAMEESKEQFR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDV--EDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd15899    79 AVDPDEDGHVSWDEYKNDTYGSVGDDEENVADniKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYML 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 202 DIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVE 281
Cdd:cd15899   159 DFVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEE 238

                         250       260
                  ....*....|....*....|....*....
gi 1240085842 282 ANHLLHESDTDKDGRLSKAEILSNWNMFV 310
Cdd:cd15899   239 AKHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 43-311 2.39e-120

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: 346.87  E-value: 2.39e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  43 APHDDAHgNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDlaGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAW 122
Cdd:cd16229     1 QLHEDNQ-SFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRID--DDKDGFVTTEELKAWIKRVQKRYIYENVAKVW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 123 HTYDTDRDGRVGWEELRNATYGHYEPG-EEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16229    78 KDYDLNKDNKISWEEYKQATYGYYLGNpEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 202 DIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVE 281
Cdd:cd16229   158 DIVVLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAE 237

                         250       260       270
                  ....*....|....*....|....*....|
gi 1240085842 282 ANHLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16229   238 ARHLVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 45-311 3.36e-103

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: 303.40  E-value: 3.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  45 HDDAHgNFQYDHEAFLGRDVAKEFDKLSPEESQARLGRIVDRMDlaGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWHT 124
Cdd:cd16228     3 HDDAQ-NFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKID--EDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 125 YDTDRDGRVGWEELRNATYGHYEpgeEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIV 204
Cdd:cd16228    80 HDLNEDGLVSWEEYKNATYGYIL---DDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 205 VAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEANH 284
Cdd:cd16228   157 VLETMEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARH 236

                         250       260
                  ....*....|....*....|....*..
gi 1240085842 285 LLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16228   237 LVYESDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 45-311 1.39e-67

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: 1.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  45 HDDAHGNFQYDHEAFLG-RDVAKEFDKLSPEESQARLGRIVDRMDLagDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16227     2 AKDGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDL--NDDGFIDRKELKAWILRSFKMLDEEEANERFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16227    80 EADEDGDGKVTWEEYLADSFGYDDEDNEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 204 VVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEeepaWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVEAN 283
Cdd:cd16227   160 LIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKE----WLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVD 235

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 284 HLLHESDTDKDGRLSKAEILSNWNMFVG 311
Cdd:cd16227   236 HLFASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 45-309 4.90e-62

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: 198.43  E-value: 4.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  45 HDDAHgNFQYDHEAFLGRDV-AKEFDKLSPEESQARLGRIVDRMDLagDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWH 123
Cdd:cd16224     3 PNGEH-NAEYDKEAFLGGEEdADEFAKLSPEEQQKRLKSIIKKIDT--DSDGFLTEEELSSWIQQSFRHYALEDAKQQFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 124 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAE--TYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16224    80 EYDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEeeSFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 202 DIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAWVQTERQQFREFRDLNKDGRLDGSEVGYWVLPPSQDQPLVE 281
Cdd:cd16224   160 EFVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEE 239

                         250       260
                  ....*....|....*....|....*...
gi 1240085842 282 ANHLLHESDTDKDGRLSKAEILSNWNMF 309
Cdd:cd16224   240 ALHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 47-309 3.34e-37

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: 134.35  E-value: 3.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  47 DAHGNFQYDHEAFLGrDVAKEFDKLSPEESQARLGRIVDRMDLagDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWHTY- 125
Cdd:cd16225     4 DGHLNKEFHKEVFLG-NEKEEFEEDSEPKKRKKLKEIFKKVDV--NTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIFk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 126 --DTDRDGRVGWEELR---------NATYGHYEPGEEFHDVEDAETyKKMLARDERRFRVADQDGDSMATREELTAFLHP 194
Cdd:cd16225    81 avDTDKDGNVSWEEYRvhfllskgySEEEAEEKIKNNEELKLDEDD-KEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 195 EEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPA---WVQTERQQFREFRDLNKDGRLDGSEVGYWVL 271
Cdd:cd16225   160 EHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAEDddeWKKERKKEFEEVIDLNHDGKVTKEELEEYMD 239

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1240085842 272 PPSQDQPLVEANHLLHESDTDKDGRLSKAEILSNWNMF 309
Cdd:cd16225   240 PRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
166-309 7.11e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 166 ARDERRFRVADQDGDSMATREELTAflhpeefphMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPawvqTE 245
Cdd:COG5126     5 RKLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP----FA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240085842 246 RQQFREFrDLNKDGRLDGSEVGywVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILSNWNMF 309
Cdd:COG5126    72 RAAFDLL-DTDGDGKISADEFR--RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
70-198 7.51e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 7.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  70 KLSPEESQARLGRIVDRM--DLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWHTYDTDRDGRVGWEELRNATyghye 147
Cdd:COG5126    21 VLERDDFEALFRRLWATLfsEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----- 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1240085842 148 pgeEFHDVEDAETykkmlardERRFRVADQDGDSMATREELTAFLHPEEFP 198
Cdd:COG5126    96 ---TALGVSEEEA--------DELFARLDTDGDGKISFEEFVAAVRDYYTP 135
EF-hand_7 pfam13499
EF-hand domain pair;
170-227 7.53e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 7.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085842 170 RRFRVADQDGDSMATREELTAFLHP-EEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIA 227
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-265 1.79e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.01  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 115 RDSVSAAWHTYDTDRDGRVGWEELRNAtyghyepgeefhdvedaetykkMLARDERRFRVADQDGDSMATREELTAFLHP 194
Cdd:COG5126     4 RRKLDRRFDLLDADGDGVLERDDFEAL----------------------FRRLWATLFSEADTDGDGRISREEFVAGMES 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240085842 195 EEFPHMRDIVVAeTLEDLDKNKDGYVQVEEYIADLYSEEPGEEEPAwvqterQQFREFrDLNKDGRLDGSE 265
Cdd:COG5126    62 LFEATVEPFARA-AFDLLDTDGDGKISADEFRRLLTALGVSEEEAD------ELFARL-DTDGDGKISFEE 124
EF-hand_7 pfam13499
EF-hand domain pair;
246-303 2.56e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 2.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 246 RQQFREFrDLNKDGRLDGSEVGYWVLPPSQDQPLV--EANHLLHESDTDKDGRLSKAEIL 303
Cdd:pfam13499   5 KEAFKLL-DSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKEFDLDKDGRISFEEFL 63
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
72-234 3.17e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.59  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842  72 SPEESQARLGRIVDRM--DLAGDSDGWVSLAELRAWIAHTQQRHIRDSVSAAWHTYDTDRDGRVGWEELRNATYGHYEPG 149
Cdd:NF041410   17 SSSTSSARSQQFQKQLfaKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 150 EEFHDVEDAETykkmlarderRFRVADQDGDSMATREELTAFLhpeefpHMRDIV--VAETLEDLDKNKDGYVQVEEYIA 227
Cdd:NF041410   97 DQAPSTELADD----------LLSALDTDGDGSISSDELSAGL------TSAGSSadSSQLFSALDSDGDGSVSSDELAA 160


                  ....*..
gi 1240085842 228 DLYSEEP 234
Cdd:NF041410  161 ALQPPPP 167
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 246-303 1.14e-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: 36.76  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1240085842 246 RQQFREFrDLNKDGRLDGSEVGYWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEIL 303
Cdd:cd00051     3 REAFRLF-DKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 169-227 1.76e-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: 36.37  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085842 169 ERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVvAETLEDLDKNKDGYVQVEEYIA 227
Cdd:cd00051     3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI-DEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 207-265 2.34e-03

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1240085842 207 ETLEDLDKNKDGYVQVEEYIADL--YSEEPGEEEPAWVqterqqFREFrDLNKDGRLDGSE 265
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEM------IREV-DKDGDGKIDFEE 57
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 247-301 2.97e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.66  E-value: 2.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240085842 247 QQFREFrDLNKDGRLDGSEVGYWV----LPPSqdqplvEANHLLHESDTDKDGRLSKAE 301
Cdd:cd00052     3 QIFRSL-DPDGDGLISGDEARPFLgksgLPRS------VLAQIWDLADTDKDGKLDKEE 54
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 213-304 5.33e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.19  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240085842 213 DKNKDGYVQVEEYiADLYseepgeeepAWVQTERQQFrEFRDLNKDGRLDGSEV-------GYWVLPPSqdqplveANHL 285
Cdd:cd16185    46 DRDGNGTIDFEEF-AALH---------QFLSNMQNGF-EQRDTSRSGRLDANEVhealaasGFQLDPPA-------FQAL 107

                          90
                  ....*....|....*....
gi 1240085842 286 LHESDTDKDGRLSKAEILS 304
Cdd:cd16185   108 FRKFDPDRGGSLGFDDYIE 126
 
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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