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Conserved domains on  [gi|2462514506|ref|XP_054195154|]
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dynein regulatory complex protein 8 isoform X14 [Homo sapiens]

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
 1-122 8.27e-17

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 71.72  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462514506   1 MADEKDREEIivAEFhkkiKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVM 80
Cdd:PTZ00184    1 MADQLTEEQI--AEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLM 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462514506  81 TEILLERKyrpiPEDVLLRAFEVLDSAKRGFLTKDELIKYMT 122
Cdd:PTZ00184   74 ARKMKDTD----SEEEIKEAFKVFDRDGNGFISAAELRHVMT 111
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-122 8.27e-17

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 71.72  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462514506   1 MADEKDREEIivAEFhkkiKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVM 80
Cdd:PTZ00184    1 MADQLTEEQI--AEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLM 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462514506  81 TEILLERKyrpiPEDVLLRAFEVLDSAKRGFLTKDELIKYMT 122
Cdd:PTZ00184   74 ARKMKDTD----SEEEIKEAFKVFDRDGNGFISAAELRHVMT 111
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 18-81 9.08e-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: 38.30  E-value: 9.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462514506  18 KIKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVMT 81
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELMA 63
EF-hand_6 pfam13405
EF-hand domain;
18-47 2.45e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.69  E-value: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462514506  18 KIKEAFEVFDHESNNTVDVREIGTIIRSLG 47
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-122 8.27e-17

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 71.72  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462514506   1 MADEKDREEIivAEFhkkiKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVM 80
Cdd:PTZ00184    1 MADQLTEEQI--AEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLM 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462514506  81 TEILLERKyrpiPEDVLLRAFEVLDSAKRGFLTKDELIKYMT 122
Cdd:PTZ00184   74 ARKMKDTD----SEEEIKEAFKVFDRDGNGFISAAELRHVMT 111
PTZ00183 PTZ00183
centrin; Provisional
 17-123 1.63e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 55.47  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462514506  17 KKIKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVMTEILLERKyrpiPEDV 96
Cdd:PTZ00183   17 KEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDG-SGKIDFEEFLDIMTKKLGERD----PREE 91

                          90       100
                  ....*....|....*....|....*..
gi 2462514506  97 LLRAFEVLDSAKRGFLTKDELIKYMTE 123
Cdd:PTZ00183   92 ILKAFRLFDDDKTGKISLKNLKRVAKE 118
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 18-81 9.08e-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: 38.30  E-value: 9.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462514506  18 KIKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEpTGYIRFEKFLPVMT 81
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELMA 63
EF-hand_6 pfam13405
EF-hand domain;
18-47 2.45e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.69  E-value: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462514506  18 KIKEAFEVFDHESNNTVDVREIGTIIRSLG 47
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 18-62 3.12e-03

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 34.25  E-value: 3.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462514506  18 KIKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEV 62
Cdd:cd22949     4 KFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDALPASM 48
 
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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