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Conserved domains on  [gi|124249218|ref|NP_084119|]
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uncharacterized protein LOC77036 [Mus musculus]

Protein Classification

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

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
66-176 1.16e-09

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  66 DMLMNRVFFVFDKDGDGYVNLEEWIKGLAVFLRGTFEEKMRFCFEVYYLNGDAYISQEKIFDMLKSSlfqHSPEEENEEG 145
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124249218 146 vkdlveisLKKMDYDNDGKISFADFEKAVKE 176
Cdd:COG5126  109 --------FARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
66-176 1.16e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  66 DMLMNRVFFVFDKDGDGYVNLEEWIKGLAVFLRGTFEEKMRFCFEVYYLNGDAYISQEKIFDMLKSSlfqHSPEEENEEG 145
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124249218 146 vkdlveisLKKMDYDNDGKISFADFEKAVKE 176
Cdd:COG5126  109 --------FARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
102-175 1.21e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249218  102 EEKMRFCFEVYYLNGDAYISQEKIFDMLKSSlfqhspeEENEEGVKDLVEISLKKMDYDNDGKISFADFEKAVK 175
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL-------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 71-130 1.81e-04

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: 38.30  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  71 RVFFVFDKDGDGYVNLEEWIKGLAVFLRGTFEEKMRFCFEVYYLNGDAYISQEKIFDMLK 130
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 77-172 5.51e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 38.97  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  77 DKDGDGYVNLEEWIKGLAVFLRGT-FEEKMRFCFEVYYLNGDAYISQEKIFDMLKsslfqHSPEEENEEGVKDLveisLK 155
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMT-----NLGEKLTDEEVDEM----IR 127

                         90
                 ....*....|....*..
gi 124249218 156 KMDYDNDGKISFADFEK 172
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
66-176 1.16e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  66 DMLMNRVFFVFDKDGDGYVNLEEWIKGLAVFLRGTFEEKMRFCFEVYYLNGDAYISQEKIFDMLKSSlfqHSPEEENEEG 145
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124249218 146 vkdlveisLKKMDYDNDGKISFADFEKAVKE 176
Cdd:COG5126  109 --------FARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
102-175 1.21e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.55  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249218  102 EEKMRFCFEVYYLNGDAYISQEKIFDMLKSSlfqhspeEENEEGVKDLVEISLKKMDYDNDGKISFADFEKAVK 175
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL-------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 71-130 1.81e-04

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: 38.30  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  71 RVFFVFDKDGDGYVNLEEWIKGLAVFLRGTFEEKMRFCFEVYYLNGDAYISQEKIFDMLK 130
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-123 1.99e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124249218  53 FRGVLQNIFGMTNDMLMNRVFFVFDKDGDGYVNLEEWIKGLAVFlrGTFEEKMRFCFEVYYLNGDAYISQE 123
Cdd:COG5126   55 FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFE 123
lipocalin_Bla_g_4_Per_a_4 cd19440
major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important ...
 38-179 3.40e-04

major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important cause of asthma. Bla g 4 and Per a 4 are male pheromone transport lipocalins, and both are major allergens. Bla g 4 is produced by Blattella germanica (German cockroach) and has been shown to bind two biogenic amines, tyramine and octopamine which may be its physiological ligands. Per a 4 is produced by Periplaneta americana (American cockroach) and may bind different ligands from Bla g 4 or have different modes for tyramine/octopamine binding. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381215  Cd Length: 148  Bit Score: 39.40  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  38 CPVGKMDNTGLDCNTFRGVLQNIFGMTNDML------MNRvfFVFDKDGDGYVNLEEWIK--GLAVFLRGTFEEKMRFCF 109
Cdd:cd19440    1 CQRGDSLFTGFDYTKYLGVWYEAFRTPNAHEeqykcwIDR--FSLDPEGPIAVTSVAYDSrgKNRVTLTGTVPVSTGNKF 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124249218 110 EVYYLNGDAYISQEKIF--DMLKSSLFQHSPEEENeegVKDLVEISLKKMDYDNDGKisfadfeKAVKEDGL 179
Cdd:cd19440   79 DIDYGDDEAWSSQYWVLgtDYETYAILAGCPAQDS---NKHLIWVQSRDTSFDNATK-------KAVNEVLK 140
PTZ00184 PTZ00184
calmodulin; Provisional
 77-172 5.51e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 38.97  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  77 DKDGDGYVNLEEWIKGLAVFLRGT-FEEKMRFCFEVYYLNGDAYISQEKIFDMLKsslfqHSPEEENEEGVKDLveisLK 155
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMT-----NLGEKLTDEEVDEM----IR 127

                         90
                 ....*....|....*..
gi 124249218 156 KMDYDNDGKISFADFEK 172
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 75-166 2.15e-03

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 38.16  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  75 VFDKDGDGYVNLEEWIKGLAV---FL-RGTFE-------EKMRFCFEVYYLNGDAYISQEKIFDMLKSsLFQHSPEEENE 143
Cdd:cd16179  149 LFDRNKDGKLQLSEMARLLPVkenFLcRPIFKgagkltrEDIDRVFALYDRDNNGTIENEELTGFLKD-LLELVQEDYDE 227

                         90       100
                 ....*....|....*....|...
gi 124249218 144 EGVKDLVEISLKKMDYDNDGKIS 166
Cdd:cd16179  228 QDLEEFKEIILRGWDFNNDGKIS 250
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 76-168 2.72e-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: 37.68  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  76 FDKDGDGYVNLEEWIKGLAvFLRGTFE---EKMRFCFEvYYLNGDAYISQEKIFDMLKSSlfqhspeeeNEEGVKDLVEI 152
Cdd:cd16227  168 KDKDNDGFISFQEFLGDRA-GHEDKEWllvEKDRFDED-YDKDGDGKLDGEEILSWLVPD---------NEEIAEEEVDH 236

                         90
                 ....*....|....*.
gi 124249218 153 SLKKMDYDNDGKISFA 168
Cdd:cd16227  237 LFASADDDHDDRLSFD 252
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 77-170 4.44e-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: 36.91  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  77 DKDGDGYVNLEE----------------WIKGLAVFLRGTFEEKMRFcfEVYYLNGDAYISQEKIfdmlksSLFQHSPEE 140
Cdd:cd16227   82 DEDGDGKVTWEEyladsfgyddedneemIKDSTEDDLKLLEDDKEMF--EAADLNKDGKLDKTEF------SAFQHPEEY 153

                         90       100       110
                 ....*....|....*....|....*....|
gi 124249218 141 ENEEGVkdLVEISLKKMDYDNDGKISFADF 170
Cdd:cd16227  154 PHMHPV--LIEQTLRDKDKDNDGFISFQEF 181
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 77-170 9.56e-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: 36.02  E-value: 9.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249218  77 DKDGDGYVNLEE---WIKGLA-VFLRGTFEEKMRfcfeVYYLNGDAYISQEKIfdmlKSSLFQHSPEEENEEGVKDlvei 152
Cdd:cd16226   45 DKNGDGFVTEEElkdWIKYVQkKYIREDVDRQWK----EYDPNKDGKLSWEEY----KKATYGFLDDEEEDDDLHE---- 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 124249218 153 SLKKM-----------DYDNDGKIS---FADF 170
Cdd:cd16226  113 SYKKMirrderrwkaaDQDGDGKLTkeeFTAF 144
 
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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