NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|155372213|ref|NP_001094717|]
View 

dynein regulatory complex protein 8 [Bos taurus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 10-160 6.69e-24

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.98  E-value: 6.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213  10 TEVAVAEFhkkiKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEVEEEEpTGYIRFEKFLPVMTEVLLER 89
Cdd:PTZ00184   6 TEEQIAEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155372213  90 RyrpiPEDILLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMMV 160
Cdd:PTZ00184  81 D----SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 10-160 6.69e-24

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.98  E-value: 6.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213  10 TEVAVAEFhkkiKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEVEEEEpTGYIRFEKFLPVMTEVLLER 89
Cdd:PTZ00184   6 TEEQIAEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155372213  90 RyrpiPEDILLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMMV 160
Cdd:PTZ00184  81 D----SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
EF-hand_7 pfam13499
EF-hand domain pair;
99-159 5.29e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 5.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 155372213   99 LLRAFEVLDPAKRGFLSKDELIKYMT--EEGEPFSQEEMEEMLSaAIDPESN-SIHYKDYITMM 159
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFK-EFDLDKDgRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 99-159 6.81e-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: 39.07  E-value: 6.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155372213  99 LLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMM 159
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
19-145 5.16e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213  19 KKIKEAFEVFDHESNNTVDVREVGTIirslgccpSEGELHDLIAEVEEEePTGYIRFEKFLPVMtevllERRYRPIPEDI 98
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEAL--------FRRLWATLFSEADTD-GDGRISREEFVAGM-----ESLFEATVEPF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 155372213  99 LLRAFEVLDPAKRGFLSKDELIKYMTEEGepFSQEEMEEMLsAAIDP 145
Cdd:COG5126   71 ARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELF-ARLDT 114
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 10-160 6.69e-24

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 90.98  E-value: 6.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213  10 TEVAVAEFhkkiKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEVEEEEpTGYIRFEKFLPVMTEVLLER 89
Cdd:PTZ00184   6 TEEQIAEF----KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG-NGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155372213  90 RyrpiPEDILLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMMV 160
Cdd:PTZ00184  81 D----SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00183 PTZ00183
centrin; Provisional
 5-159 2.87e-16

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 71.26  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213   5 RDRDSTEVAVAEFHKK-IKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEVEEEEpTGYIRFEKFLPVMT 83
Cdd:PTZ00183   2 RKRRSERPGLTEDQKKeIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDG-SGKIDFEEFLDIMT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 155372213  84 EVLLERRyrpiPEDILLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMM 159
Cdd:PTZ00183  81 KKLGERD----PREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
EF-hand_7 pfam13499
EF-hand domain pair;
99-159 5.29e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 5.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 155372213   99 LLRAFEVLDPAKRGFLSKDELIKYMT--EEGEPFSQEEMEEMLSaAIDPESN-SIHYKDYITMM 159
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFK-EFDLDKDgRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 99-159 6.81e-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: 39.07  E-value: 6.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155372213  99 LLRAFEVLDPAKRGFLSKDELIKYMTEEGEPFSQEEMEEMLSAAIDPESNSIHYKDYITMM 159
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 20-83 1.74e-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: 37.91  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 155372213  20 KIKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEVEEEEpTGYIRFEKFLPVMT 83
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
19-145 5.16e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155372213  19 KKIKEAFEVFDHESNNTVDVREVGTIirslgccpSEGELHDLIAEVEEEePTGYIRFEKFLPVMtevllERRYRPIPEDI 98
Cdd:COG5126    5 RKLDRRFDLLDADGDGVLERDDFEAL--------FRRLWATLFSEADTD-GDGRISREEFVAGM-----ESLFEATVEPF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 155372213  99 LLRAFEVLDPAKRGFLSKDELIKYMTEEGepFSQEEMEEMLsAAIDP 145
Cdd:COG5126   71 ARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELF-ARLDT 114
EF-hand_6 pfam13405
EF-hand domain;
20-49 3.03e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 33.69  E-value: 3.03e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 155372213   20 KIKEAFEVFDHESNNTVDVREVGTIIRSLG 49
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 20-64 9.11e-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: 33.48  E-value: 9.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 155372213  20 KIKEAFEVFDHESNNTVDVREVGTIIRSLGCCPSEGELHDLIAEV 64
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH