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Conserved domains on  [gi|1907141925|ref|XP_036018304|]
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calcineurin B homologous protein 1 isoform X1 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 13310055)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to Oryza sativa calcium-binding protein CML23 that is a potential calcium sensor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-153 4.20e-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: 4.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 153
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 super family cl33171
centrin; Provisional
 18-155 6.02e-08

centrin; Provisional


The actual alignment was detected with superfamily member PTZ00183:

Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 49.30  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  18 KKETGFSHSQITRLYSRFTSLDKgeNGTLREDQVNFRGFMRTLAH-------FRPIEDNEKSKD--VNGPEPLNSRSNKL 88
Cdd:PTZ00183    6 SERPGLTEDQKKEIREAFDLFDT--DGSGTIDPKELKVAMRSLGFepkkeeiKQMIADVDKDGSgkIDFEEFLDIMTKKL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907141925  89 H---------FAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVLEK 155
Cdd:PTZ00183   84 GerdpreeilKAFRLFDDDKTGKISLKNLKRVAKEL-GETITDEELQEM----IDEADRNGDGEISEEEFYRIMKK 154
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-153 4.20e-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: 4.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 153
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-155 7.58e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  27 QITRLYSRFTSLDKGENGTLREDQVN--FRGFMRTL-AHFRPIEDNEKSKD----VNGPEPLNSRSNKLHFAFRLYDLDK 99
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEalFRRLWATLfSEADTDGDGRISREefvaGMESLFEATVEPFARAAFDLLDTDG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907141925 100 DDKISRDELLQVLRMMvgvNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 155
Cdd:COG5126    83 DGKISADEFRRLLTAL---GVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
86-153 5.51e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 5.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907141925  86 NKLHFAFRLYDLDKDDKISRDELLQVLRM-MVGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 153
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEV----EELFKEFDLDKDGRISFEEFLELY 66
PTZ00183 PTZ00183
centrin; Provisional
 18-155 6.02e-08

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 49.30  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  18 KKETGFSHSQITRLYSRFTSLDKgeNGTLREDQVNFRGFMRTLAH-------FRPIEDNEKSKD--VNGPEPLNSRSNKL 88
Cdd:PTZ00183    6 SERPGLTEDQKKEIREAFDLFDT--DGSGTIDPKELKVAMRSLGFepkkeeiKQMIADVDKDGSgkIDFEEFLDIMTKKL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907141925  89 H---------FAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVLEK 155
Cdd:PTZ00183   84 GerdpreeilKAFRLFDDDKTGKISLKNLKRVAKEL-GETITDEELQEM----IDEADRNGDGEISEEEFYRIMKK 154
PTZ00184 PTZ00184
calmodulin; Provisional
 91-153 4.29e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 4.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907141925  91 AFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVL 153
Cdd:PTZ00184   89 AFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEE----VDEMIREADVDGDGQINYEEFVKMM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 87-115 5.55e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.12  E-value: 5.55e-03
                           10        20
                   ....*....|....*....|....*....
gi 1907141925   87 KLHFAFRLYDLDKDDKISRDELLQVLRMM 115
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-153 4.20e-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: 4.20e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 153
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-155 7.58e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  27 QITRLYSRFTSLDKGENGTLREDQVN--FRGFMRTL-AHFRPIEDNEKSKD----VNGPEPLNSRSNKLHFAFRLYDLDK 99
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEalFRRLWATLfSEADTDGDGRISREefvaGMESLFEATVEPFARAAFDLLDTDG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907141925 100 DDKISRDELLQVLRMMvgvNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 155
Cdd:COG5126    83 DGKISADEFRRLLTAL---GVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
86-153 5.51e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 5.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907141925  86 NKLHFAFRLYDLDKDDKISRDELLQVLRM-MVGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 153
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEV----EELFKEFDLDKDGRISFEEFLELY 66
PTZ00183 PTZ00183
centrin; Provisional
 18-155 6.02e-08

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 49.30  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  18 KKETGFSHSQITRLYSRFTSLDKgeNGTLREDQVNFRGFMRTLAH-------FRPIEDNEKSKD--VNGPEPLNSRSNKL 88
Cdd:PTZ00183    6 SERPGLTEDQKKEIREAFDLFDT--DGSGTIDPKELKVAMRSLGFepkkeeiKQMIADVDKDGSgkIDFEEFLDIMTKKL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907141925  89 H---------FAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVLEK 155
Cdd:PTZ00183   84 GerdpreeilKAFRLFDDDKTGKISLKNLKRVAKEL-GETITDEELQEM----IDEADRNGDGEISEEEFYRIMKK 154
PTZ00184 PTZ00184
calmodulin; Provisional
 91-153 4.29e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 4.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907141925  91 AFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVL 153
Cdd:PTZ00184   89 AFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEE----VDEMIREADVDGDGQINYEEFVKMM 146
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 88-156 7.37e-05

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 40.67  E-value: 7.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907141925  88 LHFAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEKV 156
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKL-NVKVDKDY----AKKLFQEADTSGEDVLDEEEFVQFYNRL 65
EF-hand_8 pfam13833
EF-hand domain pair;
99-155 7.22e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 7.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  99 KDDKISRDELLQVLRMMVGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVLEK 155
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDIL----FREFDTDGDGYISFDEFCVLLER 53
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
92-158 8.18e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 8.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  92 FRLYDLDKDDKISRDELLQVLrmmvgVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVLEKVDV 158
Cdd:COG5126    39 FSEADTDGDGRISREEFVAGM-----ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100
EF-hand_6 pfam13405
EF-hand domain;
87-115 1.02e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMM 115
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 92-150 1.19e-03

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: 35.66  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907141925  92 FRLYDLDKDDKISRDELLQVLRMmvgVNISDEQLGSIadrtIQEADQDGDSAISFTEFV 150
Cdd:cd00052     5 FRSLDPDGDGLISGDEARPFLGK---SGLPRSVLAQI----WDLADTDKDGKLDKEEFA 56
PTZ00184 PTZ00184
calmodulin; Provisional
 91-155 1.32e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.43  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907141925  91 AFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVLEK 155
Cdd:PTZ00184   16 AFSLFDKDGDGTITTKELGTVMRSL-GQNPTEAEL----QDMINEVDADGNGTIDFPEFLTLMAR 75
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 87-153 1.41e-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: 36.88  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVL 153
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRL-NIRVSEKELKKL----FKEVDTNGDGTLTFDEFEELY 62
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 64-153 2.44e-03

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


Pssm-ID: 320009  Cd Length: 107  Bit Score: 35.81  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907141925  64 RPIEDNEKSKDVNGPEPL-NSRSNKLHFAFRLYDLDKDDKISRDELLQVLRMMvgvnisdEQLGSIADRTIQEADQDGDS 142
Cdd:cd00252    22 EQDENRSYDNNKRGHDLSgTMRKEIAQWEFDNLDNNKDGKLDKRELAPFRAPL-------MPLEHCARGFFESCDLNKDK 94

                          90
                  ....*....|.
gi 1907141925 143 AISFTEFVKVL 153
Cdd:cd00252    95 KISLQEWLGCF 105
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
87-157 3.65e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 35.92  E-value: 3.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMMVgvnisdeqlgsiaDRTIQEADQDGDSAISFTEFVKVLEKVD 157
Cdd:COG5126     6 KLDRRFDLLDADGDGVLERDDFEALFRRLW-------------ATLFSEADTDGDGRISREEFVAGMESLF 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 87-115 5.55e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.12  E-value: 5.55e-03
                           10        20
                   ....*....|....*....|....*....
gi 1907141925   87 KLHFAFRLYDLDKDDKISRDELLQVLRMM 115
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 87-115 6.05e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 32.76  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907141925  87 KLHFAFRLYDLDKDDKISRDELLQVLRMM 115
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 91-155 6.06e-03

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: 34.81  E-value: 6.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907141925  91 AFRLYDLDKDDKISRDELLQVLRM----MVGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 155
Cdd:cd16252    42 AFQMLDKDKSGFIEWNEIKYILSTvpssMPVAPLSDEE----AEAMIQAADTDGDGRIDFQEFSDMVKK 106
 
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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