NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1304111637|pdb|5XOP|E]
View 

Chain E, Calcium-binding protein 1 (EhCBP1), putative

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040236)

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

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-61 1.24e-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: 58.33  E-value: 1.24e-13
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E       1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd00051  1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1-61 1.24e-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: 58.33  E-value: 1.24e-13
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E       1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd00051  1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-65 1.16e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 1.16e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
EF-hand_7 pfam13499
EF-hand domain pair;
5-62 1.98e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 1.98e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
5XOP_E         5 LFKEIDVNGDGAVSYEEVKAFVSKKRAIKN--EQLLQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:pfam13499  7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELY 66
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
3-60 1.63e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 48.14  E-value: 1.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
5XOP_E         3 EALFKEIDVNGDGAVSYEEVK-AFVSKKRAIKNEQLLQLiFKSIDKDGDGFIDFEEFAK 60
Cdd:NF041410  30 KQLFAKLDSDGDGSVSQDELSsALSSKSDDGSLIDLSEL-FSDLDSDGDGSLSSDELAA 87
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2-59 1.07e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.13  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E         2 AEALFKEIDVNGDGAVSYEEVKAFVSKkrAIKNEQLLQLiFKSIDKDGDGFIDFEEFA 59
Cdd:NF041410 105 ADDLLSALDTDGDGSISSDELSAGLTS--AGSSADSSQL-FSALDSDGDGSVSSDELA 159
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 3-59 3.14e-06

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: 40.34  E-value: 3.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
5XOP_E          3 EALFKEIDVNGDGAVSYEEVKAFVSKKRaIKNEQLLQlIFKSIDKDGDGFIDFEEFA 59
Cdd:smart00027 13 EQIFRSLDKNQDGTVTGAQAKPILLKSG-LPQTLLAK-IWNLADIDNDGELDKDEFA 67
PTZ00184 PTZ00184
calmodulin; Provisional
 5-57 4.69e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 35.51  E-value: 4.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
5XOP_E         5 LFKEIDVNGDGAVSYEEVKAFVSKK-RAIKNEQLLQLIFKSIDKDGDGFIDFEE 57
Cdd:PTZ00184  52 MINEVDADGNGTIDFPEFLTLMARKmKDTDSEEEIKEAFKVFDRDGNGFISAAE 105
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1-61 1.24e-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: 58.33  E-value: 1.24e-13
                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E       1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd00051  1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-65 1.16e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.88  E-value: 1.16e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL 98
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-61 6.14e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.95  E-value: 6.14e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAikNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:COG5126  70 FARAAFDLLDTDGDGKISADEFRRLLTALGV--SEEEADELFARLDTDGDGKISFEEFVAA 128
EF-hand_7 pfam13499
EF-hand domain pair;
5-62 1.98e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 1.98e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
5XOP_E         5 LFKEIDVNGDGAVSYEEVKAFVSKKRAIKN--EQLLQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:pfam13499  7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELY 66
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
3-60 1.63e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 48.14  E-value: 1.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
5XOP_E         3 EALFKEIDVNGDGAVSYEEVK-AFVSKKRAIKNEQLLQLiFKSIDKDGDGFIDFEEFAK 60
Cdd:NF041410  30 KQLFAKLDSDGDGSVSQDELSsALSSKSDDGSLIDLSEL-FSDLDSDGDGSLSSDELAA 87
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 5-65 1.71e-07

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


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 44.52  E-value: 1.71e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E        5 LFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:cd16202   5 QFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRL 65
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 3-61 1.75e-07

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes 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 then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 44.55  E-value: 1.75e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVskkRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd16207  41 RELFDKADTDKKGYLNFEEFQEFV---KLLKRRKDIKAIFKQLTKPGSDGLTLEEFLKF 96
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 1-65 4.69e-07

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: 43.43  E-value: 4.69e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL 65
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 3-59 9.79e-07

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 41.05  E-value: 9.79e-07
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|....*..
5XOP_E       3 EALFKEIDVNGDGAVSYEEVKAFVSKKRAikNEQLLQLIFKSIDKDGDGFIDFEEFA 59
Cdd:cd00052  2 DQIFRSLDPDGDGLISGDEARPFLGKSGL--PRSVLAQIWDLADTDKDGKLDKEEFA 56
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
2-59 1.07e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.13  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E         2 AEALFKEIDVNGDGAVSYEEVKAFVSKkrAIKNEQLLQLiFKSIDKDGDGFIDFEEFA 59
Cdd:NF041410 105 ADDLLSALDTDGDGSISSDELSAGLTS--AGSSADSSQL-FSALDSDGDGSVSSDELA 159
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 4-66 1.15e-06

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


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 42.37  E-value: 1.15e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5XOP_E        4 ALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKD-GDGFIDFEEFAKFYGSIA 66
Cdd:cd16205   4 QTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDdNQGTLDFEEFCAFYKMMS 67
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 5-63 1.65e-06

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: 42.96  E-value: 1.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5XOP_E        5 LFKEIDVNGDGAVSYEEVKA---FVSKKRAIKNeqlLQLIFKSIDKDGDGFIDFEEFAKF-YG 63
Cdd:cd16226  40 IVDKIDKNGDGFVTEEELKDwikYVQKKYIRED---VDRQWKEYDPNKDGKLSWEEYKKAtYG 99
EFh_PI-PLCeta2 cd16221
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ...
 6-62 1.88e-06

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


Pssm-ID: 320051 [Multi-domain]  Cd Length: 141  Bit Score: 41.84  E-value: 1.88e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E        6 FKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGD-GFIDFEEFAKFY 62
Cdd:cd16221   6 FDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNqGTLGFEEFCAFY 63
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 3-59 3.14e-06

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: 40.34  E-value: 3.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
5XOP_E          3 EALFKEIDVNGDGAVSYEEVKAFVSKKRaIKNEQLLQlIFKSIDKDGDGFIDFEEFA 59
Cdd:smart00027 13 EQIFRSLDKNQDGTVTGAQAKPILLKSG-LPQTLLAK-IWNLADIDNDGELDKDEFA 67
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 6-58 5.13e-06

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: 41.52  E-value: 5.13e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
5XOP_E        6 FKEIDVNGDGAVSYEEVKAFVSKK------RAIK-NEQllqlIFKSIDKDGDGFIDFEEF 58
Cdd:cd16225  40 FKKVDVNTDGFLSAEELEDWIMEKtqehfqEAVEeNEQ----IFKAVDTDKDGNVSWEEY 95
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3-64 2.38e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 2.38e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFvskkraikNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGS 64
Cdd:COG5126   8 DRRFDLLDADGDGVLERDDFEAL--------FRRLWATLFSEADTDGDGRISREEFVAGMES 61
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 4-66 3.84e-05

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: 38.96  E-value: 3.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5XOP_E        4 ALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEF-AKFYGSIA 66
Cdd:cd15899  39 VIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYkNDTYGSVG 102
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 6-58 7.00e-05

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: 38.33  E-value: 7.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
5XOP_E        6 FKEIDVNGDGAVSYEEVKAFVSKKRAIK-NEQLLQLIFKSIDKDGDGFIDFEEF 58
Cdd:cd16226 125 WKAADQDGDGKLTKEEFTAFLHPEEFPHmRDIVVQETLEDIDKNKDGFISLEEY 178
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 3-64 8.70e-05

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: 38.19  E-value: 8.70e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQ-LLQLIFKSIDKDGDGFIDFEEFAKFYGS 64
Cdd:cd15899 126 KKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDfVIKETLEDLDKNGDGFISLEEFISDPYS 188
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 2-61 1.34e-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: 37.42  E-value: 1.34e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5XOP_E        2 AEALFKEIDVNGDGAVSYEEVKA-------------FVSKKRAIKNEQLL---QLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd15899  73 SKEQFRAVDPDEDGHVSWDEYKNdtygsvgddeenvADNIKEDEEYKKLLlkdKKRFEAADQDGDLILTLEEFLAF 148
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 38-65 1.68e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 1.68e-04
                          10        20
                  ....*....|....*....|....*...
5XOP_E         38 LQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:smart00054  2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 6-62 1.77e-04

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


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 36.93  E-value: 1.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E        6 FKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGD-GFIDFEEFAKFY 62
Cdd:cd16220   6 FEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENqGTLTFEEFCVFY 63
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 3-58 3.41e-04

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 36.40  E-value: 3.41e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQL-IFKSIDKDGDGFIDFEEF 58
Cdd:cd16229 125 ERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVVLeTLEDIDKNGDGFVDEDEY 181
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 12-58 3.53e-04

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 36.49  E-value: 3.53e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
5XOP_E       12 NGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEF 58
Cdd:cd16230  49 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRDGRVGWEEL 95
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 5-58 3.54e-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: 36.14  E-value: 3.54e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        5 LFKEIDVNGDGAVSYEEVKAFVSKKRAIK-NEQLLQLIFKSIDKDGDGFIDFEEF 58
Cdd:cd16227 127 MFEAADLNKDGKLDKTEFSAFQHPEEYPHmHPVLIEQTLRDKDKDNDGFISFQEF 181
EF-hand_5 pfam13202
EF hand;
38-62 4.28e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.45  E-value: 4.28e-04
                         10        20
                 ....*....|....*....|....*
5XOP_E        38 LQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:pfam13202  1 LKDTFRQIDLNGDGKISKEELRRLL 25
PTZ00184 PTZ00184
calmodulin; Provisional
 5-57 4.69e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 35.51  E-value: 4.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
5XOP_E         5 LFKEIDVNGDGAVSYEEVKAFVSKK-RAIKNEQLLQLIFKSIDKDGDGFIDFEE 57
Cdd:PTZ00184  52 MINEVDADGNGTIDFPEFLTLMARKmKDTDSEEEIKEAFKVFDRDGNGFISAAE 105
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 1-61 4.83e-04

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: 35.34  E-value: 4.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKAFVsKKRAIKNEqlLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd15898  37 ELKKLFKEVDTNGDGTLTFDEFEELY-KSLTERPE--LEPIFKKYAGTNRDYMTLEEFIRF 94
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 2-62 6.99e-04

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: 35.27  E-value: 6.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E        2 AEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAALH 62
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 3-62 7.32e-04

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 35.33  E-value: 7.32e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVSKKraiKNEQLLQLI----FKSIDKDGDGFIDFEEF-AKFY 62
Cdd:cd16230 126 ERRFRVADQDGDSMATREELTAFLHPE---EFPHMRDIVvaetLEDLDKNKDGYVQVEEYiADLY 187
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 3-58 7.62e-04

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 35.30  E-value: 7.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVSKKR--AIKNEQLLQLIfKSIDKDGDGFIDFEEF 58
Cdd:cd16228 121 ERRFKMADKDGDLRATKEEFTAFLHPEEydYMKDIVVLETM-EDIDKNGDGFIDLEEY 177
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 38-61 8.04e-04

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 32.76  E-value: 8.04e-04
                         10        20
                 ....*....|....*....|....
5XOP_E        38 LQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:pfam00036  2 LKEIFRLFDKDGDGKIDFEEFKEL 25
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 6-62 8.78e-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: 35.37  E-value: 8.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5XOP_E        6 FKEIDVNGDGAVSYEEV--KAF------VSKKRAIKNEQLLQLI------FKSIDKDGDGFIDFEEFAKFY 62
Cdd:cd16227  78 FEEADEDGDGKVTWEEYlaDSFgyddedNEEMIKDSTEDDLKLLeddkemFEAADLNKDGKLDKTEFSAFQ 148
EFh_PI-PLCdelta3 cd16218
EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, ...
 7-61 9.22e-04

EF-hand motif found in phosphoinositide phospholipase C delta 3 (PI-PLC-delta3); PI-PLC-delta3, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (PLCD3), phospholipase C-delta-3 (PLC-delta-3), is expressed abundantly in brain, skeletal muscle and heart. PI-PLC-delta3 gene expression is down-regulation by cAMP and calcium. PI-PLC-delta3 acts as anchoring of myosin VI on plasma membrane, and further modulates Myosin IV expression and microvilli formation in enterocytes. It negatively regulates RhoA expression, inhibits RhoA/Rho kinase signaling, and plays an essential role in normal neuronal migration by promoting neuronal outgrowth in the developing brain. Moreover, PI-PLC-delta3 is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta3 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta3 contains 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. In addition, PI-PLC-delta3 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, which may be responsible transporting PI-PLC-delta3 from the cell nucleus.


Pssm-ID: 320048 [Multi-domain]  Cd Length: 138  Bit Score: 34.72  E-value: 9.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        7 KEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd16218   7 RRADLNKDGKMSFEEIKDLLQMINIDLNEQYAYQLFKECDRSNDDRLEEHEIEEF 61
PLN02964 PLN02964
phosphatidylserine decarboxylase
 9-59 1.55e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 34.45  E-value: 1.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
5XOP_E         9 IDVNGDGAVSYEE----VKAFVSKKRAIKNEQLlqliFKSIDKDGDGFIDFEEFA 59
Cdd:PLN02964 188 VDYDEDGQLSFSEfsdlIKAFGNLVAANKKEEL----FKAADLNGDGVVTIDELA 238
PTZ00183 PTZ00183
centrin; Provisional
 6-58 1.99e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 33.89  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
5XOP_E         6 FKEIDVNGDGAVSYEEVKA------FVSKKRAIKNeqllqlIFKSIDKDGDGFIDFEEF 58
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVamrslgFEPKKEEIKQ------MIADVDKDGSGKIDFEEF 75
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 1-57 2.51e-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: 33.73  E-value: 2.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
5XOP_E        1 MAEALFKEIDVNGDGAVSYEEVKA---FVSKkraikneqlLQLIFKSIDKDGDGFIDFEE 57
Cdd:cd16185  37 TAEKLIRMFDRDGNGTIDFEEFAAlhqFLSN---------MQNGFEQRDTSRSGRLDANE 87
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2-28 2.54e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 33.61  E-value: 2.54e-03
                        10        20
                ....*....|....*....|....*..
5XOP_E        2 AEALFKEIDVNGDGAVSYEEVKAFVSK 28
Cdd:COG5126 105 ADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
38-61 2.55e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 31.76  E-value: 2.55e-03
                         10        20
                 ....*....|....*....|....
5XOP_E        38 LQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:pfam13405  2 LREAFKLFDKDGDGKISLEELRKA 25
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 2-61 2.55e-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: 33.71  E-value: 2.55e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5XOP_E        2 AEALFKEIDVNGDGAVSYEEVKAFV------SKKRAIKNEQLLQLI------FKSIDKDGDGFIDFEEFAKF 61
Cdd:cd16226  73 VDRQWKEYDPNKDGKLSWEEYKKATygflddEEEDDDLHESYKKMIrrderrWKAADQDGDGKLTKEEFTAF 144
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 2-65 2.76e-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: 33.66  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5XOP_E        2 AEALFKEIDVNGDGAVSYEE-VKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:cd16180   2 LRRIFQAVDRDRSGRISAKElQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFVGLWKYI 66
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 13-61 3.44e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes 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 then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 33.38  E-value: 3.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XOP_E       13 GDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKF 61
Cdd:cd16207  15 GDERLDFEDVEKLCRRLHINCSESYLRELFDKADTDKKGYLNFEEFQEF 63
PPP2R3 cd21339
serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine ...
 2-65 4.39e-03

serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This family includes PP2A regulatory B'' subunits alpha, beta and gamma, encoded by PPP2R3A, PPP2R3B and PPP2R3C, respectively. It also includes subunit delta encoded by PPP2R3D in mouse. These B-family regulatory subunits play various roles including regulation of cytoskeletal assembly, neuronal differentiation, mitogen-activated protein kinase signaling, and apoptosis. Subunits alpha and beta contain two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity.


Pssm-ID: 410336  Cd Length: 259  Bit Score: 33.32  E-value: 4.39e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5XOP_E        2 AEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFYGSI 65
Cdd:cd21339 145 SGAVTRGKTIQKEGEMSYADFVWFLISEEDKKEPTSIEYWFRCLDIDGDGYLSVFELEYFYEEQ 208
EF-hand_5 pfam13202
EF hand;
3-26 6.23e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 30.37  E-value: 6.23e-03
                         10        20
                 ....*....|....*....|....
5XOP_E         3 EALFKEIDVNGDGAVSYEEVKAFV 26
Cdd:pfam13202  2 KDTFRQIDLNGDGKISKEELRRLL 25
EF-hand_8 pfam13833
EF-hand domain pair;
13-62 7.80e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 30.75  E-value: 7.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
5XOP_E        13 GDGAVSYEEVKAFVSKKRAIK-NEQLLQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:pfam13833  1 EKGVITREELKRALALLGLKDlSEDEVDILFREFDTDGDGYISFDEFCVLL 51
PTZ00184 PTZ00184
calmodulin; Provisional
 6-58 8.49e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 32.04  E-value: 8.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
5XOP_E         6 FKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEF 58
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEF 69
PPP2R3A cd21506
serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric ...
 11-62 9.43e-03

serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR130 (also known as protein phosphatase 2A regulatory subunit B'' subunit alpha, PR72, or PPP2R3) that is encoded by the PPP2R3A gene. PR130 and PR72 subunits are derived from the same gene through differential splicing; they harbor specific N-terminal domains of different lengths that are encoded by alternatively spliced exons and have identical C-termini. The common C-terminus contains a two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity. The PR130 subunit has been shown to interact with the LIM domain of lipoma-preferred partner (LPP) through a conserved Zn2+-finger-like motif in the N-terminus of PR130.


Pssm-ID: 410339  Cd Length: 284  Bit Score: 32.21  E-value: 9.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
5XOP_E       11 VNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAKFY 62
Cdd:cd21506 164 VQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDLDGDGVLSMYELEYFY 215
PTZ00184 PTZ00184
calmodulin; Provisional
 6-60 9.90e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 32.04  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
5XOP_E         6 FKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAK 60
Cdd:PTZ00184  90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 3-60 9.92e-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: 32.29  E-value: 9.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
5XOP_E        3 EALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDKDGDGFIDFEEFAK 60
Cdd:cd16227  39 AVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADEDGDGKVTWEEYLA 96
 
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