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Conserved domains on  [gi|4502551|ref|NP_001210|]
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calumenin isoform a precursor [Homo sapiens]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610936)

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_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-299 8.39e-175

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: 484.06  E-value: 8.39e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228   1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228  81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  197 MEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYE 276
Cdd:cd16228 161 MEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYE 240

                       250       260
                ....*....|....*....|...
gi 4502551  277 SDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16228 241 SDQNKDGKLTKEEIVDKYDLFVG 263
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-299 8.39e-175

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: 484.06  E-value: 8.39e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228   1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228  81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  197 MEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYE 276
Cdd:cd16228 161 MEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYE 240

                       250       260
                ....*....|....*....|...
gi 4502551  277 SDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16228 241 SDQNKDGKLTKEEIVDKYDLFVG 263
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
155-292 2.12e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  155 RDERRFKMADKDGDLIATKEEFTAFLHPeeydymkdiVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEwvkteR 234
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRR---------LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-----A 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4502551  235 EQFVEFRDKNRDGKMDKEETKDWIlpSDYDHAEAEARHLVYESDQNKDGKLTKEEIVD 292
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
158-218 1.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4502551    158 RRFKMADKDGDLIATKEEFTAFLHPEEYDY-MKDIVVQETMEDIDKNADGFIDLEEYIGDMY 218
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 160-291 2.58e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   160 FKMADKDGD-LIATKEEFTAF----LHPEEYDymkdivVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTER 234
Cdd:PTZ00184  17 FSLFDKDGDgTITTKELGTVMrslgQNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAF 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4502551   235 EQFvefrDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIV 291
Cdd:PTZ00184  91 KVF----DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 37-299 8.39e-175

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: 484.06  E-value: 8.39e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16228   1 KVHDDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQET 196
Cdd:cd16228  81 DLNEDGLVSWEEYKNATYGYILDDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  197 MEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYE 276
Cdd:cd16228 161 MEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYE 240

                       250       260
                ....*....|....*....|...
gi 4502551  277 SDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16228 241 SDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 39-299 2.78e-148

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: 416.98  E-value: 2.78e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   39 HNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDL 118
Cdd:cd16226   3 DDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  119 NEDGLVSWEEYKNATYGYVLDDP-DPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETM 197
Cdd:cd16226  83 NKDGKLSWEEYKKATYGFLDDEEeDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQETL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  198 EDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYES 277
Cdd:cd16226 163 EDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLIYEA 242

                       250       260
                ....*....|....*....|..
gi 4502551  278 DQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16226 243 DDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 37-299 3.15e-129

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: 368.82  E-value: 3.15e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16229   1 QLHEDNQSFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDDP----DPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIV 192
Cdd:cd16229  81 DLNKDNKISWEEYKQATYGYYLGNPeefqDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  193 VQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARH 272
Cdd:cd16229 161 VLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARH 240

                       250       260
                ....*....|....*....|....*..
gi 4502551  273 LVYESDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16229 241 LVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 37-298 4.93e-128

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: 366.00  E-value: 4.93e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   37 KVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd15899   1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDDPDPD-----DGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDI 191
Cdd:cd15899  81 DPDEDGHVSWDEYKNDTYGSVGDDEENVadnikEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  192 VVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEAR 271
Cdd:cd15899 161 VIKETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEAK 240

                       250       260
                ....*....|....*....|....*..
gi 4502551  272 HLVYESDQNKDGKLTKEEIVDKYDLFV 298
Cdd:cd15899 241 HLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 39-299 3.14e-105

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: 308.06  E-value: 3.14e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   39 HNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKID--GDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGH 116
Cdd:cd16230   3 DDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  117 DLNEDGLVSWEEYKNATYGYVLDD---PDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVV 193
Cdd:cd16230  83 DTDRDGRVGWEELRNATYGHYEPGeefHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIVV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  194 QETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHL 273
Cdd:cd16230 163 AETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHL 242

                       250       260
                ....*....|....*....|....*.
gi 4502551  274 VYESDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16230 243 LHESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 39-297 2.30e-68

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: 214.22  E-value: 2.30e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   39 HNDAQSFDYDHDAFLGAE-EAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHD 117
Cdd:cd16224   3 PNGEHNAEYDKEAFLGGEeDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPEYD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  118 LNEDGLVSWEEYKNATYGYVLD---DPDPDDG--FNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIV 192
Cdd:cd16224  83 KDGDGAVTWDEYNMQMYDRVIDydeDTVLDDEeeESFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTEFV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  193 VQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARH 272
Cdd:cd16224 163 IQEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEALH 242

                       250       260
                ....*....|....*....|....*
gi 4502551  273 LVYESDQNKDGKLTKEEIVDKYDLF 297
Cdd:cd16224 243 LIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 40-299 3.35e-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: 211.02  E-value: 3.35e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   40 NDAQSFDYDHDAFLG-AEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDL 118
Cdd:cd16227   4 DGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  119 NEDGLVSWEEYKNATYGYVLDDPDP---DDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQE 195
Cdd:cd16227  84 DGDGKVTWEEYLADSFGYDDEDNEEmikDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQ 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  196 TMEDIDKNADGFIDLEEYIGDMYSHDgntdEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVY 275
Cdd:cd16227 164 TLRDKDKDNDGFISFQEFLGDRAGHE----DKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFA 239

                       250       260
                ....*....|....*....|....
gi 4502551  276 ESDQNKDGKLTKEEIVDKYDLFVG 299
Cdd:cd16227 240 SADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 46-297 9.53e-41

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 143.21  E-value: 9.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   46 DYDHDAFLGaEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDV---ERQWKGHDLNEDG 122
Cdd:cd16225  10 EFHKEVFLG-NEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVeenEQIFKAVDTDKDG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  123 LVSWEEY---------------KNATYGYVLDDPDPDDgfnyKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDY 187
Cdd:cd16225  89 NVSWEEYrvhfllskgyseeeaEEKIKNNEELKLDEDD----KEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHPEHSRG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  188 MKDIVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNT---DEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYD 264
Cdd:cd16225 165 MLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQqaeDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPRNER 244

                       250       260       270
                ....*....|....*....|....*....|...
gi 4502551  265 HAEAEARHLVYESDQNKDGKLTKEEIVDKYDLF 297
Cdd:cd16225 245 HALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
155-292 2.12e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  155 RDERRFKMADKDGDLIATKEEFTAFLHPeeydymkdiVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEwvkteR 234
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRR---------LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-----A 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4502551  235 EQFVEFRDKNRDGKMDKEETKDWIlpSDYDHAEAEARHLVYESDQNKDGKLTKEEIVD 292
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-212 7.10e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 7.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   67 EESKERLGKIVSKIDGDKDGFVTVDELKdwiKFAQKRWiyedvERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDdg 146
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFE---ALFRRLW-----ATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502551  147 fnykqmmvrDERRFKMADKDGDLIATKEEFTAFLHPEEYDymkDIVVQETMEDIDKNADGFIDLEE 212
Cdd:COG5126  71 ---------ARAAFDLLDTDGDGKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEE 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
36-182 3.08e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 3.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   36 DKVHNDAQSFDYDHDAFLGAEEAKTFdqltpeeSKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKG 115
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEAL-------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502551  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 ...
 157-214 7.61e-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: 42.92  E-value: 7.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4502551  157 ERRFKMADKDGDLIATKEEFTAFLhPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYI 214
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAAL-KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
157-258 1.06e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.40  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551  157 ERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVvQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEwvkterEQ 236
Cdd:COG5126  36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA-RAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD------EL 108

                        90       100
                ....*....|....*....|..
gi 4502551  237 FVEFrDKNRDGKMDKEETKDWI 258
Cdd:COG5126 109 FARL-DTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 193-258 2.09e-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: 41.76  E-value: 2.09e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502551  193 VQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWvkterEQFVEFRDKNRDGKMDKEETKDWI 258
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI-----DEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 45-98 1.75e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.07  E-value: 1.75e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4502551   45 FDYDHDAFLGAEEAKTF-DQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIK 98
Cdd:cd00051   9 FDKDGDGTISADELKAAlKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
158-218 1.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4502551    158 RRFKMADKDGDLIATKEEFTAFLHPEEYDY-MKDIVVQETMEDIDKNADGFIDLEEYIGDMY 218
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 160-291 2.58e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551   160 FKMADKDGD-LIATKEEFTAF----LHPEEYDymkdivVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTER 234
Cdd:PTZ00184  17 FSLFDKDGDgTITTKELGTVMrslgQNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAF 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4502551   235 EQFvefrDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIV 291
Cdd:PTZ00184  91 KVF----DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 242-296 3.08e-03

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 37.41  E-value: 3.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4502551  242 DKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDL 296
Cdd:cd16217  10 DKNKDNKMSFKELKDFLKEINIEVDDDYAEKLFKECDKSKSGFLEGEEIEEFYKL 64
PLN02964 PLN02964
phosphatidylserine decarboxylase
 31-128 4.81e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502551    31 EPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLT-------PEESKERLGK-IVSKIDGDKDGFVTVDELKDWIKFAQK 102
Cdd:PLN02964 131 ELDLFDFVTQEPESACESFDLLDPSSSNKVVGSIFvscsiedPVETERSFARrILAIVDYDEDGQLSFSEFSDLIKAFGN 210

                         90       100
                 ....*....|....*....|....*.
gi 4502551   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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