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Conserved domains on  [gi|256223190|ref|NP_001074281|]
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calcium and integrin-binding family member 3 isoform 2 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12144783)

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

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List of domain hits

Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
80-147 4.13e-09

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.33  E-value: 4.13e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256223190   80 KAYYAFKIYDFNNDNYICAWDLEQTVTRLTRG-ELSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMIL 147
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLSDEEV----EELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
80-147 4.13e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.33  E-value: 4.13e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256223190   80 KAYYAFKIYDFNNDNYICAWDLEQTVTRLTRG-ELSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMIL 147
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLSDEEV----EELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
30-148 5.80e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  30 ELIGSMPELKDNPFRQRIAQVFSQ---DGDGHMTLENFLDMFSvmSEMAPRDLKAYY--AFKIYDFNNDNYICAWDLEQT 104
Cdd:PTZ00184  32 ELGTVMRSLGQNPTEAELQDMINEvdaDGNGTIDFPEFLTLMA--RKMKDTDSEEEIkeAFKVFDRDGNGFISAAELRHV 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 256223190 105 VTRLtrGE-LSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMILR 148
Cdd:PTZ00184 110 MTNL--GEkLTDEEV----DEMIREADVDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
84-146 2.28e-07

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.62  E-value: 2.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256223190  84 AFKIYDFNNDNYICAWDLEQTVTRLTRGELSAEevtlvCEKVLDEADGDQDGRLSLEDFQNMI 146
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEE-----IDEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
54-142 1.24e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  54 DGDGHMTLENFL-DMFSVMSEMAPRDLKAyyAFKIYDFNNDNYIcawDLEQTVTRLTRGELSAEEVtlvcEKVLDEADGD 132
Cdd:COG5126   45 DGDGRISREEFVaGMESLFEATVEPFARA--AFDLLDTDGDGKI---SADEFRRLLTALGVSEEEA----DELFARLDTD 115
                         90
                 ....*....|
gi 256223190 133 QDGRLSLEDF 142
Cdd:COG5126  116 GDGKISFEEF 125
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
80-147 4.13e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.33  E-value: 4.13e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256223190   80 KAYYAFKIYDFNNDNYICAWDLEQTVTRLTRG-ELSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMIL 147
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLSDEEV----EELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
30-148 5.80e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  30 ELIGSMPELKDNPFRQRIAQVFSQ---DGDGHMTLENFLDMFSvmSEMAPRDLKAYY--AFKIYDFNNDNYICAWDLEQT 104
Cdd:PTZ00184  32 ELGTVMRSLGQNPTEAELQDMINEvdaDGNGTIDFPEFLTLMA--RKMKDTDSEEEIkeAFKVFDRDGNGFISAAELRHV 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 256223190 105 VTRLtrGE-LSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMILR 148
Cdd:PTZ00184 110 MTNL--GEkLTDEEV----DEMIREADVDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
84-146 2.28e-07

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.62  E-value: 2.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256223190  84 AFKIYDFNNDNYICAWDLEQTVTRLTRGELSAEevtlvCEKVLDEADGDQDGRLSLEDFQNMI 146
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEE-----IDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
28-150 3.56e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 44.29  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  28 PYELIGSMPELKDNPFRQRIAQVFSQ---DGDGHMTLENFLDMFSV-MSEMAPRD--LKAyyaFKIYDFNNDNYICAWDL 101
Cdd:PTZ00183  36 PKELKVAMRSLGFEPKKEEIKQMIADvdkDGSGKIDFEEFLDIMTKkLGERDPREeiLKA---FRLFDDDKTGKISLKNL 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 256223190 102 EQTVTRLtrGE-LSAEEVtlvcEKVLDEADGDQDGRLSLEDFQNMILRAP 150
Cdd:PTZ00183 113 KRVAKEL--GEtITDEEL----QEMIDEADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
54-142 1.24e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  54 DGDGHMTLENFL-DMFSVMSEMAPRDLKAyyAFKIYDFNNDNYIcawDLEQTVTRLTRGELSAEEVtlvcEKVLDEADGD 132
Cdd:COG5126   45 DGDGRISREEFVaGMESLFEATVEPFARA--AFDLLDTDGDGKI---SADEFRRLLTALGVSEEEA----DELFARLDTD 115
                         90
                 ....*....|
gi 256223190 133 QDGRLSLEDF 142
Cdd:COG5126  116 GDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
44-146 7.98e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  44 RQRIAQVFS---QDGDGHMTLENFLDMFSVMSEMAprdlkayyaFKIYDFNNDNYIcawDLEQTVTRLTRGELSAEEVTL 120
Cdd:COG5126    4 RRKLDRRFDlldADGDGVLERDDFEALFRRLWATL---------FSEADTDGDGRI---SREEFVAGMESLFEATVEPFA 71
                         90       100
                 ....*....|....*....|....*.
gi 256223190 121 vcEKVLDEADGDQDGRLSLEDFQNMI 146
Cdd:COG5126   72 --RAAFDLLDTDGDGKISADEFRRLL 95
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
30-151 9.09e-04

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: 37.36  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256223190  30 ELIGSMPELKDNPFRQRIAQVF----SQDGDGHMTLENFLDMFSVMSemAPRDLkaYYAFKIYDfNNDNYICAWDLeqtv 105
Cdd:cd16205   21 EILQLMHKLNVNLPRRKVRQMFkeadTDDNQGTLDFEEFCAFYKMMS--TRREL--YLLLLSYS-NKKDYLTLEDL---- 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 256223190 106 TRLTRGELSAEEVTL-----VCEKVLDEADGDQDGRLSLEDFQNMiLRAPD 151
Cdd:cd16205   92 ARFLEVEQKMTNVTLeycldIIEKFEPSEENKKNGLLGIDGFTNY-MRSPA 141
PRK00977 PRK00977
exodeoxyribonuclease VII small subunit; Provisional
100-143 5.31e-03

exodeoxyribonuclease VII small subunit; Provisional


Pssm-ID: 179195  Cd Length: 80  Bit Score: 34.11  E-value: 5.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256223190 100 DLEQTVTRLTRGELSAEE--------VTLV--CEKVLDEA-------DGDQDGRLSLEDFQ 143
Cdd:PRK00977  18 ELEEIVTRLESGDLPLEEslaafergVALArqCQKKLQQAeqrveklLDEDGKEASLEPFD 78
 
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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