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Conserved domains on  [gi|1767289154|ref|NP_001361954|]
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C3H1-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

zf_CCCH_5 superfamily-containing protein( domain architecture ID 1576644)

zf_CCCH_5 superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 36-74 1.83e-15

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


:

Pssm-ID: 375810  Cd Length: 40  Bit Score: 70.27  E-value: 1.83e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1767289154  36 HYLNEFRVEACPLFKQHQCQQHRPFTCFKWHFANQRRRR 74
Cdd:pfam18384   2 HYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQRRRR 40
 
Name Accession Description Interval E-value
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 36-74 1.83e-15

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 70.27  E-value: 1.83e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1767289154  36 HYLNEFRVEACPLFKQHQCQQHRPFTCFKWHFANQRRRR 74
Cdd:pfam18384   2 HYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQRRRR 40
 
Name Accession Description Interval E-value
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 36-74 1.83e-15

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 70.27  E-value: 1.83e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1767289154  36 HYLNEFRVEACPLFKQHQCQQHRPFTCFKWHFANQRRRR 74
Cdd:pfam18384   2 HYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQRRRR 40
 
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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