NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|26338039|dbj|BAC32705|]
View 

unnamed protein product [Mus musculus]

Protein Classification

EF-hand domain-containing protein (domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein similar to Homo sapiens guanylyl cyclase-activating proteins (GCAP1 and GCAP2), myosin regulatory light chain proteins, (MYL2, MYL5, MYL9, MYL10, and MYL12), and Kv channel-interacting proteins (KChIP1, KChIP2 and KChIP4)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
50-216 6.36e-25

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


:

Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 95.84  E-value: 6.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  50 LEQLEAQTNFTKRELQVLYRGFKNECP--SGVVNEETFKQIYAqFFPHGDASTYAHYLFNAFDTtQTGSVKFEDFVTALS 127
Cdd:COG5126   5 ISDLLTFTQLTEEQIQELKEAFQLFDRdsDGLIDRNELGKILR-SLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039 128 ILL-RGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKaiydmmgkytypVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEF 206
Cdd:COG5126  83 VKLkRGDKEEELREAFKLFDKDHDGYISIGELRRVLK------------SLGERLSDEEVEKLLKEYDEDGDGEIDYEEF 150
                       170
                ....*....|
gi 26338039 207 LESCQEDDNI 216
Cdd:COG5126 151 KKLIKDSPTI 160
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
50-216 6.36e-25

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


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 95.84  E-value: 6.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  50 LEQLEAQTNFTKRELQVLYRGFKNECP--SGVVNEETFKQIYAqFFPHGDASTYAHYLFNAFDTtQTGSVKFEDFVTALS 127
Cdd:COG5126   5 ISDLLTFTQLTEEQIQELKEAFQLFDRdsDGLIDRNELGKILR-SLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039 128 ILL-RGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKaiydmmgkytypVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEF 206
Cdd:COG5126  83 VKLkRGDKEEELREAFKLFDKDHDGYISIGELRRVLK------------SLGERLSDEEVEKLLKEYDEDGDGEIDYEEF 150
                       170
                ....*....|
gi 26338039 207 LESCQEDDNI 216
Cdd:COG5126 151 KKLIKDSPTI 160
EF-hand_7 pfam13499
EF-hand domain pair;
136-211 1.44e-14

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 65.75  E-value: 1.44e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338039   136 EKLRWTFNLYDINKDGYINKEEMMDIVKAIYDmmgkytypvLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQ 211
Cdd:pfam13499   2 EKLKEAFKLLDKDGDGYLDVEELKKLLRKLFE---------EGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
137-208 1.91e-13

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: 62.57  E-value: 1.91e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338039 137 KLRWTFNLYDINKDGYINKEEMMDIVKAIYdmmgkytypvlkEDTPRQHVDVFFQKMDKNKDGIVTLDEFLE 208
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
137-165 2.37e-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: 40.05  E-value: 2.37e-05
                           10        20
                   ....*....|....*....|....*....
gi 26338039    137 KLRWTFNLYDINKDGYINKEEMMDIVKAI 165
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00184 PTZ00184
calmodulin; Provisional
105-206 1.29e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  105 LFNAFDTTQTGSVKFEDFVTALSILLRGT-VHEKLRWTFNLYDINKDGYINKEEMMDIVKAiydmmgkytypvLKEDTPR 183
Cdd:PTZ00184  52 MINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTN------------LGEKLTD 119
                         90       100
                 ....*....|....*....|...
gi 26338039  184 QHVDVFFQKMDKNKDGIVTLDEF 206
Cdd:PTZ00184 120 EEVDEMIREADVDGDGQINYEEF 142
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
50-216 6.36e-25

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


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 95.84  E-value: 6.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  50 LEQLEAQTNFTKRELQVLYRGFKNECP--SGVVNEETFKQIYAqFFPHGDASTYAHYLFNAFDTtQTGSVKFEDFVTALS 127
Cdd:COG5126   5 ISDLLTFTQLTEEQIQELKEAFQLFDRdsDGLIDRNELGKILR-SLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039 128 ILL-RGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKaiydmmgkytypVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEF 206
Cdd:COG5126  83 VKLkRGDKEEELREAFKLFDKDHDGYISIGELRRVLK------------SLGERLSDEEVEKLLKEYDEDGDGEIDYEEF 150
                       170
                ....*....|
gi 26338039 207 LESCQEDDNI 216
Cdd:COG5126 151 KKLIKDSPTI 160
EF-hand_7 pfam13499
EF-hand domain pair;
136-211 1.44e-14

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 65.75  E-value: 1.44e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338039   136 EKLRWTFNLYDINKDGYINKEEMMDIVKAIYDmmgkytypvLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQ 211
Cdd:pfam13499   2 EKLKEAFKLLDKDGDGYLDVEELKKLLRKLFE---------EGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
137-208 1.91e-13

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: 62.57  E-value: 1.91e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338039 137 KLRWTFNLYDINKDGYINKEEMMDIVKAIYdmmgkytypvlkEDTPRQHVDVFFQKMDKNKDGIVTLDEFLE 208
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
101-163 7.27e-09

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: 50.24  E-value: 7.27e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338039 101 YAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVK 163
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
136-208 2.52e-06

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: 44.67  E-value: 2.52e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26338039 136 EKLRWTFNLYDINKDGYINKEEMMDIVkaiYDMMgkytypvlkedtPRQH-VDVFFQKMDKNKDGIVTLDEFLE 208
Cdd:cd00252  45 EIAQWEFDNLDNNKDGKLDKRELAPFR---APLM------------PLEHcARGFFESCDLNKDKKISLQEWLG 103
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
137-165 2.37e-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: 40.05  E-value: 2.37e-05
                           10        20
                   ....*....|....*....|....*....
gi 26338039    137 KLRWTFNLYDINKDGYINKEEMMDIVKAI 165
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
105-166 5.50e-05

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 41.87  E-value: 5.50e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338039 105 LFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDiNKDGYINKE-------EMMDIVKAIY 166
Cdd:cd15901  59 LLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRErltqflqDLLQIPDLIG 126
EF-hand_7 pfam13499
EF-hand domain pair;
103-163 6.02e-05

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 39.95  E-value: 6.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26338039   103 HYLFNAFDTTQTGSVKFEDFVTALSILLRGTVH---EKLRWTFNLYDINKDGYINKEEMMDIVK 163
Cdd:pfam13499   5 KEAFKLLDKDGDGYLDVEELKKLLRKLFEEGEKlsdEEVEELFKEFDLDKDGRISFEEFLELYR 68
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
138-164 4.67e-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: 333786 [Multi-domain]  Cd Length: 27  Bit Score: 36.21  E-value: 4.67e-04
                          10        20
                  ....*....|....*....|....*..
gi 26338039   138 LRWTFNLYDINKDGYINKEEMMDIVKA 164
Cdd:pfam00036   1 LKEIFRLFDKDGDGKIDFEEFKELLKK 27
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
142-207 4.96e-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: 39.99  E-value: 4.96e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338039 142 FNLYDINKDGYINKEEMMdivkaiydmmgKYTYPvlkEDTPRQH---VDVFFQKMDKNKDGIVTLDEFL 207
Cdd:cd16227 128 FEAADLNKDGKLDKTEFS-----------AFQHP---EEYPHMHpvlIEQTLRDKDKDNDGFISFQEFL 182
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
105-210 7.05e-04

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: 38.66  E-value: 7.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039 105 LFNAFDTTQTGSVKFEDFVtalsillrGTVHEKLRWT--FNLYDINKDGYINKEEMmdiVKAIYdMMGkytYPVlkedtP 182
Cdd:cd16180  42 MINMFDRDRSGTINFDEFV--------GLWKYIQDWRrlFRRFDRDRSGSIDFNEL---QNALS-SFG---YRL-----S 101
                        90       100
                ....*....|....*....|....*...
gi 26338039 183 RQHVDVFFQKMDKNKDGIVTLDEFLESC 210
Cdd:cd16180 102 PQFVQLLVRKFDRRRRGSISFDDFVEAC 129
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
105-175 1.00e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477  Cd Length: 96  Bit Score: 37.26  E-value: 1.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26338039    105 LFNAFDTTQTGSVKFEDfvtALSIL----LRGTVHEKLrWtfNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYP 175
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQ---AKPILlksgLPQTLLAKI-W--NLADIDNDGELDKDEFALAMHLIYRKLNGYPIP 83
EF-hand_6 pfam13405
EF-hand domain;
137-165 1.08e-03

EF-hand domain;


Pssm-ID: 338723 [Multi-domain]  Cd Length: 30  Bit Score: 35.25  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*....
gi 26338039   137 KLRWTFNLYDINKDGYINKEEMMDIVKAI 165
Cdd:pfam13405   1 ELREAFKLFDKDGDGYISLEELRKALRSL 29
PTZ00184 PTZ00184
calmodulin; Provisional
105-206 1.29e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.82  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  105 LFNAFDTTQTGSVKFEDFVTALSILLRGT-VHEKLRWTFNLYDINKDGYINKEEMMDIVKAiydmmgkytypvLKEDTPR 183
Cdd:PTZ00184  52 MINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTN------------LGEKLTD 119
                         90       100
                 ....*....|....*....|...
gi 26338039  184 QHVDVFFQKMDKNKDGIVTLDEF 206
Cdd:PTZ00184 120 EEVDEMIREADVDGDGQINYEEF 142
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
105-162 1.86e-03

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: 37.51  E-value: 1.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039 105 LFNAFDTTQTGSVKFEDFVTALSILLRgtvhekLRWTFNLYDINKDGY--INKEEMMDIV 162
Cdd:cd16180 108 LVRKFDRRRRGSISFDDFVEACVTLKR------LTDAFRKYDTNRTGYatISYEDFLTMV 161
SPARC_Ca_bdg pfam10591
Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of ...
140-206 2.33e-03

Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of Secreted Protein Acidic and Rich in Cysteine is responsible for the anti-spreading activity of human urothelial cells. It is rich in alpha-helices. This extracellular calcium-binding domain contains two EF-hands that each coordinates one Ca2+ ion, forming a helix-loop-helix structure that not only drives the conformation of the protein but is also necessary for biological activity. The anti-spreading activity was dependent on the coordination of Ca2+ by a Glu residue at the Z position of EF-hand 2.


Pssm-ID: 313749  Cd Length: 110  Bit Score: 36.53  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338039   140 WTFNLYDINKDGYINKEEMmDIVKAIYDMMGKYTYPvlkedtprqhvdvFFQKMDKNKDGIVTLDEF 206
Cdd:pfam10591  57 WMFHRLDTNDDLLLDQEEL-APIRAPLVPMEHCIKP-------------FFESCDANKDGLISLEEW 109
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
135-207 2.78e-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: 37.56  E-value: 2.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338039 135 HEKLRWtfNLYDINKDGYINKEEMMDIVkaiydmmgkytYPvlkEDTPRQH---VDVFFQKMDKNKDGIVTLDEFL 207
Cdd:cd16226 120 RDERRW--KAADQDGDGKLTKEEFTAFL-----------HP---EEFPHMRdivVQETLEDIDKNKDGFISLEEYI 179
EF-hand_8 pfam13833
EF-hand domain pair;
113-160 3.33e-03

EF-hand domain pair;


Pssm-ID: 316358 [Multi-domain]  Cd Length: 53  Bit Score: 34.48  E-value: 3.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 26338039   113 QTGSVKFEDFVTALSIL-LRGTVHEKLRWTFNLYDINKDGYINKEEMMD 160
Cdd:pfam13833   1 EKGVITREDLRRALALLgLKGLSEEEVDILFREFDTDGDGYISFEEFCV 49
PTZ00183 PTZ00183
centrin; Provisional
134-223 6.80e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 35.82  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338039  134 VHEKLRWTFNLYDINKDGYINKEEMMDIVKAiydmmgkytypvLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESC--- 210
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRS------------LGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMtkk 82
                         90
                 ....*....|....*..
gi 26338039  211 ----QEDDNIMRSLQLF 223
Cdd:PTZ00183  83 lgerDPREEILKAFRLF 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH