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Conserved domains on  [gi|30316268|sp|Q96D15|]
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RecName: Full=Reticulocalbin-3; AltName: Full=EF-hand calcium-binding protein RLP49; Flags: Precursor

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610940)

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_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
44-311 0e+00

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: 513.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230   1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230  81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 204 VIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEAN 283
Cdd:cd16230 161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240
                       250       260
                ....*....|....*....|....*...
gi 30316268 284 HLLHESDTDKDGRLSKAEILGNWNMFVG 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 0e+00

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: 513.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230   1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230  81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 204 VIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEAN 283
Cdd:cd16230 161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240
                       250       260
                ....*....|....*....|....*...
gi 30316268 284 HLLHESDTDKDGRLSKAEILGNWNMFVG 311
Cdd:cd16230 241 HLLHESDTDKDGRLSKAEILGNWNMFVG 268
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
74-227 3.39e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 3.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  74 EESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQrhirdsvsAAWDTYDTDRDGRVGWEELRNATyghyapgeefh 153
Cdd:COG5126   1 DLQRRKLDRRFDLLDA--DGDGVLERDDFEALFRRLWA--------TLFSEADTDGDGRISREEFVAGM----------- 59
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30316268 154 dveDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPhmrDIVIAETLEDLDRNKDGYVQVEEYIA 227
Cdd:COG5126  60 ---ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
170-227 1.51e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.24  E-value: 1.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30316268   170 RRFRVADQDGDSMATREELTAFLHP-EEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIA 227
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
92-234 4.97e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.82  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268   92 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETykkmlarderR 171
Cdd:NF041410  39 DGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADD----------L 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30316268  172 FRVADQDGDSMATREELTAFLhpeefPHMRDIVIAETLED-LDRNKDGYVQVEEYIADLYSAEP 234
Cdd:NF041410 109 LSALDTDGDGSISSDELSAGL-----TSAGSSADSSQLFSaLDSDGDGSVSSDELAAALQPPPP 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 0e+00

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: 513.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230   1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230  81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 204 VIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEAN 283
Cdd:cd16230 161 VVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEAN 240
                       250       260
                ....*....|....*....|....*...
gi 30316268 284 HLLHESDTDKDGRLSKAEILGNWNMFVG 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 1.52e-141

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: 400.42  E-value: 1.52e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKID--KNGDGFVTEEELKDWIKYVQKKYIREDVDRQWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDveDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16226  79 EYDPNKDGKLSWEEYKKATYGFLDDEEEDDD--LHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 204 VIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEAN 283
Cdd:cd16226 157 VVQETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAK 236
                       250       260
                ....*....|....*....|....*...
gi 30316268 284 HLLHESDTDKDGRLSKAEILGNWNMFVG 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 1.15e-136

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: 388.34  E-value: 1.15e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd15899   1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMD--VDKDGFISAKELHSWILESFKRHAMEESKEQFR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDV--EDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd15899  79 AVDPDEDGHVSWDEYKNDTYGSVGDDEENVADniKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 202 DIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVE 281
Cdd:cd15899 159 DFVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEE 238
                       250       260
                ....*....|....*....|....*....
gi 30316268 282 ANHLLHESDTDKDGRLSKAEILGNWNMFV 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 2.05e-123

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: 354.96  E-value: 2.05e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  43 APHDDAHgNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAW 122
Cdd:cd16229   1 QLHEDNQ-SFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRID--DDKDGFVTTEELKAWIKRVQKRYIYENVAKVW 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 123 DTYDTDRDGRVGWEELRNATYGHY-APGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16229  78 KDYDLNKDNKISWEEYKQATYGYYlGNPEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 202 DIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVE 281
Cdd:cd16229 158 DIVVLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAE 237
                       250       260       270
                ....*....|....*....|....*....|
gi 30316268 282 ANHLLHESDTDKDGRLSKAEILGNWNMFVG 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 2.79e-104

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: 306.10  E-value: 2.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  45 HDDAHgNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDT 124
Cdd:cd16228   3 HDDAQ-NFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKID--EDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 125 YDTDRDGRVGWEELRNATYGHYApgeEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIV 204
Cdd:cd16228  80 HDLNEDGLVSWEEYKNATYGYIL---DDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 205 IAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANH 284
Cdd:cd16228 157 VLETMEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARH 236
                       250       260
                ....*....|....*....|....*..
gi 30316268 285 LLHESDTDKDGRLSKAEILGNWNMFVG 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 8.17e-66

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: 207.94  E-value: 8.17e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  45 HDDAHGNFQYDHEAFLG-REVAKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16227   2 AKDGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDL--NDDGFIDRKELKAWILRSFKMLDEEEANERFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16227  80 EADEDGDGKVTWEEYLADSFGYDDEDNEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 204 VIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEeepaWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEAN 283
Cdd:cd16227 160 LIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKE----WLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVD 235
                       250       260
                ....*....|....*....|....*...
gi 30316268 284 HLLHESDTDKDGRLSKAEILGNWNMFVG 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 1.60e-59

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: 191.88  E-value: 1.60e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  45 HDDAHgNFQYDHEAFLGREV-AKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16224   3 PNGEH-NAEYDKEAFLGGEEdADEFAKLSPEEQQKRLKSIIKKIDT--DSDGFLTEEELSSWIQQSFRHYALEDAKQQFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAE--TYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16224  80 EYDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEeeSFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 202 DIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVE 281
Cdd:cd16224 160 EFVIQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEE 239
                       250       260
                ....*....|....*....|....*...
gi 30316268 282 ANHLLHESDTDKDGRLSKAEILGNWNMF 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 3.13e-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: 3.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  47 DAHGNFQYDHEAFLGREVaKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAA---WD 123
Cdd:cd16225   4 DGHLNKEFHKEVFLGNEK-EEFEEDSEPKKRKKLKEIFKKVDV--NTDGFLSAEELEDWIMEKTQEHFQEAVEENeqiFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 124 TYDTDRDGRVGWEELR---------NATYGHYAPGEEFHDVEDAETyKKMLARDERRFRVADQDGDSMATREELTAFLHP 194
Cdd:cd16225  81 AVDTDKDGNVSWEEYRvhfllskgySEEEAEEKIKNNEELKLDEDD-KEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 195 EEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPA---WVQTERQQFRDFRDLNKDGHLDGSEVGHWVL 271
Cdd:cd16225 160 EHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAEDddeWKKERKKEFEEVIDLNHDGKVTKEELEEYMD 239
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 30316268 272 PPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMF 309
Cdd:cd16225 240 PRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
74-227 3.39e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 3.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  74 EESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQrhirdsvsAAWDTYDTDRDGRVGWEELRNATyghyapgeefh 153
Cdd:COG5126   1 DLQRRKLDRRFDLLDA--DGDGVLERDDFEALFRRLWA--------TLFSEADTDGDGRISREEFVAGM----------- 59
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30316268 154 dveDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPhmrDIVIAETLEDLDRNKDGYVQVEEYIA 227
Cdd:COG5126  60 ---ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEEFVA 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
70-198 5.75e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.95  E-value: 5.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  70 QLTPEESQARLGRIVDRMDRAGD--GDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATyghya 147
Cdd:COG5126  21 VLERDDFEALFRRLWATLFSEADtdGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----- 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 30316268 148 pgeEFHDVEDAETykkmlardERRFRVADQDGDSMATREELTAFLHPEEFP 198
Cdd:COG5126  96 ---TALGVSEEEA--------DELFARLDTDGDGKISFEEFVAAVRDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
166-303 7.25e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.56  E-value: 7.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 166 ARDERRFRVADQDGDSMATREELTAflhpeefphMRDIVIAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPawvqTE 245
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP----FA 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30316268 246 RQQFRDFrDLNKDGHLDGSEVGHWVlpPAQDQPLVEANHLLHESDTDKDGRLSKAEIL 303
Cdd:COG5126  72 RAAFDLL-DTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-270 4.26e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 4.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268 115 RDSVSAAWDTYDTDRDGRVGWEELRNAtyghyapgeefhdvedaetykkMLARDERRFRVADQDGDSMATREELTAFLHP 194
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEAL----------------------FRRLWATLFSEADTDGDGRISREEFVAGMES 61
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30316268 195 EEFPHMRDIViAETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAwvqterQQFRDFrDLNKDGHLDGSEVGHWV 270
Cdd:COG5126  62 LFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD------ELFARL-DTDGDGKISFEEFVAAV 129
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
63-148 4.43e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 4.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268  63 EVAKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIahTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNAT 142
Cdd:COG5126  54 EFVAGMESLFEATVEPFARAAFDLLDT--DGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129

                ....*.
gi 30316268 143 YGHYAP 148
Cdd:COG5126 130 RDYYTP 135
EF-hand_7 pfam13499
EF-hand domain pair;
170-227 1.51e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.24  E-value: 1.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30316268   170 RRFRVADQDGDSMATREELTAFLHP-EEFPHMRDIVIAETLEDLDRNKDGYVQVEEYIA 227
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EF-hand_7 pfam13499
EF-hand domain pair;
246-303 3.30e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 3.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268   246 RQQFRDFrDLNKDGHLDGSEVGHWVLPPAQDQPLV--EANHLLHESDTDKDGRLSKAEIL 303
Cdd:pfam13499   5 KEAFKLL-DSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKEFDLDKDGRISFEEFL 63
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
92-234 4.97e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.82  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30316268   92 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETykkmlarderR 171
Cdd:NF041410  39 DGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADD----------L 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30316268  172 FRVADQDGDSMATREELTAFLhpeefPHMRDIVIAETLED-LDRNKDGYVQVEEYIADLYSAEP 234
Cdd:NF041410 109 LSALDTDGDGSISSDELSAGL-----TSAGSSADSSQLFSaLDSDGDGSVSSDELAAALQPPPP 167
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
246-303 1.03e-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: 1.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30316268 246 RQQFRDFrDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEIL 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 1.49e-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: 1.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30316268 169 ERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIvIAETLEDLDRNKDGYVQVEEYIA 227
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEE-IDEMIREVDKDGDGKIDFEEFLE 60
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
247-301 4.45e-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: 35.27  E-value: 4.45e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30316268 247 QQFRDFrDLNKDGHLDGSEV----GHWVLPPaqdqplVEANHLLHESDTDKDGRLSKAE 301
Cdd:cd00052   3 QIFRSL-DPDGDGLISGDEArpflGKSGLPR------SVLAQIWDLADTDKDGKLDKEE 54
EF-hand_7 pfam13499
EF-hand domain pair;
79-143 4.66e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.31  E-value: 4.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30316268    79 RLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRH--IRDSVSAAWDTYDTDRDGRVGWEELRNATY 143
Cdd:pfam13499   3 KLKEAFKLLDS--DGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
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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