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Conserved domains on  [gi|121583697|ref|NP_001073554|]
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paralemmin-3 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYO6_MIU_linker super family cl46503
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
16-59 1.78e-07

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


The actual alignment was detected with superfamily member pfam03285:

Pssm-ID: 480843  Cd Length: 301  Bit Score: 52.44  E-value: 1.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 121583697   16 AEKRRVQEEQERARREMEDERLRLQQLKRKSLRDQWLMEGPPTS 59
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSS 44
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
16-59 1.78e-07

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 52.44  E-value: 1.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 121583697   16 AEKRRVQEEQERARREMEDERLRLQQLKRKSLRDQWLMEGPPTS 59
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSS 44
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
16-59 1.78e-07

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 52.44  E-value: 1.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 121583697   16 AEKRRVQEEQERARREMEDERLRLQQLKRKSLRDQWLMEGPPTS 59
Cdd:pfam03285   1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSS 44
 
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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