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Conserved domains on  [gi|15228545|ref|NP_186990|]
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EF hand calcium-binding protein family [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
 10-134 4.54e-21

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 82.89  E-value: 4.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSSggDVEKELKDAFKLYD 89
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDT--DSEEEIKEAFKVFD 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15228545   90 INCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:PTZ00184  95 RDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 10-134 4.54e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 82.89  E-value: 4.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSSggDVEKELKDAFKLYD 89
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDT--DSEEEIKEAFKVFD 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15228545   90 INCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:PTZ00184  95 RDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-134 3.62e-20

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 80.22  E-value: 3.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALspsipsekLVEMFIQLDTNGDGQVDAAKFASCMDQTAqssGGDVEKELKDAF 85
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRL--------WATLFSEADTDGDGRISREEFVAGMESLF---EATVEPFARAAF 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15228545  86 KLYDINCDGKISANELHVVMTRLGEkcTVESCVGMVQAIDVDGDGYIRF 134
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISF 122
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 80-134 1.76e-11

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: 55.63  E-value: 1.76e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15228545  80 ELKDAFKLYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDF 55
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
8-130 2.13e-09

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 53.53  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545    8 DIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSSGGDVEKELKDA-FK 86
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADDlLS 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15228545   87 LYDINCDGKISANELHVVMTRLGEKCTVEScvgMVQAIDVDGDG 130
Cdd:NF041410 111 ALDTDGDGSISSDELSAGLTSAGSSADSSQ---LFSALDSDGDG 151
EF-hand_7 pfam13499
EF-hand domain pair;
78-134 1.12e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.40  E-value: 1.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228545    78 EKELKDAFKLYDINCDGKISANELHVVMTRLGEKC--TVESCVGMVQAIDVDGDGYIRF 134
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISF 59
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 80-108 3.00e-05

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: 38.51  E-value: 3.00e-05
                           10        20
                   ....*....|....*....|....*....
gi 15228545     80 ELKDAFKLYDINCDGKISANELHVVMTRL 108
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2-66 1.91e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 36.58  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228545    2 NNMSLSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLvemFIQLDTNGDGQVDAAKFASCM 66
Cdd:NF041410 101 STELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAAL 162
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 10-134 4.54e-21

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 82.89  E-value: 4.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSSggDVEKELKDAFKLYD 89
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDT--DSEEEIKEAFKVFD 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15228545   90 INCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:PTZ00184  95 RDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-134 3.62e-20

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 80.22  E-value: 3.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALspsipsekLVEMFIQLDTNGDGQVDAAKFASCMDQTAqssGGDVEKELKDAF 85
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRL--------WATLFSEADTDGDGRISREEFVAGMESLF---EATVEPFARAAF 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15228545  86 KLYDINCDGKISANELHVVMTRLGEkcTVESCVGMVQAIDVDGDGYIRF 134
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISF 122
PTZ00183 PTZ00183
centrin; Provisional
 10-134 1.32e-15

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 68.95  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMdqTAQSSGGDVEKELKDAFKLYD 89
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIM--TKKLGERDPREEILKAFRLFD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15228545   90 INCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:PTZ00183 101 DDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISE 145
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-106 3.49e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 3.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   1 MNNMSLSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMdqtaqSSGGDVEKE 80
Cdd:COG5126  30 LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-----TALGVSEEE 104

                        90       100
                ....*....|....*....|....*.
gi 15228545  81 LKDAFKLYDINCDGKISANELHVVMT 106
Cdd:COG5126 105 ADELFARLDTDGDGKISFEEFVAAVR 130
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
36-132 1.67e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  36 SIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQtaqssggdvekELKDAFKLYDINCDGKISANELHVVMTRLGEKCTVE 115
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRR-----------LWATLFSEADTDGDGRISREEFVAGMESLFEATVEP 69

                        90
                ....*....|....*..
gi 15228545 116 SCVGMVQAIDVDGDGYI 132
Cdd:COG5126  70 FARAAFDLLDTDGDGKI 86
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 80-134 1.76e-11

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: 55.63  E-value: 1.76e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15228545  80 ELKDAFKLYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDF 55
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 6-58 1.77e-10

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: 52.94  E-value: 1.77e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVD 58
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKID 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
6-68 3.25e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 3.25e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALSpsIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQ 68
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
8-130 2.13e-09

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 53.53  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545    8 DIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSSGGDVEKELKDA-FK 86
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADDlLS 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15228545   87 LYDINCDGKISANELHVVMTRLGEKCTVEScvgMVQAIDVDGDG 130
Cdd:NF041410 111 ALDTDGDGSISSDELSAGLTSAGSSADSSQ---LFSALDSDGDG 151
EF-hand_7 pfam13499
EF-hand domain pair;
78-134 1.12e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.40  E-value: 1.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228545    78 EKELKDAFKLYDINCDGKISANELHVVMTRLGEKC--TVESCVGMVQAIDVDGDGYIRF 134
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISF 59
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 10-109 3.32e-07

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: 46.82  E-value: 3.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  10 FERFDTSKDGKISWEEFRdaiHALSPSIPS------EKLVEMFiqlDTNGDGQVDAAKFAScMDQTAQSsggdvekeLKD 83
Cdd:cd16185   6 FRAVDRDRSGSIDVNELQ---KALAGGGLLfslataEKLIRMF---DRDGNGTIDFEEFAA-LHQFLSN--------MQN 70

                        90       100
                ....*....|....*....|....*.
gi 15228545  84 AFKLYDINCDGKISANELHVVMTRLG 109
Cdd:cd16185  71 GFEQRDTSRSGRLDANEVHEALAASG 96
PTZ00184 PTZ00184
calmodulin; Provisional
 80-135 5.15e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.91  E-value: 5.15e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228545   80 ELKDAFKLYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRFV 135
Cdd:PTZ00184  12 EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFP 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 41-106 6.02e-07

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: 43.69  E-value: 6.02e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228545  41 KLVEMFIQLDTNGDGQVDAAKFASCMDQTaqsSGGDVEKELKDAFKLYDINCDGKISANELHVVMT 106
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL---GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PLN02964 PLN02964
phosphatidylserine decarboxylase
 14-63 6.95e-07

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 47.16  E-value: 6.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15228545   14 DTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFA 63
Cdd:PLN02964 189 DYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELA 238
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 5-134 1.11e-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: 45.21  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   5 SLSDIFERFDTSKDGKISWEEFRdaiHALS---PSIPSEKLVEMFIQL-DTNGDGQVDAAKFAScmdqtaqssggdVEKE 80
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQ---RALSngdWTPFSIETVRLMINMfDRDRSGTINFDEFVG------------LWKY 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  81 LKD---AFKLYDINCDGKISANELHVVMTRLGEK---CTVEScvgMVQAIDVDGDGYIRF 134
Cdd:cd16180  66 IQDwrrLFRRFDRDRSGSIDFNELQNALSSFGYRlspQFVQL---LVRKFDRRRRGSISF 122
PTZ00183 PTZ00183
centrin; Provisional
 76-134 1.20e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.07  E-value: 1.20e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228545   76 DVEKELKDAFKLYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:PTZ00183  14 DQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDF 72
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 9-96 1.44e-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: 44.83  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   9 IFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFA-SCMdqtaqssggdVEKELKDAFKL 87
Cdd:cd16180  72 LFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVeACV----------TLKRLTDAFRK 141


                ....*....
gi 15228545  88 YDINCDGKI 96
Cdd:cd16180 142 YDTNRTGYA 150
EF-hand_7 pfam13499
EF-hand domain pair;
8-58 1.52e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 1.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15228545     8 DIFERFDTSKDGKISWEEFRDAIHALSPSIP-SEKLVEMFIQ-LDTNGDGQVD 58
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKeFDLDKDGRIS 58
EF-hand_7 pfam13499
EF-hand domain pair;
40-106 5.68e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 5.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228545    40 EKLVEMFIQLDTNGDGQVDAAKFaSCMDQTAQSSGGDVEKELKDAFKLYDINCDGKISANELHVVMT 106
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEEL-KKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 9-101 1.69e-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: 42.73  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   9 IFERFDTSKDGKISWEEFRD----------AIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMD-----QTAQSS 73
Cdd:cd15902  49 FMEKYDENEDGKIEIRELANilpteenfllLFRREQPLISSVEFMKIWRKYDTDGSGFIEAKELKGFLKdlllkNKKHVS 128

                        90       100
                ....*....|....*....|....*...
gi 15228545  74 GGDVEKELKDAFKLYDINCDGKISANEL 101
Cdd:cd15902 129 PPKLDEYTKLILKEFDANKDGKLELDEM 156
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 6-101 2.68e-05

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: 41.11  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQ-TAQssggdveKELKDA 84
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSlTER-------PELEPI 74

                        90
                ....*....|....*..
gi 15228545  85 FKLYDINCDGKISANEL 101
Cdd:cd15898  75 FKKYAGTNRDYMTLEEF 91
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 80-108 3.00e-05

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: 38.51  E-value: 3.00e-05
                           10        20
                   ....*....|....*....|....*....
gi 15228545     80 ELKDAFKLYDINCDGKISANELHVVMTRL 108
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00183 PTZ00183
centrin; Provisional
 9-69 3.74e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 41.21  E-value: 3.74e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228545    9 IFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQT 69
Cdd:PTZ00183  95 AFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIMKKT 155
EF-hand_6 pfam13405
EF-hand domain;
80-109 4.33e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 4.33e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 15228545    80 ELKDAFKLYDINCDGKISANELHVVMTRLG 109
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_6 pfam13405
EF-hand domain;
6-33 1.22e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.16  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....*...
gi 15228545     6 LSDIFERFDTSKDGKISWEEFRDAIHAL 33
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 55-134 1.35e-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: 38.67  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  55 GQVDAAKFASCMDQTAQSsgGDVEKELKDAFKLYDINCDGKISANELHVVMTRLGEKCTV-----ESCVGMVQAIDVDGD 129
Cdd:cd16252  15 GSFNYSKFFEYMQKFQTS--EQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVaplsdEEAEAMIQAADTDGD 92


                ....*
gi 15228545 130 GYIRF 134
Cdd:cd16252  93 GRIDF 97
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 9-132 1.37e-04

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: 40.03  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   9 IFERFDTSKDGKISWEEFR----DAIHALSPSIPSEKLVEmFIQL-----DTNGDGQVDAAKFASCM------DQTAQSS 73
Cdd:cd15902  95 IWRKYDTDGSGFIEAKELKgflkDLLLKNKKHVSPPKLDE-YTKLilkefDANKDGKLELDEMAKLLpvqenfLLKFQIL 173

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228545  74 GGDVE--KELKDAFKLYDINCDGKISANELHVVMTRLGEKC-------TVESCVGMVQAI-DVDGDGYI 132
Cdd:cd15902 174 GAMDLtkEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNkadidkpDLENFRDAILRAcDKNKDGKI 242
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 10-65 1.39e-04

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: 38.51  E-value: 1.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228545  10 FERFDTSKDGKISWEEFRDAIHALspsIPSEKLVEMFIQL-DTNGDGQVDAAKFASC 65
Cdd:cd00252  51 FDNLDNNKDGKLDKRELAPFRAPL---MPLEHCARGFFEScDLNKDKKISLQEWLGC 104
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 80-108 2.58e-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: 36.22  E-value: 2.58e-04
                          10        20
                  ....*....|....*....|....*....
gi 15228545    80 ELKDAFKLYDINCDGKISANELHVVMTRL 108
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 9-64 4.14e-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: 37.13  E-value: 4.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228545   9 IFERFDTSKDGKISWEEFRDAIHALSPSIP--SEKLVEMFIQL-DTNGDGQVDAAKFAS 64
Cdd:cd16251  39 VFQILDKDKSGFIEEEELKYILKGFSIAGRdlTDEETKALLAAgDTDGDGKIGVEEFAT 97
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 9-130 4.35e-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: 38.82  E-value: 4.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   9 IFERFDTSKDGKISWEEFRdaIHALSPSIPSEKLVEMFIQLDTNGDGQVDaakfascmDQtaqssggDVEKELKDAFKLY 88
Cdd:cd16225  78 IFKAVDTDKDGNVSWEEYR--VHFLLSKGYSEEEAEEKIKNNEELKLDED--------DK-------EVLDRYKDRWSQA 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15228545  89 DINCDGKISANELHVVmtRLGEKCtVESCVGMVQAI----DVDGDG 130
Cdd:cd16225 141 DEPEDGLLDVEEFLSF--RHPEHS-RGMLKNMVKEIlhdlDQDGDE 183
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 8-132 5.15e-04

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, 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 possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 38.32  E-value: 5.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   8 DIFERFDTSKDGKISWEEFRDAIHAL-----------SPSIPSEKLVEMFIQLDTNGDGQVDAAKFAS----------CM 66
Cdd:cd16177   3 EIWKHFDADGNGYIEGKELENFFRELerarrgagvdsKSANFGEKMKEFMQKYDKNADGRIEMAELAQilpteenfllCF 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228545  67 DQTAQSSGgdvekELKDAFKLYDINCDGKISANELHVVMTRLGEKCT--------VESCVGMVQAIDVDGDGYI 132
Cdd:cd16177  83 RQHVGSSS-----EFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANrpydekklQEYTQTILRMFDLNGDGKL 151
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 6-33 8.21e-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: 34.68  E-value: 8.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 15228545     6 LSDIFERFDTSKDGKISWEEFRDAIHAL 33
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 8-130 1.33e-03

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: 37.28  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   8 DIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQ-LDTNGDGQVDAAKFASC----MDQTAQSSGGDVEKELK 82
Cdd:cd16225 135 DRWSQADEPEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHdLDQDGDEKLTLDEFVSLppgtVEEQQAEDDDEWKKERK 214

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15228545  83 DAFK-LYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDG 130
Cdd:cd16225 215 KEFEeVIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDG 263
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 12-111 1.50e-03

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 37.13  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  12 RFDTSKDGKISWEEF----RDAIHALSPSIPSEKLVE----MFIQLDTNGDGQVDAAKFASCMD---------QTAQSSG 74
Cdd:cd16176  93 KYDADHSGFIEADELksflKDLLKKANKPFDESKLEEythtMLKMFDSNNDGKLGLTEMARLLPvqenfllkfQGVKMCG 172

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15228545  75 gdveKELKDAFKLYDINCDGKISANELHVVMTRLGEK 111
Cdd:cd16176 173 ----KEFNKIFELYDQDGNGYIDENELDALLKDLCEK 205
PTZ00184 PTZ00184
calmodulin; Provisional
 10-66 1.53e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 36.66  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228545   10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCM 66
Cdd:PTZ00184  90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
EF-hand_8 pfam13833
EF-hand domain pair;
17-66 1.73e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.60  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15228545    17 KDGKISWEEFRDAIHALS-PSIPSEKLVEMFIQLDTNGDGQVDAAKFASCM 66
Cdd:pfam13833   1 EKGVITREELKRALALLGlKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 10-100 1.89e-03

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: 36.91  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  10 FERFDTSKDGKISWEEFRDAIHA-----LSPSIPSEKLVEMfiqlDTNGDGQVDAAKFascMDQTAQSSGGDVEKELKDA 84
Cdd:cd16227 128 FEAADLNKDGKLDKTEFSAFQHPeeyphMHPVLIEQTLRDK----DKDNDGFISFQEF---LGDRAGHEDKEWLLVEKDR 200

                        90
                ....*....|....*..
gi 15228545  85 FK-LYDINCDGKISANE 100
Cdd:cd16227 201 FDeDYDKDGDGKLDGEE 217
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2-66 1.91e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 36.58  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228545    2 NNMSLSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLvemFIQLDTNGDGQVDAAKFASCM 66
Cdd:NF041410 101 STELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAAL 162
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 6-134 1.99e-03

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: 36.46  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRdaiHALSPSIPS---EKLVEMFIQL-DTNGDGQVDAAKFAScmdqtaqssggdVEKEL 81
Cdd:cd16183   2 LWNVFQRVDKDRSGQISATELQ---QALSNGTWTpfnPETVRLMIGMfDRDNSGTINFQEFAA------------LWKYI 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228545  82 KD---AFKLYDINCDGKISANELHVVMTRLGEKCTVESCVGMVQAIDVDGDGYIRF 134
Cdd:cd16183  67 TDwqnCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAF 122
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 10-52 2.00e-03

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: 36.16  E-value: 2.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15228545  10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTN 52
Cdd:cd16220   6 FEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTD 48
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 10-63 2.04e-03

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: 36.79  E-value: 2.04e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228545  10 FERFDTSKDGKISWEEFRDAIHALSPSIPSEKLV-----EM-------FIQLDTNGDGQVDAAKFA 63
Cdd:cd16226  77 WKEYDPNKDGKLSWEEYKKATYGFLDDEEEDDDLhesykKMirrderrWKAADQDGDGKLTKEEFT 142
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 6-134 2.42e-03

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: 36.65  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDTNGDGQV-----DAAKFASCMDQTAQSSGGDVEKE 80
Cdd:cd15899  37 LGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVswdeyKNDTYGSVGDDEENVADNIKEDE 116

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  81 --------LKDAFKLYDINCDGKISANEL--------HVVMTRLGEKCTVEScvgmvqaIDVDGDGYIRF 134
Cdd:cd15899 117 eykklllkDKKRFEAADQDGDLILTLEEFlaflhpeeSPYMLDFVIKETLED-------LDKNGDGFISL 179
EF-hand_7 pfam13499
EF-hand domain pair;
8-30 2.63e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.54  E-value: 2.63e-03
                          10        20
                  ....*....|....*....|...
gi 15228545     8 DIFERFDTSKDGKISWEEFRDAI 30
Cdd:pfam13499  44 ELFKEFDLDKDGRISFEEFLELY 66
EF-hand_5 pfam13202
EF hand;
8-27 2.91e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.45  E-value: 2.91e-03
                          10        20
                  ....*....|....*....|
gi 15228545     8 DIFERFDTSKDGKISWEEFR 27
Cdd:pfam13202   3 DTFRQIDLNGDGKISKEELR 22
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 6-64 3.40e-03

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: 35.43  E-value: 3.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   6 LSDIFERFDTSKDGKISWEEFRDAIHALSPSIPSEKLVEMFIQLDT-NGDGQVDAAKFAS 64
Cdd:cd16205   2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTdDNQGTLDFEEFCA 61
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 33-105 6.60e-03

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: 35.25  E-value: 6.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228545  33 LSPSIPSEKLVEMFIQLDTNGDGQVDAAKFASCMDQTAQSsggDVEKELKDAFKLYDINCDGKISANELHVVM 105
Cdd:cd16226  28 LTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKK---YIREDVDRQWKEYDPNKDGKLSWEEYKKAT 97
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 1-101 7.90e-03

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: 35.11  E-value: 7.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545   1 MNNMSLSDIFERFDTSKDGKISWEEF------RDAIHALSPSIPSEKlvEMFIQL-DTNGDGQVDAAKFASCMDQTAQss 73
Cdd:cd15899 157 MLDFVIKETLEDLDKNGDGFISLEEFisdpysADENEEEPEWVKVEK--ERFVELrDKDKDGKLDGEELLSWVDPSNQ-- 232

                        90       100
                ....*....|....*....|....*...
gi 15228545  74 gGDVEKELKDAFKLYDINCDGKISANEL 101
Cdd:cd15899 233 -EIALEEAKHLIAESDENKDGKLSPEEI 259
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 10-130 8.13e-03

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: 35.11  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  10 FERFDTSKDGKISWEEFRDAIHALSPSIPSE----------------KLVEMFIQ------------------------- 48
Cdd:cd15899  77 FRAVDPDEDGHVSWDEYKNDTYGSVGDDEENvadnikedeeykklllKDKKRFEAadqdgdliltleeflaflhpeespy 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228545  49 ------------LDTNGDGQVDAAKFASCM--DQTAQSSGGDVEKELKDAFKLYDINCDGKISANELHVVMTRLGEKCTV 114
Cdd:cd15899 157 mldfviketledLDKNGDGFISLEEFISDPysADENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIAL 236

                       170
                ....*....|....*.
gi 15228545 115 ESCVGMVQAIDVDGDG 130
Cdd:cd15899 237 EEAKHLIAESDENKDG 252
 
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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