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Conserved domains on  [gi|15226592|ref|NP_179170|]
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Calcium-binding EF-hand family protein [Arabidopsis thaliana]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

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
PTZ00184 super family cl33172
calmodulin; Provisional
44-185 8.66e-31

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 109.47  E-value: 8.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   44 SQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFID--AYKRSGGIRSSD 121
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTlmARKMKDTDSEEE 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226592  122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMSSN 185
Cdd:PTZ00184  86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
44-185 8.66e-31

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 109.47  E-value: 8.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   44 SQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFID--AYKRSGGIRSSD 121
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTlmARKMKDTDSEEE 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226592  122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMSSN 185
Cdd:PTZ00184  86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
51-184 1.32e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 80.22  E-value: 1.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  51 MRRVFSRFDLDKDGKISQTEYKVVLRALGQeraiedvpKIFKAVDLDGDGFIDFREFIDAYKRSGGIRS-SDIRNSFWTF 129
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWA--------TLFSEADTDGDGRISREEFVAGMESLFEATVePFARAAFDLL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15226592 130 DLNGDGKISAEEVMSVLWKLGErcSLEDCNRMVRAVDADGDGLVNMEEFIKMMSS 184
Cdd:COG5126  79 DTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
50-112 1.90e-15

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: 67.19  E-value: 1.90e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226592  50 EMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYK 112
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
32-178 1.23e-11

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 60.85  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   32 SSGLSSPGPGGFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAY 111
Cdd:NF041410  10 SSYTSTSSSSTSSARSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226592  112 K--------RSGGIRSSDIrnsFWTFDLNGDGKISAEEVMSVLWKLGercSLEDCNRMVRAVDADGDGLVNMEEF 178
Cdd:NF041410  90 PppppppdqAPSTELADDL---LSALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVSSDEL 158
EF-hand_7 pfam13499
EF-hand domain pair;
120-183 4.58e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.58e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592   120 SDIRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSL--EDCNRMVRAVDADGDGLVNMEEFIKMMS 183
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
89-113 9.09e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 9.09e-04
                           10        20
                   ....*....|....*....|....*
gi 15226592     89 KIFKAVDLDGDGFIDFREFIDAYKR 113
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKA 28
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
126-182 9.83e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 35.43  E-value: 9.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15226592  126 FWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:NF041410  33 FAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA 89
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
44-185 8.66e-31

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 109.47  E-value: 8.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   44 SQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFID--AYKRSGGIRSSD 121
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTlmARKMKDTDSEEE 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226592  122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMSSN 185
Cdd:PTZ00184  86 IKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
PTZ00183 PTZ00183
centrin; Provisional
42-186 5.33e-25

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 94.76  E-value: 5.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   42 GFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGGIRSSD 121
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPR 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226592  122 --IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMSSNN 186
Cdd:PTZ00183  90 eeILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
51-184 1.32e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 80.22  E-value: 1.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  51 MRRVFSRFDLDKDGKISQTEYKVVLRALGQeraiedvpKIFKAVDLDGDGFIDFREFIDAYKRSGGIRS-SDIRNSFWTF 129
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWA--------TLFSEADTDGDGRISREEFVAGMESLFEATVePFARAAFDLL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15226592 130 DLNGDGKISAEEVMSVLWKLGErcSLEDCNRMVRAVDADGDGLVNMEEFIKMMSS 184
Cdd:COG5126  79 DTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAAVRD 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
20-144 2.38e-16

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 71.75  E-value: 2.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  20 RKPSRMFSR-DRQSSGLSSPGPggFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDG 98
Cdd:COG5126   5 RKLDRRFDLlDADGDGVLERDD--FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDG 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15226592  99 DGFIDFREFIDAYkRSGGIRSSDIRNSFWTFDLNGDGKISAEEVMS 144
Cdd:COG5126  83 DGKISADEFRRLL-TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
50-112 1.90e-15

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: 67.19  E-value: 1.90e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226592  50 EMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYK 112
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
121-183 5.23e-15

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: 66.03  E-value: 5.23e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226592 121 DIRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMS 183
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
50-181 8.48e-14

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: 65.70  E-value: 8.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  50 EMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKrsggiRSSDIRNSFWTF 129
Cdd:cd16185   1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAALHQ-----FLSNMQNGFEQR 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15226592 130 DLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKM 181
Cdd:cd16185  76 DTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIEL 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-110 2.50e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.66  E-value: 2.50e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226592  42 GFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERaiEDVPKIFKAVDLDGDGFIDFREFIDA 110
Cdd:COG5126  62 LFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSE--EEADELFARLDTDGDGKISFEEFVAA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-187 4.94e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 4.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  83 AIEDVPKIFKAVDLDGDGFIDFREFIDAYKRsggirssDIRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMV 162
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRR-------LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAF 75
                        90       100
                ....*....|....*....|....*
gi 15226592 163 RAVDADGDGLVNMEEFIKMMSSNNV 187
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLLTALGV 100
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
32-178 1.23e-11

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 60.85  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   32 SSGLSSPGPGGFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAY 111
Cdd:NF041410  10 SSYTSTSSSSTSSARSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226592  112 K--------RSGGIRSSDIrnsFWTFDLNGDGKISAEEVMSVLWKLGercSLEDCNRMVRAVDADGDGLVNMEEF 178
Cdd:NF041410  90 PppppppdqAPSTELADDL---LSALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVSSDEL 158
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
43-186 2.55e-11

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: 60.68  E-value: 2.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  43 FSQPSVNEMRR----VFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGGIR 118
Cdd:cd16226  25 FDQLTPEESKErlgiIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSWEEYKKATYGFLDDE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 119 SSDIRNSF------------W-TFDLNGDGKISAEEVMSVLWKlgercslEDCNRMVRAV--------DADGDGLVNMEE 177
Cdd:cd16226 105 EEDDDLHEsykkmirrderrWkAADQDGDGKLTKEEFTAFLHP-------EEFPHMRDIVvqetlediDKNKDGFISLEE 177

                ....*....
gi 15226592 178 FIKMMSSNN 186
Cdd:cd16226 178 YIGDMYRDD 186
EF-hand_7 pfam13499
EF-hand domain pair;
120-183 4.58e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.58e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592   120 SDIRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSL--EDCNRMVRAVDADGDGLVNMEEFIKMMS 183
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
EF-hand_7 pfam13499
EF-hand domain pair;
49-112 1.37e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.57  E-value: 1.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592    49 NEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAI--EDVPKIFKAVDLDGDGFIDFREFIDAYK 112
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
46-184 2.15e-10

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: 57.84  E-value: 2.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  46 PSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREF-IDAYKRSGGIRSSDIRN 124
Cdd:cd15899  32 ESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYkNDTYGSVGDDEENVADN 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 125 S----------------FWTFDLNGDGKISAEEVMSVLWKlgercslEDCNRMVRAV--------DADGDGLVNMEEFIK 180
Cdd:cd15899 112 IkedeeykklllkdkkrFEAADQDGDLILTLEEFLAFLHP-------EESPYMLDFViketledlDKNGDGFISLEEFIS 184

                ....
gi 15226592 181 MMSS 184
Cdd:cd15899 185 DPYS 188
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
51-184 2.01e-09

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 53.44  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  51 MRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSggIRSSDIRNSFWTFD 130
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL--TERPELEPIFKKYA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592 131 LNGDGKISAEEVMSVLWK-LGERCSLEDCNRMVRAVDADG-DGLVNMEEFIKMMSS 184
Cdd:cd15898  80 GTNRDYMTLEEFIRFLREeQGENVSEEECEELIEKYEPEReNRQLSFEGFTNFLLS 135
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
52-177 1.18e-08

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: 52.97  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  52 RRVFSRFDLDKDGKISQTEYKVVLR---------ALGQErAIEDVpkifkavDLDGDGFIDFREFI-DAYKRSGGIRSSD 121
Cdd:cd16226 122 ERRWKAADQDGDGKLTKEEFTAFLHpeefphmrdIVVQE-TLEDI-------DKNKDGFISLEEYIgDMYRDDDEEEDPD 193
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226592 122 I----RNSFWTF-DLNGDGKISAEEV----MSVLWKLGErcslEDCNRMVRAVDADGDGLVNMEE 177
Cdd:cd16226 194 WvkseREQFKEFrDKNKDGKMDREEVkdwiLPEDYDHAE----AEAKHLIYEADDDKDGKLTKEE 254
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
55-186 1.17e-07

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: 50.01  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  55 FSRFDLDKDGKISQTEYkvVLRALGQE----------------RAIEDVPKIFKAVDLDGDGFIDFREFI-----DAYKR 113
Cdd:cd16227  78 FEEADEDGDGKVTWEEY--LADSFGYDdedneemikdsteddlKLLEDDKEMFEAADLNKDGKLDKTEFSafqhpEEYPH 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 114 SGGIrssDIRNSFWTFDLNGDGKISAEEVmsvlwkLGERCSLEDC-------NRMVRAVDADGDGLVNMEEFIKMMSSNN 186
Cdd:cd16227 156 MHPV---LIEQTLRDKDKDNDGFISFQEF------LGDRAGHEDKewllvekDRFDEDYDKDGDGKLDGEEILSWLVPDN 226
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
54-179 2.66e-07

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 48.02  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  54 VFSRFDLDKDGKISQTEYKVVLRAlGQERAI--EDVPKIFKAVDLDGDGFIDFREFIDAYKrsggiRSSDIRNSFWTFDL 131
Cdd:cd16183   5 VFQRVDKDRSGQISATELQQALSN-GTWTPFnpETVRLMIGMFDRDNSGTINFQEFAALWK-----YITDWQNCFRSFDR 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15226592 132 NGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFI 179
Cdd:cd16183  79 DNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFI 126
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
52-186 8.07e-07

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 46.45  E-value: 8.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  52 RRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSggIRSSDIRNSFWTFDL 131
Cdd:cd16202   3 KDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRL--TKRPEIEELFKKYSG 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226592 132 NGDgKISAEEVMSVLWKLGER--CSLEDCNRMVRAVDADGD----GLVNMEEFIKMMSSNN 186
Cdd:cd16202  81 DDE-ALTVEELRRFLQEEQKVkdVTLEWAEQLIETYEPSEDlkaqGLMSLDGFTLFLLSPD 140
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
43-181 8.26e-07

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: 47.68  E-value: 8.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  43 FSQPSVNEMRR----VFSRFDLDKDGKISQTEYKVVLRALGQE---RAIEDVPKIFKAVDLDGDGFIDFREF-------- 107
Cdd:cd16225  24 FEEDSEPKKRKklkeIFKKVDVNTDGFLSAEELEDWIMEKTQEhfqEAVEENEQIFKAVDTDKDGNVSWEEYrvhfllsk 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 108 ------IDAYKRSGGIRSSD---------IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLED-CNRMVRAVDADGDG 171
Cdd:cd16225 104 gyseeeAEEKIKNNEELKLDeddkevldrYKDRWSQADEPEDGLLDVEEFLSFRHPEHSRGMLKNmVKEILHDLDQDGDE 183
                       170
                ....*....|
gi 15226592 172 LVNMEEFIKM 181
Cdd:cd16225 184 KLTLDEFVSL 193
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
50-182 1.02e-06

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 46.37  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  50 EMRRVFSRFDLDKDGKISQTEYKVVLR-ALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRsggIRssDIRNSFWT 128
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALSnGDWTPFSIETVRLMINMFDRDRSGTINFDEFVGLWKY---IQ--DWRRLFRR 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15226592 129 FDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:cd16180  76 FDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEAC 129
EF-hand_7 pfam13499
EF-hand domain pair;
90-146 2.22e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592    90 IFKAVDLDGDGFIDFREFIDAYKRSGG---IRSSDIRNSFWTFDLNGDGKISAEEVMSVL 146
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEgepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
87-180 2.87e-06

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: 46.28  E-value: 2.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  87 VPKIFKAVDLDGDGFIDFREFI-DAYKRSGGIRSS----DIRNSFWTF-DLNGDGKISAEEVMSVLWKLGERCSLEDCNR 160
Cdd:cd15899 162 IKETLEDLDKNGDGFISLEEFIsDPYSADENEEEPewvkVEKERFVELrDKDKDGKLDGEELLSWVDPSNQEIALEEAKH 241
                        90       100
                ....*....|....*....|
gi 15226592 161 MVRAVDADGDGLVNMEEFIK 180
Cdd:cd15899 242 LIAESDENKDGKLSPEEILD 261
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
57-179 4.27e-06

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: 45.51  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  57 RFDLDKDGKISQTEYKVvLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGGIRS-SDIRNSFWTFDLNGDG 135
Cdd:cd15899   8 NSDYDHEAFLGKEEAEE-FDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAmEESKEQFRAVDPDEDG 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 136 KISAEEVMSVLWKLG----------------ERCSLEDCNRMVRAVDADGDGLVNMEEFI 179
Cdd:cd15899  87 HVSWDEYKNDTYGSVgddeenvadnikedeeYKKLLLKDKKRFEAADQDGDLILTLEEFL 146
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
53-182 5.10e-06

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 45.42  E-value: 5.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  53 RVFSRFDLDKDGKISQTEYKVVLRAL-----GQERAIEDVPKIFK----AVDLDGDGFIDFRE----------FIDAYKR 113
Cdd:cd15902   3 EVWMHFDADGNGYIEGKELDSFLRELlkalnGKDKTDDEVAEKKKefmeKYDENEDGKIEIRElanilpteenFLLLFRR 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226592 114 SGGIRSSDIRNSFWT-FDLNGDGKISAEEVMSVLWKL--------GERCSLEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:cd15902  83 EQPLISSVEFMKIWRkYDTDGSGFIEAKELKGFLKDLllknkkhvSPPKLDEYTKLILKEFDANKDGKLELDEMAKLL 160
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
55-110 8.44e-06

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: 41.82  E-value: 8.44e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592  55 FSRFDLDKDGKISQTEYKVVLRALGQERAIedVPKIFKAVDLDGDGFIDFREFIDA 110
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPFLGKSGLPRSV--LAQIWDLADTDKDGKLDKEEFAIA 58
PLN02964 PLN02964
phosphatidylserine decarboxylase
52-106 1.11e-05

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15226592   52 RRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFRE 106
Cdd:PLN02964 182 RRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDE 236
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
45-186 1.56e-05

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: 44.16  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  45 QPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRaLGQERAI-EDVPKIFKAVDLDGDGFIDFREFIDA------------- 110
Cdd:cd16228  31 EESKERLGKIVGKIDEDKDGFVTEDELKAWIK-FAQKRWIyEDVERQWKGHDLNEDGLVSWEEYKNAtygyilddpdpdd 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 111 ---YKRsggIRSSDIRNsFWTFDLNGDGKISAEEVMSVLWKlgercslEDCNRM--------VRAVDADGDGLVNMEEFI 179
Cdd:cd16228 110 gfnYKQ---MMVRDERR-FKMADKDGDLRATKEEFTAFLHP-------EEYDYMkdivvletMEDIDKNGDGFIDLEEYI 178

                ....*..
gi 15226592 180 KMMSSNN 186
Cdd:cd16228 179 GDMYSQD 185
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
35-146 1.85e-05

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 43.88  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  35 LSSPGPGGFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVL----------RALGQERAIEDVPKIFKAVDLDGDGFIDF 104
Cdd:cd15902  30 KALNGKDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILpteenflllfRREQPLISSVEFMKIWRKYDTDGSGFIEA 109
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15226592 105 RE----FIDAYKRSGGIRSSD-----IRNSFWTFDLNGDGKISAEEVMSVL 146
Cdd:cd15902 110 KElkgfLKDLLLKNKKHVSPPkldeyTKLILKEFDANKDGKLELDEMAKLL 160
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
24-145 2.54e-05

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 42.52  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  24 RMFSRDRqSSGLsspGPGGFSQ--PSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGF 101
Cdd:cd16180  44 NMFDRDR-SGTI---NFDEFVGlwKYIQDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGS 119
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15226592 102 IDFREFIDA---YKRsggirssdIRNSFWTFDLNGDG--KISAEEVMSV 145
Cdd:cd16180 120 ISFDDFVEAcvtLKR--------LTDAFRKYDTNRTGyaTISYEDFLTM 160
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
47-184 2.92e-05

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: 43.33  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  47 SVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDA---------------- 110
Cdd:cd16229  33 SKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDYDLNKDNKISWEEYKQAtygyylgnpeefqdat 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 111 ----YKRsggIRSSDIRNsFWTFDLNGDGKISAEEVMSVLW-----KLGERCSLEdcnrMVRAVDADGDGLVNMEEFIKM 181
Cdd:cd16229 113 dqfsFKK---MLPRDERR-FKAADLDGDLAATREEFTAFLHpeefeHMKDIVVLE----TLEDIDKNGDGFVDEDEYIAD 184

                ...
gi 15226592 182 MSS 184
Cdd:cd16229 185 MFS 187
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
29-138 3.30e-05

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: 42.20  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  29 DRQSSG----------LSSPGPGgFSQPSVNEMRRVFsrfDLDKDGKISQTEYKVVLRALGQERAIedvpkiFKAVDLDG 98
Cdd:cd16185  10 DRDRSGsidvnelqkaLAGGGLL-FSLATAEKLIRMF---DRDGNGTIDFEEFAALHQFLSNMQNG------FEQRDTSR 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226592  99 DGFIDFRE----------------FIDAYK-----RSGGIRSSD----------IRNSFWTFDLNGDGKIS 138
Cdd:cd16185  80 SGRLDANEvhealaasgfqldppaFQALFRkfdpdRGGSLGFDDyielciflasARNLFQAFDRQRTGRVT 150
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
51-113 3.90e-05

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 40.98  E-value: 3.90e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226592  51 MRRVFSRFDLDKDGKISQTEYKVVLRALGQERAI-----EDVPKIFKAVDLDGDGFIDFREFIDAYKR 113
Cdd:cd16252  39 IRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVaplsdEEAEAMIQAADTDGDGRIDFQEFSDMVKK 106
EF-hand_8 pfam13833
EF-hand domain pair;
133-182 5.02e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 39.61  E-value: 5.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15226592   133 GDGKISAEEVMSVLWKLGER-CSLEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:pfam13833   1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
42-107 9.49e-05

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 39.82  E-value: 9.49e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226592  42 GFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRAL---GQERAIEDVPKIFKAVDLDGDGFIDFREF 107
Cdd:cd16251  27 GLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLAAGDTDGDGKIGVEEF 95
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
36-109 9.69e-05

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 40.05  E-value: 9.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226592  36 SSPGPGGFSQPSVNEMRRV----FSRFDLDKDGKISQTEYKVVLRAL-GQERAIEdvpKIFKAVDLDGDGFIDFREFID 109
Cdd:cd00252  28 SYDNNKRGHDLSGTMRKEIaqweFDNLDNNKDGKLDKRELAPFRAPLmPLEHCAR---GFFESCDLNKDKKISLQEWLG 103
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
77-180 1.22e-04

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: 41.53  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  77 ALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSggIRSSDIRNS---FWTFDLNGDGKISAEEVM---------- 143
Cdd:cd16227  28 ELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRS--FKMLDEEEAnerFEEADEDGDGKVTWEEYLadsfgydded 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15226592 144 -SVLWKLG---ERCSLEDCNRMVRAVDADGDGLVNMEEFIK 180
Cdd:cd16227 106 nEEMIKDStedDLKLLEDDKEMFEAADLNKDGKLDKTEFSA 146
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
53-179 1.26e-04

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: 41.50  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  53 RVFSRFDLDKDGKISQTEYKVVL--------RALGQERAIEDVpkifkavDLDGDGFIDFREFI-DAYKRSGGIRS---- 119
Cdd:cd16230 127 RRFRVADQDGDSMATREELTAFLhpeefphmRDIVVAETLEDL-------DKNKDGYVQVEEYIaDLYSGEPGEEEpawv 199
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226592 120 SDIRNSFWTF-DLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFI 179
Cdd:cd16230 200 QTERQQFRQFrDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEIL 260
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
122-183 1.39e-04

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 40.06  E-value: 1.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592 122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDAD-GDGLVNMEEFI---KMMS 183
Cdd:cd16205   2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDdNQGTLDFEEFCafyKMMS 67
EF-hand_8 pfam13833
EF-hand domain pair;
62-113 1.68e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 1.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15226592    62 KDGKISQTEYKVVLRALGQERAIED-VPKIFKAVDLDGDGFIDFREFIDAYKR 113
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDeVDILFREFDTDGDGYISFDEFCVLLER 53
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
81-182 2.30e-04

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: 40.49  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  81 ERAIEDVpkiFKAVDLDGDGFIDFREFIDAYKRSGGIRSSDI-----RNSFWT-FDLNGDGKISAEEVMSVLWKLGERCS 154
Cdd:cd16224 160 EFVIQEA---LEEHDKDGDGFISLEEFLGDYRKDPTANEDPEwiiveKDRFVNdYDKDNDGKLDPQELLPWVVPNNYGIA 236
                        90       100
                ....*....|....*....|....*...
gi 15226592 155 LEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:cd16224 237 QEEALHLIDEMDLNGDGRLSEEEILENQ 264
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
58-178 2.41e-04

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: 40.70  E-value: 2.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  58 FDLDKDGKISQTEYKVvLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGG-IRSSDIRNSFWTFDLNGDGK 136
Cdd:cd16228   9 FDYDHDAFLGAEEAKT-FDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKrWIYEDVERQWKGHDLNEDGL 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15226592 137 ISAEEVMSVLWKLgercSLEDCN---------------RMVRAVDADGDGLVNMEEF 178
Cdd:cd16228  88 VSWEEYKNATYGY----ILDDPDpddgfnykqmmvrdeRRFKMADKDGDLRATKEEF 140
EF-hand_6 pfam13405
EF-hand domain;
50-79 2.71e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.77  E-value: 2.71e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 15226592    50 EMRRVFSRFDLDKDGKISQTEYKVVLRALG 79
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
89-113 3.17e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.61  E-value: 3.17e-04
                          10        20
                  ....*....|....*....|....*
gi 15226592    89 KIFKAVDLDGDGFIDFREFIDAYKR 113
Cdd:pfam00036   4 EIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
43-186 3.20e-04

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: 40.11  E-value: 3.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  43 FSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLralgQERAI---EDVP-----------------KIFKAVDLDGDGFI 102
Cdd:cd16224  66 FRHYALEDAKQQFPEYDKDGDGAVTWDEYNMQM----YDRVIdydEDTVlddeeeesfrqlhlkdkKRFDKANTDGGPGL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 103 DFREFIDAYKRSGGIRSSD--IRNSFWTFDLNGDGKISAEEVM-----------SVLWKLGERcsledcNRMVRAVDADG 169
Cdd:cd16224 142 NLTEFIAFEHPEEVDYMTEfvIQEALEEHDKDGDGFISLEEFLgdyrkdptaneDPEWIIVEK------DRFVNDYDKDN 215
                       170
                ....*....|....*..
gi 15226592 170 DGLVNMEEFIKMMSSNN 186
Cdd:cd16224 216 DGKLDPQELLPWVVPNN 232
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
52-180 3.86e-04

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: 39.98  E-value: 3.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  52 RRVFSRFDLDKDGKISQTEY---------KVVLRALGQEraiedvpkIFKAVDLDGDGFIDFREFI-------------- 108
Cdd:cd16225 134 KDRWSQADEPEDGLLDVEEFlsfrhpehsRGMLKNMVKE--------ILHDLDQDGDEKLTLDEFVslppgtveeqqaed 205
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226592 109 -DAYKRSggiRSSDIRNsfwTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIK 180
Cdd:cd16225 206 dDEWKKE---RKKEFEE---VIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILK 272
PRK12309 PRK12309
transaldolase;
79-146 4.07e-04

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 40.10  E-value: 4.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592   79 GQERAIEDVPKIFKAVDLDGDGFIDFREFI--DAYkrsggirssdirnsFWTFDLNGDGKISAEEVMSVL 146
Cdd:PRK12309 328 GGEAFTHAAQEIFRLYDLDGDGFITREEWLgsDAV--------------FDALDLNHDGKITPEEMRAGL 383
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
104-184 4.66e-04

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 37.90  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592 104 FREFIDAYKRSGGiRSSDIRNSFWTFDLNGDGKISAEEVMSVLWKLGER-----CSLEDCNRMVRAVDADGDGLVNMEEF 178
Cdd:cd16252  22 FFEYMQKFQTSEQ-QEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAADTDGDGRIDFQEF 100

                ....*.
gi 15226592 179 IKMMSS 184
Cdd:cd16252 101 SDMVKK 106
EF-hand_8 pfam13833
EF-hand domain pair;
98-146 5.31e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 5.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15226592    98 GDGFIDFREFIDAYKRSG--GIRSSDIRNSFWTFDLNGDGKISAEEVMSVL 146
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
84-181 5.98e-04

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 37.51  E-value: 5.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  84 IEDVPKIFKAVDLdgdgfIDFREFIDAYKRSGGiRSSDIRNSFWTFDLNGDGKISAEEVMSVLWKL---GERCSLEDCNR 160
Cdd:cd16251   4 IEKAPSAFRAHGS-----FNYKKFFEHVGLKQK-SEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKA 77
                        90       100
                ....*....|....*....|.
gi 15226592 161 MVRAVDADGDGLVNMEEFIKM 181
Cdd:cd16251  78 LLAAGDTDGDGKIGVEEFATL 98
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
41-181 6.21e-04

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 38.74  E-value: 6.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  41 GGFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERaiedvpKIFKAVDLDGDGFIDFREFIDAYKRSGGIRSS 120
Cdd:cd16182  34 PKFDGFSLETCRSLIALMDTNGSGRLDLEEFKTLWSDLKKWQ------AIFKKFDTDRSGTLSSYELRKALESAGFHLSN 107
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15226592 121 DIRNSFWTFDLNGDGKISAEEVMSVLwklgerCSLEDCNRMVRAVDADGDG--LVNMEEFIKM 181
Cdd:cd16182 108 KVLQALVLRYADSTGRITFEDFVSCL------VRLKTAFETFSALDKKNEGviPLTLEEWLLL 164
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
122-183 8.90e-04

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 38.08  E-value: 8.90e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592 122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGD-GLVNMEEFI---KMMS 183
Cdd:cd16220   2 VKQTFEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENqGTLTFEEFCvfyKMMS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
89-113 9.09e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 9.09e-04
                           10        20
                   ....*....|....*....|....*
gi 15226592     89 KIFKAVDLDGDGFIDFREFIDAYKR 113
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
122-180 9.21e-04

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 37.98  E-value: 9.21e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15226592 122 IRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIK 180
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
78-178 9.85e-04

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: 38.71  E-value: 9.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  78 LGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGGIRSSDIRNSFWT-FDLNGDGKISAEEVMSVLWK--LGERCS 154
Cdd:cd16229  28 LTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKdYDLNKDNKISWEEYKQATYGyyLGNPEE 107
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15226592 155 LEDCN-------------RMVRAVDADGDGLVNMEEF 178
Cdd:cd16229 108 FQDATdqfsfkkmlprdeRRFKAADLDGDLAATREEF 144
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
42-108 1.34e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 36.72  E-value: 1.34e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  42 GFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRAL---GQERAIEDVPKIFKAVDLDGDGFIDFREFI 108
Cdd:cd16254  27 GLKKKSADDVKKVFHILDKDKSGFIEEDELKFVLKGFspdGRDLSDKETKALLAAGDKDGDGKIGIDEFA 96
EFh_PI-PLCeta2 cd16221
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ...
123-184 1.57e-03

EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320051 [Multi-domain]  Cd Length: 141  Bit Score: 37.22  E-value: 1.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592 123 RNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGD-GLVNMEEFI---KMMSS 184
Cdd:cd16221   3 KQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNqGTLGFEEFCafyKMMST 68
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
50-78 1.64e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*....
gi 15226592     50 EMRRVFSRFDLDKDGKISQTEYKVVLRAL 78
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
50-78 2.08e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 2.08e-03
                          10        20
                  ....*....|....*....|....*....
gi 15226592    50 EMRRVFSRFDLDKDGKISQTEYKVVLRAL 78
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
91-147 2.72e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 35.81  E-value: 2.72e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15226592  91 FKAVDLDGDGFIDFREfIDAYKRSGGIRSSDIRNSFWTFDLNGDGKISAEEVMSVLW 147
Cdd:cd00252  51 FDNLDNNKDGKLDKRE-LAPFRAPLMPLEHCARGFFESCDLNKDKKISLQEWLGCFG 106
PLN02964 PLN02964
phosphatidylserine decarboxylase
89-152 3.01e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 37.53  E-value: 3.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226592   89 KIFKAVDLDGDGFIDFREFIDAYKRSGGIRSSD-IRNSFWTFDLNGDGKISAEEVMSVLWKLGER 152
Cdd:PLN02964 183 RILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANkKEELFKAADLNGDGVVTIDELAALLALQQEQ 247
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
50-177 5.43e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 36.56  E-value: 5.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  50 EMRRVFSRFDLDKDGKISQTEYKVVLRAL--------GQERAIEDVPKIFKAVDLDGDGFIDFRE----------FIDAY 111
Cdd:cd15902  91 EFMKIWRKYDTDGSGFIEAKELKGFLKDLllknkkhvSPPKLDEYTKLILKEFDANKDGKLELDEmakllpvqenFLLKF 170
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226592 112 KRSGGI--RSSDIRNSFWTFDLNGDGKISAEEVMSVLWKLGERC-------SLEDCNRMV-RAVDADGDGLVNMEE 177
Cdd:cd15902 171 QILGAMdlTKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNkadidkpDLENFRDAIlRACDKNKDGKIQKTE 246
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
121-149 6.50e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.14  E-value: 6.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 15226592   121 DIRNSFWTFDLNGDGKISAEEVMSVLWKL 149
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
133-178 8.02e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 35.48  E-value: 8.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15226592 133 GDGKISAEEVMSVLWKLGER-----CSLEDCNRMVRAVDADGDGLVNMEEF 178
Cdd:cd15897  12 DDGEISATELQQALSNVGWThfdlgFSLETCRSMIAMMDRDHSGKLNFSEF 62
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
42-107 8.63e-03

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 34.46  E-value: 8.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226592  42 GFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQE-RAIEDV-PKIF-KAVDLDGDGFIDFREF 107
Cdd:cd16253  27 GLSKKSPADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGaRVLSDKeTKNFlAAGDSDGDGKIGVDEF 95
EFh_PEF_CAPN3 cd16190
Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), ...
134-178 9.19e-03

Calcium-activated neutral; CAPN3, also termed calcium-activated neutral proteinase 3 (CANP 3), or calpain L3, or calpain p94, or muscle-specific calcium-activated neutral protease 3, or new calpain 1 (nCL-1), is a calpain large subunit that is mainly expressed in skeletal muscle, or lens. The skeletal muscle-specific CAPN3 are pathologically associated with limb girdle muscular dystrophy type 2A (LGMD2A). Its autolytic activity can be positively regulated by calmodulin (CaM), a known transducer of the calcium signal. CAPN3 is also involved in human melanoma tumorigenesis and progression. It impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells. Moreover, it plays an important role in sarcomere remodeling and mitochondrial protein turnover. Furthermore, the phosphorylated skeletal muscle-specific CAPN3 acts as a myofibril structural component and may participate in myofibril-based signaling pathways. In the eye, the lens-specific CAPN3, together with CAPN2, is responsible for proteolytic cleavages of alpha and beta-crystallin. Overactivated alpha and beta-crystallin can lead to cataract formation. CAPN3 exists as a homodimer, rather than a heterodimer with the calpain small subunit. It may also form heterodimers with other calpain large subunits. CAPN3 contains a long N-terminal region, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. Ca2+ binding at EF5 of the CAPN3 PEF domain is a distinct feature not observed in other calpain isoforms.


Pssm-ID: 320065 [Multi-domain]  Cd Length: 169  Bit Score: 35.22  E-value: 9.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15226592 134 DGKISAEEVMSVLWKL--------GERCSLEDCNRMVRAVDADGDGLVNMEEF 178
Cdd:cd16190  13 DMEISADELRSVLNRVvkkhkdlkTEGFTLESCRSMIALMDTDGSGKLNLQEF 65
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
53-142 9.28e-03

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: 35.63  E-value: 9.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226592  53 RVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDV-PKIFKAVDLDGDGFIDFREFI-DAYKRSGGIRSSDI----RNSF 126
Cdd:cd16229 126 RRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVvLETLEDIDKNGDGFVDEDEYIaDMFSHEEGGPEPDWvkteREQF 205
                        90
                ....*....|....*..
gi 15226592 127 WTF-DLNGDGKISAEEV 142
Cdd:cd16229 206 SDFrDLNKDGKMDKEEI 222
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
126-182 9.83e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 35.43  E-value: 9.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15226592  126 FWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMM 182
Cdd:NF041410  33 FAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA 89
 
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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