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Conserved domains on  [gi|74736866|sp|Q6NVV0|]
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PUTATIVE PSEUDOGENE: RecName: Full=Putative makorin-5; AltName: Full=Makorin ring finger protein pseudogene 6; AltName: Full=Makorin ring finger protein pseudogene 9; AltName: Full=Putative RING finger protein 65

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MKRN1_C super family cl24397
E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ...
1-33 1.84e-10

E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ubiquitin-protein ligase makorin-1, or MKRN1, a family of eukaryotic putative ribonucleoproteins with a distinctive array of zinc-finger motifs. MKRN1 plays an important role in modulating the homeostasis of telomere-length through a dynamic balance involving the stability of the protein hTERT. MKRN1 has been shown to be a a transcriptional co-regulator and an E3 ligase. It functions simultaneously as a differentially negative regulator of p53 and p21, preferentially leading cells to p53-dependent apoptosis by suppressing p21. The exact function of the C-terminal region has not been determined.


The actual alignment was detected with superfamily member pfam15815:

Pssm-ID: 464890  Cd Length: 87  Bit Score: 49.64  E-value: 1.84e-10
                         10        20        30
                 ....*....|....*....|....*....|...
gi 74736866    1 MLLAAVGDDELTDSEDESDLFHEELEDFYDLDL 33
Cdd:pfam15815 55 KLLLALRDDELTDSEDEWDLLHYELEEYFDLDL 87
 
Name Accession Description Interval E-value
MKRN1_C pfam15815
E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ...
1-33 1.84e-10

E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ubiquitin-protein ligase makorin-1, or MKRN1, a family of eukaryotic putative ribonucleoproteins with a distinctive array of zinc-finger motifs. MKRN1 plays an important role in modulating the homeostasis of telomere-length through a dynamic balance involving the stability of the protein hTERT. MKRN1 has been shown to be a a transcriptional co-regulator and an E3 ligase. It functions simultaneously as a differentially negative regulator of p53 and p21, preferentially leading cells to p53-dependent apoptosis by suppressing p21. The exact function of the C-terminal region has not been determined.


Pssm-ID: 464890  Cd Length: 87  Bit Score: 49.64  E-value: 1.84e-10
                         10        20        30
                 ....*....|....*....|....*....|...
gi 74736866    1 MLLAAVGDDELTDSEDESDLFHEELEDFYDLDL 33
Cdd:pfam15815 55 KLLLALRDDELTDSEDEWDLLHYELEEYFDLDL 87
 
Name Accession Description Interval E-value
MKRN1_C pfam15815
E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ...
1-33 1.84e-10

E3 ubiquitin-protein ligase makorin, C-terminal; MKRN1_C is the very C-terminus of E3 ubiquitin-protein ligase makorin-1, or MKRN1, a family of eukaryotic putative ribonucleoproteins with a distinctive array of zinc-finger motifs. MKRN1 plays an important role in modulating the homeostasis of telomere-length through a dynamic balance involving the stability of the protein hTERT. MKRN1 has been shown to be a a transcriptional co-regulator and an E3 ligase. It functions simultaneously as a differentially negative regulator of p53 and p21, preferentially leading cells to p53-dependent apoptosis by suppressing p21. The exact function of the C-terminal region has not been determined.


Pssm-ID: 464890  Cd Length: 87  Bit Score: 49.64  E-value: 1.84e-10
                         10        20        30
                 ....*....|....*....|....*....|...
gi 74736866    1 MLLAAVGDDELTDSEDESDLFHEELEDFYDLDL 33
Cdd:pfam15815 55 KLLLALRDDELTDSEDEWDLLHYELEEYFDLDL 87
 
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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