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Conserved domains on  [gi|392921375|ref|NP_506261|]
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RILP-like protein 1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC_brat-like super family cl29238
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 13-76 1.14e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


The actual alignment was detected with superfamily member cd20482:

Pssm-ID: 475168 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921375  13 LEVQSVKLNEVQNNLRLNRYKAQQDIRQAIAAMIVSLRERERQLIGDLDRAFYKKEGKLVNQMD 76
Cdd:cd20482   19 LRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQQQ 82
 
Name Accession Description Interval E-value
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 13-76 1.14e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921375  13 LEVQSVKLNEVQNNLRLNRYKAQQDIRQAIAAMIVSLRERERQLIGDLDRAFYKKEGKLVNQMD 76
Cdd:cd20482   19 LRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQQQ 82
 
Name Accession Description Interval E-value
CC_brat-like cd20482
coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family ...
 13-76 1.14e-03

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.


Pssm-ID: 467844 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392921375  13 LEVQSVKLNEVQNNLRLNRYKAQQDIRQAIAAMIVSLRERERQLIGDLDRAFYKKEGKLVNQMD 76
Cdd:cd20482   19 LRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQQQ 82
 
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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