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Conserved domains on  [gi|157787022|ref|NP_001099447|]
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dynein regulatory complex protein 8 [Rattus norvegicus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 22-134 2.01e-08

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.76  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022  22 KEAFEVFDHESNNTVDVEE---------EEPT----------------GYIRFEKFIPVMTTVLLEKRyrpiAEDVLLRA 76
Cdd:PTZ00184  14 KEAFSLFDKDGDGTITTKElgtvmrslgQNPTeaelqdminevdadgnGTIDFPEFLTLMARKMKDTD----SEEEIKEA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157787022  77 FEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMMV 134
Cdd:PTZ00184  90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 22-134 2.01e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.76  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022  22 KEAFEVFDHESNNTVDVEE---------EEPT----------------GYIRFEKFIPVMTTVLLEKRyrpiAEDVLLRA 76
Cdd:PTZ00184  14 KEAFSLFDKDGDGTITTKElgtvmrslgQNPTeaelqdminevdadgnGTIDFPEFLTLMARKMKDTD----SEEEIKEA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157787022  77 FEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMMV 134
Cdd:PTZ00184  90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 73-133 1.78e-05

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: 39.84  E-value: 1.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157787022  73 LLRAFEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMM 133
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
70-133 5.38e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 5.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157787022   70 EDVLLRAFEVLDPTKRGFLTKDELVKYMT--EEGEPFSQEEMEEMLSaAIDPESN-TINYRDYITMM 133
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFK-EFDLDKDgRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
15-119 1.44e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022  15 AELHKKIKEAFEVFDHESNNTVDVEEEE-----------------PTGYIRFEKFIPVMttvllEKRYRPIAEDVLLRAF 77
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEalfrrlwatlfseadtdGDGRISREEFVAGM-----ESLFEATVEPFARAAF 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157787022  78 EVLDPTKRGFLTKDELVKYMTEEGepFSQEEMEEMLsAAIDP 119
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLTALG--VSEEEADELF-ARLDT 114
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 22-134 2.01e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.76  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022  22 KEAFEVFDHESNNTVDVEE---------EEPT----------------GYIRFEKFIPVMTTVLLEKRyrpiAEDVLLRA 76
Cdd:PTZ00184  14 KEAFSLFDKDGDGTITTKElgtvmrslgQNPTeaelqdminevdadgnGTIDFPEFLTLMARKMKDTD----SEEEIKEA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157787022  77 FEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMMV 134
Cdd:PTZ00184  90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00183 PTZ00183
centrin; Provisional
 5-133 6.58e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.84  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022   5 KDPESTEaivaELHKKIKEAFEVFDHESNNTVDVEE-------------------------EEPTGYIRFEKFIPVMTTV 59
Cdd:PTZ00183   7 ERPGLTE----DQKKEIREAFDLFDTDGSGTIDPKElkvamrslgfepkkeeikqmiadvdKDGSGKIDFEEFLDIMTKK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157787022  60 LLEKRYRpiaeDVLLRAFEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMM 133
Cdd:PTZ00183  83 LGERDPR----EEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 73-133 1.78e-05

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: 39.84  E-value: 1.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157787022  73 LLRAFEVLDPTKRGFLTKDELVKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITMM 133
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
70-133 5.38e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 5.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157787022   70 EDVLLRAFEVLDPTKRGFLTKDELVKYMT--EEGEPFSQEEMEEMLSaAIDPESN-TINYRDYITMM 133
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFK-EFDLDKDgRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
15-119 1.44e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157787022  15 AELHKKIKEAFEVFDHESNNTVDVEEEE-----------------PTGYIRFEKFIPVMttvllEKRYRPIAEDVLLRAF 77
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEalfrrlwatlfseadtdGDGRISREEFVAGM-----ESLFEATVEPFARAAF 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157787022  78 EVLDPTKRGFLTKDELVKYMTEEGepFSQEEMEEMLsAAIDP 119
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLTALG--VSEEEADELF-ARLDT 114
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 69-132 5.43e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 34.43  E-value: 5.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157787022  69 AEDVLLRAFEVLDPTKRGFLTKDEL---VKYMTEEGEPFSQEEMEEMLSAAIDPESNTINYRDYITM 132
Cdd:cd16251   32 SEDQIKKVFQILDKDKSGFIEEEELkyiLKGFSIAGRDLTDEETKALLAAGDTDGDGKIGVEEFATL 98
 
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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