NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|73621129|sp|Q6PIL6|]
View 

RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltName: Full=Calsenilin-like protein; AltName: Full=Potassium channel-interacting protein 4

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

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];
128-235 2.81e-18

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 78.30  E-value: 2.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 128 LFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIydmmgkctypvlkeDAPRQ 207
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 73621129 208 HVETFFQKMDKNKDGVVTIDEFIESCQK 235
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_8 pfam13833
EF-hand domain pair;
99-146 2.76e-04

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 2.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73621129    99 PSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFI 146
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFC 48
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
128-235 2.81e-18

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 78.30  E-value: 2.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 128 LFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIydmmgkctypvlkeDAPRQ 207
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 73621129 208 HVETFFQKMDKNKDGVVTIDEFIESCQK 235
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 160-231 2.10e-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: 63.34  E-value: 2.10e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73621129 160 KLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMgkctypvlkedaPRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL------------SEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
159-231 4.41e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.57  E-value: 4.41e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73621129   159 EKLNWAFNLYDINKDGYITKEEMLDIMKAIYdmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE----------EGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 160-188 2.45e-06

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: 43.14  E-value: 2.45e-06
                           10        20
                   ....*....|....*....|....*....
gi 73621129    160 KLNWAFNLYDINKDGYITKEEMLDIMKAI 188
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00184 PTZ00184
calmodulin; Provisional
 106-230 2.60e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.21  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  106 ETFKEIYSQFFPQGDST-----------------TYAHF--LFNAFDTDHNGAVSFEDFIKGLSILLRGT-VQEKLNWAF 165
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTittkelgtvmrslgqnpTEAELqdMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAF 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73621129  166 NLYDINKDGYITKEEMLDIMKAiydmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFI 230
Cdd:PTZ00184  91 KVFDRDGNGFISAAELRHVMTN------------LGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
EF-hand_8 pfam13833
EF-hand domain pair;
99-146 2.76e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 2.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73621129    99 PSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFI 146
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFC 48
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
128-235 2.81e-18

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 78.30  E-value: 2.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 128 LFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIydmmgkctypvlkeDAPRQ 207
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 73621129 208 HVETFFQKMDKNKDGVVTIDEFIESCQK 235
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 160-231 2.10e-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: 63.34  E-value: 2.10e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73621129 160 KLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMgkctypvlkedaPRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL------------SEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 124-186 2.38e-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: 62.95  E-value: 2.38e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73621129 124 YAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMK 186
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
159-231 4.41e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.57  E-value: 4.41e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73621129   159 EKLNWAFNLYDINKDGYITKEEMLDIMKAIYdmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE----------EGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-189 1.41e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  83 TKKELQILYRGFKNEC-------PSGVVNEETFKEIYSQFFPQGDSTTyAHFLFNAFDTDHNGAVSFEDFIKGLSILlrG 155
Cdd:COG5126  23 ERDDFEALFRRLWATLfseadtdGDGRISREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRLLTAL--G 99

                        90       100       110
                ....*....|....*....|....*....|....
gi 73621129 156 TVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIY 189
Cdd:COG5126 100 VSEEEADELFARLDTDGDGKISFEEFVAAVRDYY 133
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
158-229 2.96e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 51.33  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 158 QEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMM---------GKCT-------YPVLKEDAPRQHVETFFQKMDKNKD 221
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLfseadtdgdGRISreefvagMESLFEATVEPFARAAFDLLDTDGD 83


                ....*...
gi 73621129 222 GVVTIDEF 229
Cdd:COG5126  84 GKISADEF 91
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 126-233 1.33e-07

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: 49.83  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 126 HFLFNAFDTDHNGAVSFEDFIKglsilLRGTVQeklNW--AFNLYDINKDGYITKEEMLDIMKaiydMMGkctYPVlked 203
Cdd:cd16180  40 RLMINMFDRDRSGTINFDEFVG-----LWKYIQ---DWrrLFRRFDRDRSGSIDFNELQNALS----SFG---YRL---- 100

                        90       100       110
                ....*....|....*....|....*....|
gi 73621129 204 aPRQHVETFFQKMDKNKDGVVTIDEFIESC 233
Cdd:cd16180 101 -SPQFVQLLVRKFDRRRRGSISFDDFVEAC 129
EF-hand_7 pfam13499
EF-hand domain pair;
123-186 4.90e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 4.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73621129   123 TYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRG--TVQEKLNWAFNLYDINKDGYITKEEMLDIMK 186
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
SPARC_Ca_bdg pfam10591
Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of ...
 130-229 2.08e-06

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: 463162  Cd Length: 111  Bit Score: 45.41  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129   130 NAFDTDHNGAVSFEDFIKGLSIllrgtVQEKLNWAFNLYDINKDGYITKEEmLDIMKAIYDMMGKCTYPvlkedaprqhv 209
Cdd:pfam10591  29 RRERKDHSSTLEKRDESLLYPC-----CKDPLGWMFKRLDTNDDLLLDHEE-LAPIRAPLKPEEHCIKP----------- 91

                          90       100
                  ....*....|....*....|
gi 73621129   210 etFFQKMDKNKDGVVTIDEF 229
Cdd:pfam10591  92 --FFESCDANKDKLISLEEW 109
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 160-188 2.45e-06

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: 43.14  E-value: 2.45e-06
                           10        20
                   ....*....|....*....|....*....
gi 73621129    160 KLNWAFNLYDINKDGYITKEEMLDIMKAI 188
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 159-231 3.13e-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: 3.13e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73621129 159 EKLNWAFNLYDINKDGYITKEEMLDImkaIYDMM--GKCTYPvlkedaprqhvetFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd00252  45 EIAQWEFDNLDNNKDGKLDKRELAPF---RAPLMplEHCARG-------------FFESCDLNKDKKISLQEWLG 103
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 100-230 6.83e-06

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: 44.58  E-value: 6.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 100 SGVVNEETFKEIYSQFFPQGdSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILlrgTVQEKLNWAFNLYDINKDGYITKE 179
Cdd:cd15898  14 DGKLSLKEIKKLLKRLNIRV-SEKELKKLFKEVDTNGDGTLTFDEFEELYKSL---TERPELEPIFKKYAGTNRDYMTLE 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 73621129 180 EMLDIMKAiydmmgkctypVLKEDAPRQHVETFFQKMDKN-KDGVVTIDEFI 230
Cdd:cd15898  90 EFIRFLRE-----------EQGENVSEEECEELIEKYEPErENRQLSFEGFT 130
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 117-192 1.03e-05

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 43.03  E-value: 1.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73621129    117 PQGDSTTYAHfLFNAFDTDHNGAVSFEDfikGLSILLR-GTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMM 192
Cdd:smart00027   5 SPEDKAKYEQ-IFRSLDKNQDGTVTGAQ---AKPILLKsGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKL 77
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 132-231 2.07e-05

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: 44.62  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 132 FDTDHNGAVSFEDFIKGLSILL--RGTVQEKLNWAfNLYDINKDGYITKEEMLDIMkaiydmmgkctYPVLKEDApRQHV 209
Cdd:cd16227 168 KDKDNDGFISFQEFLGDRAGHEdkEWLLVEKDRFD-EDYDKDGDGKLDGEEILSWL-----------VPDNEEIA-EEEV 234

                        90       100
                ....*....|....*....|..
gi 73621129 210 ETFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd16227 235 DHLFASADDDHDDRLSFDEILD 256
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 125-233 2.52e-05

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 43.36  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 125 AHFLFNAFDTDHNGAVSFEDFIKGLSILLrgTVQEklnwAFNLYDINKDGYITKEEmldimkaIYDMMGKCTYPVlkeda 204
Cdd:cd16185  38 AEKLIRMFDRDGNGTIDFEEFAALHQFLS--NMQN----GFEQRDTSRSGRLDANE-------VHEALAASGFQL----- 99

                        90       100
                ....*....|....*....|....*....
gi 73621129 205 PRQHVETFFQKMDKNKDGVVTIDEFIESC 233
Cdd:cd16185 100 DPPAFQALFRKFDPDRGGSLGFDDYIELC 128
PTZ00184 PTZ00184
calmodulin; Provisional
 106-230 2.60e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.21  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  106 ETFKEIYSQFFPQGDST-----------------TYAHF--LFNAFDTDHNGAVSFEDFIKGLSILLRGT-VQEKLNWAF 165
Cdd:PTZ00184  11 AEFKEAFSLFDKDGDGTittkelgtvmrslgqnpTEAELqdMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAF 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73621129  166 NLYDINKDGYITKEEMLDIMKAiydmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFI 230
Cdd:PTZ00184  91 KVFDRDGNGFISAAELRHVMTN------------LGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 160-188 6.71e-05

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: 38.92  E-value: 6.71e-05
                          10        20
                  ....*....|....*....|....*....
gi 73621129   160 KLNWAFNLYDINKDGYITKEEMLDIMKAI 188
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 133-231 1.75e-04

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: 41.66  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 133 DTDHNGAVSFEDFIKglsiLLRGTV--QEKLNWAF-------NLYDINKDGYITKEEMLDIMkaiyDMMgkctypvlKED 203
Cdd:cd15899 170 DKNGDGFISLEEFIS----DPYSADenEEEPEWVKvekerfvELRDKDKDGKLDGEELLSWV----DPS--------NQE 233

                        90       100
                ....*....|....*....|....*...
gi 73621129 204 APRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd15899 234 IALEEAKHLIAESDENKDGKLSPEEILD 261
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 128-192 2.05e-04

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 38.74  E-value: 2.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73621129 128 LFNAFDTDHNGAVSFEdfiKGLSILLR-GTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMM 192
Cdd:cd00052   4 IFRSLDPDGDGLISGD---EARPFLGKsGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_6 pfam13405
EF-hand domain;
160-188 2.67e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.16  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....*....
gi 73621129   160 KLNWAFNLYDINKDGYITKEEMLDIMKAI 188
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EF-hand_8 pfam13833
EF-hand domain pair;
99-146 2.76e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.06  E-value: 2.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73621129    99 PSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFI 146
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFC 48
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 165-230 3.87e-04

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: 40.64  E-value: 3.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 165 FNLYDINKDGYITKEEMLDIMkaiydmmgkctYPvlkEDAPRQ----HVETFfQKMDKNKDGVVTIDEFI 230
Cdd:cd16226 125 WKAADQDGDGKLTKEEFTAFL-----------HP---EEFPHMrdivVQETL-EDIDKNKDGFISLEEYI 179
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 165-229 6.17e-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: 40.36  E-value: 6.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73621129 165 FNLYDINKDGYITKEEMLD-IMKAIYDMMgkctypvlkEDApRQHVETFFQKMDKNKDGVVTIDEF 229
Cdd:cd16225  40 FKKVDVNTDGFLSAEELEDwIMEKTQEHF---------QEA-VEENEQIFKAVDTDKDGNVSWEEY 95
PTZ00183 PTZ00183
centrin; Provisional
 157-247 1.04e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  157 VQEKLNWAFNLYDINKDGYITKEEMLDIMKAiydmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQK- 235
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRS------------LGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKk 82

                         90
                 ....*....|....*...
gi 73621129  236 ------DENIMRSMQLFE 247
Cdd:PTZ00183  83 lgerdpREEILKAFRLFD 100
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 127-177 1.38e-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: 38.28  E-value: 1.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 73621129 127 FLFNAFDTDHNGAVSFEDFIKGLSILLRgtvqekLNWAFNLYDINKDGYIT 177
Cdd:cd16180 107 LLVRKFDRRRRGSISFDDFVEACVTLKR------LTDAFRKYDTNRTGYAT 151
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 128-228 1.79e-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: 38.84  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 128 LFNAFDTDHNGAVSFEDFIK---------GLSILLRGTVQEKlnwafnlyDINKDGYITKEEMLDIMkaiYDMMGKCTYP 198
Cdd:cd16227 127 MFEAADLNKDGKLDKTEFSAfqhpeeyphMHPVLIEQTLRDK--------DKDNDGFISFQEFLGDR---AGHEDKEWLL 195

                        90       100       110
                ....*....|....*....|....*....|
gi 73621129 199 VLKEDaprqhvetFFQKMDKNKDGVVTIDE 228
Cdd:cd16227 196 VEKDR--------FDEDYDKDGDGKLDGEE 217
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 127-189 4.40e-03

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: 36.87  E-value: 4.40e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 127 FLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDiNKDGYITKE-------EMLDIMKAIY 189
Cdd:cd15901  58 WLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRErltqflqDLLQIPDLIG 126
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 133-231 4.60e-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: 37.56  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129 133 DTDHNGAVSFEDFIKglSILLRGTVQEKLNW------AFNLY-DINKDGYITKEEMLD-IMKAIYDmmgkctypvlKEDA 204
Cdd:cd16226 166 DKNKDGFISLEEYIG--DMYRDDDEEEDPDWvksereQFKEFrDKNKDGKMDREEVKDwILPEDYD----------HAEA 233

                        90       100
                ....*....|....*....|....*..
gi 73621129 205 PRQHVetfFQKMDKNKDGVVTIDEFIE 231
Cdd:cd16226 234 EAKHL---IYEADDDKDGKLTKEEILD 257
EFh_SPARC_TICN cd16232
EF-hand, extracellular calcium-binding (EC) motif, found in testicans; Testicans are nervous ...
 158-228 5.41e-03

EF-hand, extracellular calcium-binding (EC) motif, found in testicans; Testicans are nervous system-expressed proteoglycans that play important roles in the regulation of protease activity, as well as in the determination of age at menarche. Testican-1 (TICN1, also termed protein SPOCK) is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It has been implicated in autoimmune disease. It also acts as a regulator of bone morphogenetic protein (BMP) signaling and show critical functions in the nervous system. Testican-2 (TICN2, also termed protein SPOCK2) is an extracellular heparan sulphate proteoglycan highly expressed in brain. It may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. TICN1, but not TICN2, inhibits cathepsin L. TICN1 also inhibits attachment and neurite outgrowth in cultures of N2A neuroblastoma cells, While TICN2 is able to inhibit neurite outgrowth from primary cerebellar cells. Testicans contain an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr orTyr in the +Y position of EF hand 2 in testican-2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity. The substitution of a ligating Asp residue by Phe or Tyr in the +Y position of EF-hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity.


Pssm-ID: 320011  Cd Length: 108  Bit Score: 35.81  E-value: 5.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73621129 158 QEKLNWAFNLYDINKDGYITKEEMLDIMkaiYDMMGKCTYPvlkedaprqhvetFFQKMDKNKDGVVTIDE 228
Cdd:cd16232  45 KPSVGWMFNQLDTNNDLHLSQSELYDLE---LDKYEPCIKP-------------FLDSCDRNKDGKISSDE 99
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 87-177 5.96e-03

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: 36.42  E-value: 5.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  87 LQILYRGFK--NECPSGVVN-EETFKEIYSQFFPQGDSTTYAhfLFNAFDTDHNGAVSFEDFIkGLSILLRGTvqeklNW 163
Cdd:cd16185  65 LSNMQNGFEqrDTSRSGRLDaNEVHEALAASGFQLDPPAFQA--LFRKFDPDRGGSLGFDDYI-ELCIFLASA-----RN 136

                        90
                ....*....|....
gi 73621129 164 AFNLYDINKDGYIT 177
Cdd:cd16185 137 LFQAFDRQRTGRVT 150
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 160-231 6.64e-03

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: 36.11  E-value: 6.64e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73621129 160 KLNWAFNLYDINKDGYITKEEMLDIMKAiydmmgkctypvLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIE 231
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKR------------LNIRVSEKELKKLFKEVDTNGDGTLTFDEFEE 60
EF-hand_7 pfam13499
EF-hand domain pair;
100-150 8.75e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.15  E-value: 8.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 73621129   100 SGVVNEETFKEIYSQFFPQGDSTTYA-HFLFNAFDTDHNGAVSFEDFIKGLS 150
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEEGEPLSDEEvEELFKEFDLDKDGRISFEEFLELYS 67
PLN02964 PLN02964
phosphatidylserine decarboxylase
 169-228 8.92e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 37.15  E-value: 8.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621129  169 DINKDGYITKEEMLDIMKAIYDMMGKctypvlkedaprQHVETFFQKMDKNKDGVVTIDE 228
Cdd:PLN02964 189 DYDEDGQLSFSEFSDLIKAFGNLVAA------------NKKEELFKAADLNGDGVVTIDE 236
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH